Journal Menu
- About this Journal
- Abstracting and Indexing
- Aims and Scope
- Article Processing Charges
- Articles in Press
- Author Guidelines
- Bibliographic Information
- Citations to this Journal
- Contact Information
- Editorial Board
- Editorial Workflow
- Free eTOC Alerts
- Publication Ethics
- Reviewers Acknowledgment
- Submit a Manuscript
- Subscription Information
- Table of Contents
Journal of Oncology
Volume 2012 (2012), Article ID 125278, 25 pages
doi:10.1155/2012/125278
Review Article
Integrin-Mediated Cell-Matrix Interaction in Physiological and Pathological Blood Vessel Formation
Center for Molecular Medicine, Department of Vascular Matrix Biology, Excellence Cluster Cardio-Pulmonary System, J. W. Goethe University Hospital, Theodor-Stern-Kai 7, Building 9 b, 60590 Frankfurt, Germany
Received 25 May 2011; Accepted 15 July 2011
Academic Editor: Debabrata Mukhopadhyay
Copyright © 2012 Stephan Niland and Johannes A. Eble. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Linked References
- K. Kinzler and B. Vogelstein, The Genetic Basis of Human Cancer, McGraw-Hill, Medical Pub. Division, 2nd edition, 2002.
- G. Bergers and L. E. Benjamin, “Tumorigenesis and the angiogenic switch,” Nature Reviews Cancer, vol. 3, no. 6, pp. 401–410, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Rheingold, A. Neugut, and A. Meadows, “Secondary cancers: incidence, risk factors, and management,” in Holland-Frei Cancer Medicine, D. Kufe, R. Pollock, and R. Weichselbaum, Eds., p. 2399, B. C. Decker, Hamilton, Ont, Canada, 2003.
- D. Hanahan and R. A. Weinberg, “The hallmarks of cancer,” Cell, vol. 100, no. 1, pp. 57–70, 2000. View at Scopus
- D. Hanahan and R. A. Weinberg, “Hallmarks of cancer: the next generation,” Cell, vol. 144, no. 5, pp. 646–674, 2011.
- D. Hanahan and J. Folkman, “Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis,” Cell, vol. 86, no. 3, pp. 353–364, 1996. View at Publisher · View at Google Scholar · View at Scopus
- B. Nico, E. Crivellato, D. Guidolin et al., “Intussusceptive microvascular growth in human glioma,” Clinical and Experimental Medicine, vol. 10, no. 2, pp. 93–98, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. J. Avraamides, B. Garmy-Susini, and J. A. Varner, “Integrins in angiogenesis and lymphangiogenesis,” Nature Reviews Cancer, vol. 8, no. 8, pp. 604–617, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. Rathinam and S. K. Alahari, “Important role of integrins in the cancer biology,” Cancer and Metastasis Reviews, vol. 29, no. 1, pp. 223–237, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. Alghisi and C. Rüegg, “Vascular integrins in tumor angiogenesis: mediators and therapeutic targets,” Endothelium, vol. 13, no. 2, pp. 113–135, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Rüegg and G. C. Alghisi, “Vascular integrins: therapeutic and imaging targets of tumor angiogenesis,” Recent Results in Cancer Research, vol. 180, pp. 83–101, 2010. View at Publisher · View at Google Scholar · View at Scopus
- J. S. Desgrosellier and D. A. Cheresh, “Integrins in cancer: biological implications and therapeutic opportunities,” Nature Reviews Cancer, vol. 10, no. 1, pp. 9–22, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S.-H. Kim, J. Turnbull, and S. Guimond, “Extracellular matrix and cell signalling: the dynamic cooperation of integrin, proteoglycan and growth factor receptor,” Journal of Endocrinology, vol. 209, no. 2, pp. 139–151, 2011. View at Publisher · View at Google Scholar · View at PubMed
- L. Gartner and J. Hiat, Color Atlas of Histology, Williams & Wilkins, Baltimore, Md, USA, 1994.
- J. A. Eble and S. Niland, “The extracellular matrix of blood vessels,” Current Pharmaceutical Design, vol. 15, no. 12, pp. 1385–1400, 2009. View at Publisher · View at Google Scholar · View at Scopus
- V. S. LeBleu, B. MacDonald, and R. Kalluri, “Structure and function of basement membranes,” Experimental Biology and Medicine, vol. 232, no. 9, pp. 1121–1129, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. V. Iozzo, J. J. Zoeller, and A. Nyström, “Basement membrane proteoglycans: modulators Par excellence of cancer growth and angiogenesis,” Molecules and Cells, vol. 27, no. 5, pp. 503–513, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. D. Yurchenco, “Basement membranes: cell scaffoldings and signaling platforms,” Cold Spring Harbor Perspectives in Biology, vol. 3, no. 2, 2011.
- S. Astrof and R. O. Hynes, “Fibronectins in vascular morphogenesis,” Angiogenesis, vol. 12, no. 2, pp. 165–175, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Katsuda and T. Kaji, “Atherosclerosis and extracellular matrix,” Journal of Atherosclerosis and Thrombosis, vol. 10, no. 5, pp. 267–274, 2003. View at Scopus
- G. A. M. Plenz, M. C. Deng, H. Robenek, and W. Völker, “Vascular collagens: spotlight on the role of type VIII collagen in atherogenesis,” Atherosclerosis, vol. 166, no. 1, pp. 1–11, 2003. View at Publisher · View at Google Scholar
- K. Kühn, “Basement membrane (type IV) collagen,” Matrix Biology, vol. 14, no. 6, pp. 439–445, 1995.
- E. Pöschl, U. Schlötzer-Schrehardt, B. Brachvogel, K. Saito, Y. Ninomiya, and U. Mayer, “Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development,” Development, vol. 131, no. 7, pp. 1619–1628, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. M. Mithieux and A. S. Weiss, “Elastin,” Advances in Protein Chemistry, vol. 70, pp. 437–461, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. M. Kielty, “Elastic fibres in health and disease,” Expert Reviews in Molecular Medicine, vol. 8, no. 19, pp. 1–23, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Patel, B. Fine, M. Sandig, and K. Mequanint, “Elastin biosynthesis: the missing link in tissue-engineered blood vessels,” Cardiovascular Research, vol. 71, no. 1, pp. 40–49, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Colombatti, R. Doliana, S. Bot et al., “The EMILIN protein family,” Matrix Biology, vol. 19, no. 4, pp. 289–301, 2000. View at Publisher · View at Google Scholar · View at Scopus
- B. S. Brooke, S. K. Karnik, and D. Y. Li, “Extracellular matrix in vascular morphogenesis and disease: structure versus signal,” Trends in Cell Biology, vol. 13, no. 1, pp. 51–56, 2003. View at Publisher · View at Google Scholar · View at Scopus
- R. Timpl, T. Sasaki, G. Kostka, and M. L. Chu, “Fibulins: a versatile family of extracellular matrix proteins,” Nature Reviews Molecular Cell Biology, vol. 4, no. 6, pp. 479–489, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. Nakamura, P. R. Lozano, Y. Ikeda et al., “Fibulin-5/DANCE is essential for elastogenesis in vivo,” Nature, vol. 415, no. 6868, pp. 171–175, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Hirai, T. Ohbayashi, M. Horiguchi et al., “Fibulin-5/DANCE has an elastogenic organizer activity that is abrogated by proteolytic cleavage in vivo,” Journal of Cell Biology, vol. 176, no. 7, pp. 1061–1071, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. Giltay, R. Timpl, and G. Kostka, “Sequence, recombinant expression and tissue localization of two novel extracellular matrix proteins, fibulin-3 and fibulin-4,” Matrix Biology, vol. 18, no. 5, pp. 469–480, 1999. View at Publisher · View at Google Scholar · View at Scopus
- K. P. Dingemans, P. Teeling, J. H. Lagendijk, and A. E. Becker, “Extracellular matrix of the human aortic media: an ultrastructural histochemical and immunohistochemical study of the adult aortic media,” Anatomical Record, vol. 258, no. 1, pp. 1–14, 2000. View at Publisher · View at Google Scholar · View at Scopus
- A. G. Marneros and B. R. Olsen, “Physiological role of collagen XVIII and endostatin,” FASEB Journal, vol. 19, no. 7, pp. 716–728, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Grässel, C. Unsöld, H. Schäcke, L. Bruckner-Tuderman, and P. Bruckner, “Collagen XVI is expressed by human dermal fibroblasts and keratinocytes and is associated with the microfibrillar apparatus in the upper papillary dermis,” Matrix Biology, vol. 18, no. 3, pp. 309–317, 1999. View at Publisher · View at Google Scholar · View at Scopus
- A. Kassner, U. Hansen, N. Miosge et al., “Discrete integration of collagen XVI into tissue-specific collagen fibrils or beaded microfibrils,” Matrix Biology, vol. 22, no. 2, pp. 131–143, 2003. View at Publisher · View at Google Scholar · View at Scopus
- E. P. Moiseeva, “Adhesion receptors of vascular smooth muscle cells and their functions,” Cardiovascular Research, vol. 52, no. 3, pp. 372–386, 2001. View at Publisher · View at Google Scholar · View at Scopus
- J. A. Eble, A. Kassner, S. Niland, M. Mörgelin, J. Grifka, and S. Grässel, “Collagen XVI harbors an integrin α1β1 recognition site in its C-terminal domains,” Journal of Biological Chemistry, vol. 281, no. 35, pp. 25745–25756, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Thyberg, K. Blomgren, J. Roy, P. K. Tran, and U. Hedin, “Phenotypic modulation of smooth muscle cells after arterial injury is associated with changes in the distribution of laminin and fibronectin,” Journal of Histochemistry and Cytochemistry, vol. 45, no. 6, pp. 837–846, 1997. View at Scopus
- A. P. Hall, “Review of the pericyte during angiogenesis and its role in cancer and diabetic retinopathy,” Toxicologic Pathology, vol. 34, no. 6, pp. 763–775, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. H. Adams and K. Alitalo, “Molecular regulation of angiogenesis and lymphangiogenesis,” Nature Reviews Molecular Cell Biology, vol. 8, no. 6, pp. 464–478, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. Gerhardt and H. Semb, “Pericytes: gatekeepers in tumour cell metastasis?” Journal of Molecular Medicine, vol. 86, no. 2, pp. 135–144, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Z. Isogai, A. Aspberg, D. R. Keene, R. N. Ono, D. P. Reinhardt, and L. Y. Sakai, “Versican interacts with fibrillin-1 and links extracellular microfibrils to other connective tissue networks,” Journal of Biological Chemistry, vol. 277, no. 6, pp. 4565–4572, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Aspberg, S. Adam, G. Kostka, R. Timpl, and D. Heinegård, “Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican,” Journal of Biological Chemistry, vol. 274, no. 29, pp. 20444–20449, 1999. View at Publisher · View at Google Scholar · View at Scopus
- A. I. Olin, M. Mörgelin, T. Sasaki, R. Timpl, D. Heinegård, and A. Aspberg, “The proteoglycans aggrecan and versican form networks with fibulin-2 through their lectin domain binding,” Journal of Biological Chemistry, vol. 276, no. 2, pp. 1253–1261, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Heino and J. Käpylä, “Cellular receptors of extracellular matrix molecules,” Current Pharmaceutical Design, vol. 15, no. 12, pp. 1309–1317, 2009. View at Publisher · View at Google Scholar · View at Scopus
- L. Contois, A. Akalu, and P. C. Brooks, “Integrins as “functional hubs” in the regulation of pathological angiogenesis,” Seminars in Cancer Biology, vol. 19, no. 5, pp. 318–328, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. Zaidel-Bar, S. Itzkovitz, A. Ma'ayan, R. Iyengar, and B. Geiger, “Functional atlas of the integrin adhesome,” Nature Cell Biology, vol. 9, no. 8, pp. 858–867, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. Silva, G. D'Amico, K. M. Hodivala-Dilke, and L. E. Reynolds, “Integrins: the keys to unlocking angiogenesis,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 28, no. 10, pp. 1703–1713, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Miettinen, R. Castello, E. Wayner, and R. Schwarting, “Distribution of VLA integrins in solid tumors: emergence of tumor-type- related expression patterns in carcinomas and sarcomas,” American Journal of Pathology, vol. 142, no. 4, pp. 1009–1018, 1993. View at Scopus
- D. R. Senger, K. P. Claffey, J. E. Benes, C. A. Perruzzi, A. P. Sergiou, and M. Detmar, “Angiogenesis promoted by vascular endothelial growth factor: regulation through α1β1 and α2β1 integrins,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 25, pp. 13612–13617, 1997. View at Scopus
- D. R. Senger, C. A. Perruzzi, M. Streit, V. E. Koteliansky, A. R. De Fougerolles, and M. Detmar, “The α1β1 and α2β1 integrins provide critical support for vascular endothelial growth factor signaling, endothelial cell migration, and tumor angiogenesis,” American Journal of Pathology, vol. 160, no. 1, pp. 195–204, 2002. View at Scopus
- K. Vuoriluoto, G. Högnäs, P. Meller, K. Lehti, and J. Ivaska, “Syndecan-1 and -4 differentially regulate oncogenic K-ras dependent cell invasion into collagen through α2β1 integrin and MT1-MMP,” Matrix Biology, vol. 30, no. 3, pp. 207–217, 2011. View at Publisher · View at Google Scholar · View at PubMed
- R. O. Hynes, “Integrins: bidirectional, allosteric signaling machines,” Cell, vol. 110, no. 6, pp. 673–687, 2002. View at Publisher · View at Google Scholar · View at Scopus
- J. T. Yang, H. Rayburn, and R. O. Hynes, “Cell adhesion events mediated by α4 integrins are essential in placental and cardiac development,” Development, vol. 121, no. 2, pp. 549–560, 1995. View at Scopus
- M. R. Morgan, M. J. Humphries, and M. D. Bass, “Synergistic control of cell adhesion by integrins and syndecans,” Nature Reviews Molecular Cell Biology, vol. 8, no. 12, pp. 957–969, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. C. Brooks, R. A. F. Clark, and D. A. Cheresh, “Requirement of vascular integrin α(v)β3 for angiogenesis,” Science, vol. 264, no. 5158, pp. 569–571, 1994. View at Scopus
- R. O. Hynes, “Cell-matrix adhesion in vascular development,” Journal of Thrombosis and Haemostasis, vol. 5, no. 1, pp. 32–40, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. N. Landen, T. J. Kim, Y. G. Lin et al., “Tumor-selective response to antibody-mediated targeting of αvβ3 integrin in ovarian cancer,” Neoplasia, vol. 10, no. 11, pp. 1259–1267, 2008. View at Publisher · View at Google Scholar · View at Scopus
- G. E. Davis, “Affinity of integrins for damaged extracellular matrix: α(v)β3 binds to denatured collagen type I through RGD sites,” Biochemical and Biophysical Research Communications, vol. 182, no. 3, pp. 1025–1031, 1992. View at Scopus
- B. Nieswandt, M. Hafner, B. Echtenacher, and D. N. Männel, “Lysis of tumor cells by natural killer cells in mice is impeded by platelets,” Cancer Research, vol. 59, no. 6, pp. 1295–1300, 1999. View at Scopus
- P. C. Brooks, S. Stromblad, R. Klemke, D. Visscher, F. H. Sarkar, and D. A. Cheresh, “Antiintegrin αvβ3 blocks human breast cancer growth and angiogenesis in human skin,” Journal of Clinical Investigation, vol. 96, no. 4, pp. 1815–1822, 1995. View at Scopus
- G. H. Mahabeleshwar, W. Feng, D. R. Phillips, and T. V. Byzova, “Integrin signaling is critical for pathological angiogenesis,” Journal of Experimental Medicine, vol. 203, no. 11, pp. 2495–2507, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- X. Huang, M. Griffiths, J. Wu, R. V. Farese, and D. Sheppard, “Normal development, wound healing, and adenovirus susceptibility in β5- deficient mice,” Molecular and Cellular Biology, vol. 20, no. 3, pp. 755–759, 2000. View at Publisher · View at Google Scholar · View at Scopus
- B. L. Bader, H. Rayburn, D. Crowley, and R. O. Hynes, “Extensive vasculogenesis, angiogenesis, and organogenesis precede lethality in mice lacking all αv integrins,” Cell, vol. 95, no. 4, pp. 507–519, 1998. View at Scopus
- J. H. McCarty, R. A. Monahan-Earley, L. F. Brown et al., “Defective associations between blood vessels and brain parenchyma lead to cerebral hemorrhage in mice lacking αv integrins,” Molecular and Cellular Biology, vol. 22, no. 21, pp. 7667–7677, 2002. View at Publisher · View at Google Scholar · View at Scopus
- J. H. McCarty, A. Lacy-Hulbert, A. Charest et al., “Selective ablation of αv integrins in the central nervous system leads to cerebral hemorrhage, seizures, axonal degeneration and premature death,” Development, vol. 132, no. 1, pp. 165–176, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- L. E. Reynolds, L. Wyder, J. C. Lively et al., “Enhanced pathological angiogenesis in mice lacking β3 integrin or β3 and β5 integrins,” Nature Medicine, vol. 8, no. 1, pp. 27–34, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- F. Díaz-González, J. Forsyth, B. Steiner, and M. H. Ginsberg, “Trans-dominant inhibition of integrin function,” Molecular Biology of the Cell, vol. 7, no. 12, pp. 1939–1951, 1996. View at Scopus
- K. M. Hodivala-Dilke, C. M. DiPersio, J. A. Kreidberg, and R. O. Hynes, “Novel roles for α3β1 integrin as a regulator of cytoskeletal assembly and as a trans-dominant inhibitor of integrin receptor function in mouse keratinocytes,” Journal of Cell Biology, vol. 142, no. 5, pp. 1357–1369, 1998. View at Publisher · View at Google Scholar · View at Scopus
- D. G. Stupack, X. S. Puente, S. Boutsaboualoy, C. M. Storgard, and D. A. Cheresh, “Apoptosis of adherent cells by recruitment of caspase-8 to unligated integrins,” Journal of Cell Biology, vol. 155, no. 4, pp. 459–470, 2001. View at Scopus
- J. Zhu, K. Motejlek, D. Wang, K. Zang, A. Schmidt, and L. F. Reichardt, “β8 Integrins are required for vascular morphogenesis in mouse embryos,” Development, vol. 129, no. 12, pp. 2891–2903, 2002. View at Scopus
- K. Venstrom and L. Reichardt, “Beta 8 integrins mediate interactions of chick sensory neurons with laminin-1, collagen IV, and fibronectin,” Molecular Biology of the Cell, vol. 6, no. 4, pp. 419–431, 1995. View at Scopus
- R. Milner, J. B. Relvas, J. Fawcett, and C. Ffrench-Constant, “Developmental regulation of αv integrins produces functional changes in astrocyte behavior,” Molecular and Cellular Neuroscience, vol. 18, no. 1, pp. 108–118, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. Mu, S. Cambier, L. Fjellbirkeland et al., “The integrin ανβ8 mediates epithelial homeostasis through MT1-MMP-dependent activation of TGF-β1,” Journal of Cell Biology, vol. 157, no. 3, pp. 493–507, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Kern, J. Eble, R. Golbik, and K. Kuhn, “Interaction of type IV collagen with the isolated integrins α1β1 and α2β1,” European Journal of Biochemistry, vol. 215, no. 1, pp. 151–159, 1993. View at Scopus
- M. Tulla, O. T. Pentikäinen, T. Viitasalo et al., “Selective binding of collagen subtypes by integrin α1I, α2I, and α10I domains,” Journal of Biological Chemistry, vol. 276, no. 51, pp. 48206–48212, 2001. View at Scopus
- M. M. Zutter and S. A. Santoro, “Widespread histologic distribution of the α2β1 integrin cell-surface collagen receptor,” American Journal of Pathology, vol. 137, no. 1, pp. 113–120, 1990. View at Scopus
- T. Bengtsson, A. Aszodi, C. Nicolae, E. B. Hunziker, E. Lundgren-Åkerlund, and R. Fässler, “Loss of α10β1 integrin expression leads to moderate dysfunction of growth plate chondrocytes,” Journal of Cell Science, vol. 118, no. 5, pp. 929–936, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. N. Popova, M. Barczyk, C. F. Tiger et al., “α11β1 integrin-dependent regulation of periodontal ligament function in the erupting mouse incisor,” Molecular and Cellular Biology, vol. 27, no. 12, pp. 4306–4316, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. Riikonen, J. Westermarck, L. Koivisto, A. Broberg, V. M. Kahari, and J. Heino, “Integrin α2β1 is a positive regulator of collagenase (MMP-1) and collagen α1(I) gene expression,” Journal of Biological Chemistry, vol. 270, no. 22, pp. 13548–13552, 1995. View at Publisher · View at Google Scholar · View at Scopus
- O. Langholz, D. Röckel, C. Mauch et al., “Collagen and collagenase gene expression in three-dimensional collagen lattices are differentially regulated by α1β1 and α2β1 integrins,” Journal of Cell Biology, vol. 131, no. 6, pp. 1903–1915, 1995. View at Publisher · View at Google Scholar · View at Scopus
- H. Gardner, A. Broberg, A. Pozzi, M. Laato, and J. Heino, “Absence of integrin α1β1 in the mouse causes loss of feedback regulation of collagen synthesis in normal and wounded dermis,” Journal of Cell Science, vol. 112, no. 3, pp. 263–272, 1999. View at Scopus
- F. Alves, W. Vogel, K. Mossie, B. Millauer, H. Hofler, and A. Ullrich, “Distinct structural characteristics of discoidin I subfamily receptor tyrosine kinases and complementary expression in human cancer,” Oncogene, vol. 10, no. 3, pp. 609–618, 1995. View at Scopus
- J. M. Auger, M. J. E. Kuijpers, Y. A. Senis, S. P. Watson, and J. W. M. Heemskerk, “Adhesion of human and mouse platelets to collagen under shear: a unifying model,” FASEB Journal, vol. 19, no. 7, pp. 825–827, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- L. Meyaard, “The inhibitory collagen receptor LAIR-1 (CD305),” Journal of Leukocyte Biology, vol. 83, no. 4, pp. 799–803, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. C. Curino, L. H. Engelholm, S. S. Yamada et al., “Intracellular collagen degradation mediated by uPARAP/Endo180 is a major pathway of extracellular matrix turnover during malignancy,” Journal of Cell Biology, vol. 169, no. 6, pp. 977–985, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. A. Kreidberg, M. J. Donovan, S. L. Goldstein et al., “Alpha 3 beta 1 integrin has a crucial role in kidney and lung organogenesis,” Development, vol. 122, no. 11, pp. 3537–3547, 1996. View at Scopus
- C. M. DiPersio, K. M. Hodivala-Dilke, R. Jaenisch, J. A. Kreidberg, and R. O. Hynes, “α3β1 integrin is required for normal development of the epidermal basement membrane,” Journal of Cell Biology, vol. 137, no. 3, pp. 729–742, 1997. View at Publisher · View at Google Scholar · View at Scopus
- U. Mayer, G. Saher, R. Fässler et al., “Absence of integrin α7 causes a novel form of muscular dystrophy,” Nature Genetics, vol. 17, no. 3, pp. 318–323, 1997. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. A. Stepp, S. Spurr-Michaud, A. Tisdale, J. Elwell, and I. K. Gipson, “α6β4 integrin heterodimer is a component of hemidesmosomes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 87, no. 22, pp. 8970–8974, 1990. View at Publisher · View at Google Scholar · View at Scopus
- O. Ibraghimov-Beskrovnaya, J. M. Ervasti, C. J. Leveille, C. A. Slaughter, S. W. Sernett, and K. P. Campbell, “Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix,” Nature, vol. 355, no. 6362, pp. 696–702, 1992. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. Haenggi and J. M. Fritschy, “Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue,” Cellular and Molecular Life Sciences, vol. 63, no. 14, pp. 1614–1631, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Nelson, N. V. McFerran, G. Pivato et al., “The 67 kDa laminin receptor: structure, function and role in disease,” Bioscience reports, vol. 28, no. 1, pp. 33–48, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. Fontanini, S. Vignati, S. Chiné et al., “67-kilodalton laminin receptor expression correlates with worse prognostic indicators in non-small cell lung carcinomas,” Clinical Cancer Research, vol. 3, no. 2, pp. 227–231, 1997. View at Scopus
- D. Waltregny, L. De Leval, S. Ménard, J. De Leval, and V. Castronovo, “Independent prognostic value of the 67-kd laminin receptor in human prostate cancer,” Journal of the National Cancer Institute, vol. 89, no. 16, pp. 1224–1227, 1997. View at Scopus
- E. Ardini, E. Tagliabue, A. Magnifico et al., “Co-regulation and physical association of the 67-kDa monomeric laminin receptor and the α6β4 integrin,” Journal of Biological Chemistry, vol. 272, no. 4, pp. 2342–2345, 1997. View at Publisher · View at Google Scholar · View at Scopus
- T. Ogawa, Y. Tsubota, J. Hashimoto, Y. Kariya, and K. Miyazaki, “The short arm of laminin γ2 chain of laminin-5 (laminin-332) binds syndecan-1 and regulates cellular adhesion and migration by suppressing phosphorylation of integrin β4 chain,” Molecular Biology of the Cell, vol. 18, no. 5, pp. 1621–1633, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. G. Da Silva, B. Tavora, S. D. Robinson et al., “Endothelial α3β1-integrin represses pathological angiogenesis and sustains endothelial-VEGF,” American Journal of Pathology, vol. 177, no. 3, pp. 1534–1548, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. Van der Neut, P. Krimpenfort, J. Calafat, C. M. Niessen, and A. Sonnenberg, “Epithelial detachment due to absence of hemidesmosomes in integrin β null mice,” Nature Genetics, vol. 13, no. 3, pp. 366–369, 1996. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. N. Nikolopoulos, P. Blaikie, T. Yoshioka, W. Guo, and F. G. Giancotti, “Integrin β4 signaling promotes tumor angiogenesis,” Cancer Cell, vol. 6, no. 5, pp. 471–483, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. S. Hiran, J. E. Mazurkiewicz, P. Kreienberg, F. L. Rice, and S. E. LaFlamme, “Endothelial expression of the α6β4 integrin is negatively regulated during angiogenesis,” Journal of Cell Science, vol. 116, no. 18, pp. 3771–3781, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. M. Frisch and H. Francis, “Disruption of epithelial cell-matrix interactions induces apoptosis,” Journal of Cell Biology, vol. 124, no. 4, pp. 619–626, 1994. View at Scopus
- S. A. Wickström, K. Radovanac, and R. Fässler, “Genetic analyses of integrin signaling,” Cold Spring Harbor Perspectives in Biology, vol. 3, no. 2, 2011.
- F. G. Giancotti and E. Ruoslahti, “Integrin signaling,” Science, vol. 285, no. 5430, pp. 1028–1032, 1999. View at Publisher · View at Google Scholar · View at Scopus
- M. A. Arnaout, B. Mahalingam, and J. P. Xiong, “Integrin structure, allostery, and bidirectional signaling,” Annual Review of Cell and Developmental Biology, vol. 21, pp. 381–410, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. Methe, S. Hess, and E. R. Edelman, “Endothelial immunogenicity—a matter of matrix microarchitecture,” Thrombosis and Haemostasis, vol. 98, no. 2, pp. 278–282, 2007. View at Publisher · View at Google Scholar · View at Scopus
- Y. Wallez and P. Huber, “Endothelial adherens and tight junctions in vascular homeostasis, inflammation and angiogenesis,” Biochimica et Biophysica Acta, vol. 1778, no. 3, pp. 794–809, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Orpana, V. Ranta, T. Mikkola, L. Viinikka, and O. Ylikorkala, “Inducible nitric oxide and prostacyclin productions are differently controlled by extracellular matrix and cell density in human vascular endothelial cells,” Journal of Cellular Biochemistry, vol. 64, no. 4, pp. 538–546, 1997. View at Publisher · View at Google Scholar · View at Scopus
- M. A. Schwartz and D. W. DeSimone, “Cell adhesion receptors in mechanotransduction,” Current Opinion in Cell Biology, vol. 20, no. 5, pp. 551–556, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Ivaska and J. Heino, “Interplay between cell adhesion and growth factor receptors: from the plasma membrane to the endosomes,” Cell and Tissue Research, vol. 339, no. 1, pp. 111–120, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. Hutchings, N. Ortega, and J. Plouët, “Extracellular matrix-bound vascular endothelial growth factor promotes endothelial cell adhesion, migration, and survival through integrin ligation,” The FASEB Journal, vol. 17, no. 11, pp. 1520–1522, 2003. View at Scopus
- N. E. Vlahakis, B. A. Young, A. Atakilit et al., “Integrin α9β1 directly binds to vascular endothelial growth factor (VEGF)-A and contributes to VEGF-A-induced angiogenesis,” Journal of Biological Chemistry, vol. 282, no. 20, pp. 15187–15196, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- N. E. Vlahakis, B. A. Young, A. Atakilit, and D. Sheppard, “The lymphangiogenic vascular endothelial growth factors VEGF-C and -D are ligands for the integrin α9β1,” Journal of Biological Chemistry, vol. 280, no. 6, pp. 4544–4552, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. R. Carlson, Y. Feng, P. C. Maisonpierre, M. Mrksich, and A. O. Morla, “Direct cell adhesion to the angiopoietins mediated by integrins,” Journal of Biological Chemistry, vol. 276, no. 28, pp. 26516–26525, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. J. Leu, S. C. T. Lam, and L. F. Lau, “Pro-angiogenic activities of CYR61 (CCN1) mediated through integrins αvβ3 and α6β1 in human umbilical vein endothelial cells,” Journal of Biological Chemistry, vol. 277, no. 48, pp. 46248–46255, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. J. Leu, Y. Liu, N. Chen, C. C. Chen, S. C. T. Lam, and L. F. Lau, “Identification of a novel integrin α6β1 binding site in the angiogenic inducer CCN1 (CYR61),” Journal of Biological Chemistry, vol. 278, no. 36, pp. 33801–33808, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Mori, C. Y. Wu, S. Yamaji et al., “Direct binding of integrin αvβ3 to FGF1 plays a role in FGF1 signaling,” Journal of Biological Chemistry, vol. 283, no. 26, pp. 18066–18075, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. Suzuki, T. Okuno, M. Yamamoto et al., “Semaphorin 7A initiates T-cell-mediated inflammatory responses through α1β1 integrin,” Nature, vol. 446, no. 7136, pp. 680–684, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. T. Chao, L. A. Martinez-Lemus, S. J. Kaufman, G. A. Meininger, K. S. Ramos, and E. Wilson, “Modulation of α7-integrin-mediated adhesion and expression by platelet-derived growth factor in vascular smooth muscle cells,” American Journal of Physiology, vol. 290, no. 4, pp. C972–C980, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- N. L. Flintoff-Dye, J. Welser, J. Rooney et al., “Role for the α7β1 integrin in vascular development and integrity,” Developmental Dynamics, vol. 234, no. 1, pp. 11–21, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Y. Taooka, J. Chen, T. Yednock, and D. Sheppard, “The integrin α9β1 mediates adhesion to activated endothelial cells and transendothelial neutrophil migration through interaction with vascular cell adhesion molecule-1,” Journal of Cell Biology, vol. 145, no. 2, pp. 413–420, 1999. View at Publisher · View at Google Scholar · View at Scopus
- I. Staniszewska, S. Zaveri, L. D. Valle et al., “Interaction of α9β1 integrin with thrombospondin-1 promotes angiogenesis,” Circulation Research, vol. 100, no. 9, pp. 1308–1316, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. Bouvard, C. Brakebusch, E. Gustafsson et al., “Functional consequences of integrin gene mutations in mice,” Circulation Research, vol. 89, no. 3, pp. 211–223, 2001. View at Scopus
- R. Fässler and M. Meyer, “Consequences of lack of β1 integrin gene expression in mice,” Genes and Development, vol. 9, no. 15, pp. 1896–1908, 1995. View at Scopus
- L. E. Stephens, A. E. Sutherland, I. V. Klimanskaya et al., “Deletion of β1 integrins in mice results in inner cell mass failure and peri-implantation lethality,” Genes and Development, vol. 9, no. 15, pp. 1883–1895, 1995. View at Scopus
- T. R. Carlson, H. Hu, R. Braren, Y. H. Kim, and R. A. Wang, “Cell-autonomous requirement for β1 integrin in endothelial cell adhesion, migration and survival during angiogenesis in mice,” Development, vol. 135, no. 12, pp. 2193–2202, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- L. Lei, D. Liu, Y. Huang et al., “Endothelial expression of β1 integrin is required for embryonic vascular patterning and postnatal vascular remodeling,” Molecular and Cellular Biology, vol. 28, no. 2, pp. 794–802, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. Tanjore, E. M. Zeisberg, B. Gerami-Naini, and R. Kalluri, “β1 integrin expression on endothelial cells is required for angiogenesis but not for vasculogenesis,” Developmental Dynamics, vol. 237, no. 1, pp. 75–82, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. C. Zovein, A. Luque, K. A. Turlo et al., “β1 integrin establishes endothelial cell polarity and arteriolar lumen formation via a Par3-dependent mechanism,” Developmental Cell, vol. 18, no. 1, pp. 39–51, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Pozzi, P. E. Moberg, L. A. Miles, S. Wagner, P. Soloway, and H. A. Gardner, “Elevated matrix metalloprotease and angiostatin levels in integrin α1 knockout mice cause reduced tumor vascularization,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 5, pp. 2202–2207, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Z. Zhang, N. E. Ramirez, T. E. Yankeelov et al., “α2β1 integrin expression in the tumor microenvironment enhances tumor angiogenesis in a tumor cell-specific manner,” Blood, vol. 111, no. 4, pp. 1980–1988, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. T. Yang, H. Rayburn, and R. O. Hynes, “Embryonic mesodermal defects in α5 integrin-deficient mice,” Development, vol. 119, no. 4, pp. 1093–1105, 1993. View at Scopus
- S. E. Francis, K. L. Goh, K. Hodivala-Dilke et al., “Central roles of α5β1 integrin and fibronectin in vascular development in mouse embryos and embryoid bodies,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 22, no. 6, pp. 927–933, 2002. View at Publisher · View at Google Scholar · View at Scopus
- P. Parsons-Wingerter, I. M. Kasman, S. Norberg et al., “Uniform overexpression and rapid accessibility of α5β1 integrin on blood vessels in tumors,” American Journal of Pathology, vol. 167, no. 1, pp. 193–211, 2005. View at Scopus
- E. Georges-Labouesse, N. Messaddeq, G. Yehia, L. Cadalbert, A. Dierich, and M. Le Meur, “Absence of integrin α6 leads to epidermolysis bullosa and neonatal death in mice,” Nature Genetics, vol. 13, no. 3, pp. 370–373, 1996. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. V. Welser, N. D. Lange, N. Flintoff-Dye, H. R. Burkin, and D. J. Burkin, “Placental Defects in α7 Integrin Null Mice,” Placenta, vol. 28, no. 11-12, pp. 1219–1228, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. Fässler, E. Georges-Labouesse, and E. Hirsch, “Genetic analyses of integrin function in mice,” Current Opinion in Cell Biology, vol. 8, no. 5, pp. 641–646, 1996. View at Publisher · View at Google Scholar · View at Scopus
- X. Z. Huang, J. F. Wu, R. Ferrando et al., “Fatal bilateral chylothorax in mice lacking the integrin α9β1,” Molecular and Cellular Biology, vol. 20, no. 14, pp. 5208–5215, 2000. View at Publisher · View at Google Scholar · View at Scopus
- K. M. Hodivala-Dilke, K. P. McHugh, D. A. Tsakiris et al., “β3-integrin-deficient mice are a model for Glanzmann thrombasthenia showing placental defects and reduced survival,” Journal of Clinical Investigation, vol. 103, no. 2, pp. 229–238, 1999. View at Scopus
- Y. Takada, X. Ye, and S. Simon, “The integrins,” Genome Biology, vol. 8, no. 5, article 215, pp. 211–219, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. H. Ginsberg, A. Partridge, and S. J. Shattil, “Integrin regulation,” Current Opinion in Cell Biology, vol. 17, no. 5, pp. 509–516, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. A. Arnaout, S. L. Goodman, and J. P. Xiong, “Structure and mechanics of integrin-based cell adhesion,” Current Opinion in Cell Biology, vol. 19, no. 5, pp. 495–507, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- B. H. Luo, C. V. Carman, and T. A. Springer, “Structural basis of integrin regulation and signaling,” Annual Review of Immunology, vol. 25, pp. 619–647, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Takagi, K. Strokovich, T. A. Springer, and T. Walz, “Structure of integrin α5β1 in complex with fibronectin,” EMBO Journal, vol. 22, no. 18, pp. 4607–4615, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. P. Xiong, T. Stehle, B. Diefenbach, et al., “Crystal structure of the extracellular segment of integrin αVβ3,” Science, vol. 294, no. 5541, pp. 339–345, 2001.
- J. P. Xiong, T. Stehle, S. L. Goodman, and M. A. Arnaout, “New insights into the structural basis of integrin activation,” Blood, vol. 102, no. 4, pp. 1155–1159, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J.-P. Xiong, T. Stehle, R. Zhang et al., “Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand,” Science, vol. 296, no. 5565, pp. 151–155, 2002. View at Publisher · View at Google Scholar · View at PubMed
- M. J. Humphries, E. J. H. Symonds, and A. P. Mould, “Mapping functional residues onto integrin crystal structures,” Current Opinion in Structural Biology, vol. 13, no. 2, pp. 236–243, 2003. View at Publisher · View at Google Scholar · View at Scopus
- A. P. Mould, E. J. Koper, A. Byron, G. Zahn, and M. J. Humphries, “Mapping the ligand-binding pocket of integrin α5β1 using a gain-of-function approach,” Biochemical Journal, vol. 424, no. 2, pp. 179–189, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. A. Calderwood, “Integrin activation,” Journal of Cell Science, vol. 117, no. 5, pp. 657–666, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. J. Shattil, C. Kim, and M. H. Ginsberg, “The final steps of integrin activation: the end game,” Nature Reviews Molecular Cell Biology, vol. 11, no. 4, pp. 288–300, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. R. Ramjaun and K. Hodivala-Dilke, “The role of cell adhesion pathways in angiogenesis,” International Journal of Biochemistry and Cell Biology, vol. 41, no. 3, pp. 521–530, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. L. Wegener, A. W. Partridge, J. Han et al., “Structural Basis of Integrin Activation by Talin,” Cell, vol. 128, no. 1, pp. 171–182, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Moser, B. Nieswandt, S. Ussar, M. Pozgajova, and R. Fässler, “Kindlin-3 is essential for integrin activation and platelet aggregation,” Nature Medicine, vol. 14, no. 3, pp. 325–330, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Zhu, C. V. Carman, M. Kim, M. Shimaoka, T. A. Springer, and B. H. Luo, “Requirement of α and β subunit transmembrane helix separation for integrin outside-in signaling,” Blood, vol. 110, no. 7, pp. 2475–2483, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. Xiao, J. Takagi, B. S. Coller, J. H. Wang, and T. A. Springer, “Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics,” Nature, vol. 432, no. 7013, pp. 59–67, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- N. Nishida, C. Xie, M. Shimaoka, Y. Cheng, T. Walz, and T. A. Springer, “Activation of leukocyte β2 integrins by conversion from bent to extended conformations,” Immunity, vol. 25, no. 4, pp. 583–594, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. R. Legate, E. Montañez, O. Kudlacek, and R. Fässler, “ILK, PINCH and parvin: the tIPP of integrin signalling,” Nature Reviews Molecular Cell Biology, vol. 7, no. 1, pp. 20–31, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Zöller, “Tetraspanins: push and pull in suppressing and promoting metastasis,” Nature Reviews Cancer, vol. 9, no. 1, pp. 40–55, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. H. Park, J. M. Ryu, and H. J. Han, “Involvement of caveolin-1 in fibronectin-induced mouse embryonic stem cell proliferation: role of FAK, RhoA, PI3K/Akt, and ERK 1/2 pathways,” Journal of Cellular Physiology, vol. 226, no. 1, pp. 267–275, 2011. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. H. Lee, Y. J. Lee, S. W. Park, H. S. Kim, and H. J. Han, “Caveolin-1 and integrin β1 regulate embryonic stem cell proliferation via p38 MAPK and FAK in high glucose,” Journal of Cellular Physiology, vol. 226, no. 7, pp. 1850–1859, 2011. View at Publisher · View at Google Scholar
- A. Byron, M. R. Morgan, and M. J. Humphries, “Adhesion signalling complexes,” Current Biology, vol. 20, no. 24, pp. R1063–R1067, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. A. Del Pozo, N. B. Alderson, W. B. Kiosses, H. H. Chiang, R. G. W. Anderson, and M. A. Schwartz, “Integrins regulate rac targeting by internalization of membrane domains,” Science, vol. 303, no. 5659, pp. 839–842, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- I. J. Salanueva, A. Cerezo, M. C. Guadamillas, and M. A. Del Pozo, “Integrin regulation of caveolin function: caveolae review series,” Journal of Cellular and Molecular Medicine, vol. 11, no. 5, pp. 969–980, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- I. Bethani, S. S. Skånland, I. Dikic, and A. Acker-Palmer, “Spatial organization of transmembrane receptor signalling,” EMBO Journal, vol. 29, no. 16, pp. 2677–2688, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. W. Tilghman and J. T. Parsons, “Focal adhesion kinase as a regulator of cell tension in the progression of cancer,” Seminars in Cancer Biology, vol. 18, no. 1, pp. 45–52, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. C. Brown, L. A. Cary, J. S. Jamieson, J. A. Cooper, and C. E. Turner, “Src and FAK kinases cooperate to phosphorylate paxillin kinase linker, stimulate its focal adhesion localization, and regulate cell spreading and protrusiveness,” Molecular Biology of the Cell, vol. 16, no. 9, pp. 4316–4328, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- E. G. Arias-Salgado, S. Lizano, S. Sarkar, J. S. Brugge, M. H. Ginsberg, and S. J. Shattil, “Src kinase activation by direct interaction with the integrin β cytoplasmic domain,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 23, pp. 13298–13302, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. K. Hanks, M. B. Calalb, M. C. Harper, and S. K. Patel, “Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 18, pp. 8487–8491, 1992. View at Scopus
- A. Papapetropoulos, D. Fulton, K. Mahboubi et al., “Angiopoietin-1 inhibits endothelial cell apoptosis via the Akt/survivin pathway,” Journal of Biological Chemistry, vol. 275, no. 13, pp. 9102–9105, 2000. View at Publisher · View at Google Scholar · View at Scopus
- S. H. Kim and S. H. Kim, “Antagonistic effect of EGF on FAK phosphorylation/dephosphorylation in a cell,” Cell Biochemistry and Function, vol. 26, no. 5, pp. 539–547, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. K. Slack-Davis, S. T. Eblen, M. Zecevic et al., “PAK1 phosphorylation of MEK1 regulates fibronectin-stimulated MAPK activation,” Journal of Cell Biology, vol. 162, no. 2, pp. 281–291, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. L. Edin and R. L. Juliano, “Raf-1 serine 338 phosphorylation plays a key role in adhesion-dependent activation of extracellular signal-regulated kinase by epidermal growth factor,” Molecular and Cellular Biology, vol. 25, no. 11, pp. 4466–4475, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. L. Shen, A. Y. J. Park, A. Alcaraz et al., “Conditional knockout of focal adhesion kinase in endothelial cells reveals its role in angiogenesis and vascular development in late embryogenesis,” Journal of Cell Biology, vol. 169, no. 6, pp. 941–952, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. L. Courter, L. Lomas, M. Scatena, and C. M. Giachelli, “Src kinase activity is required for integrin αvβ 3-mediated activation of nuclear factor-κB,” Journal of Biological Chemistry, vol. 280, no. 13, pp. 12145–12151, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Zaric and C. Rüegg, “Integrin-mediated adhesion and soluble ligand binding stabilize COX-2 protein levels in endothelial cells by inducing expression and preventing degradation,” Journal of Biological Chemistry, vol. 280, no. 2, pp. 1077–1085, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- B. P. Eliceiri, X. S. Puente, J. D. Hood et al., “Src-mediated coupling of focal adhesion kinase to integrin αvβ5 in vascular endothelial growth factor signaling,” Journal of Cell Biology, vol. 157, no. 1, pp. 149–160, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. A. Wickström, K. Alitalo, and J. Keski-Oja, “Endostatin associates with integrin α5β1 and caveolin-1, and activates Src via a tyrosyl phosphatase-dependent pathway in human endothelial cells,” Cancer Research, vol. 62, no. 19, pp. 5580–5589, 2002. View at Scopus
- A. Aiyer and J. Varner, “The role of integrins in tumor angiogenesis,” in Cancer Drug Discovery Development—Antiangiogenic Agents in Cancer Therapy, B. A. Teicher and L. M. Ellis, Eds., pp. 49–73, Humana Press, Totowa, NJ, USA, 2008.
- C. Chandra Kumar, “Signaling by integrin receptors,” Oncogene, vol. 17, no. 11, pp. 1365–1373, 1998. View at Scopus
- K. I. Nagashima, A. Endo, H. Ogita et al., “Adaptor protein Crk is required for ephrin-B1-induced membrane ruffling and focal complex assembly of human aortic endothelial cells,” Molecular Biology of the Cell, vol. 13, no. 12, pp. 4231–4242, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- F. Paulhe, C. Racaud-Sultan, A. Ragab et al., “Differential regulation of phosphoinositide metabolism by α vβ3 and αvβ5 integrins upon smooth muscle cell migration,” Journal of Biological Chemistry, vol. 276, no. 45, pp. 41832–41840, 2001. View at Publisher · View at Google Scholar · View at PubMed
- V. Carloni, R. G. Romanelli, M. Pinzani, G. Laffi, and P. Gentilini, “Focal adhesion kinase and phospholipase Cγ involvement in adhesion and migration of human hepatic stellate cells,” Gastroenterology, vol. 112, no. 2, pp. 522–531, 1997. View at Publisher · View at Google Scholar · View at Scopus
- X. Zhang, A. Chattopadhyay, Q. S. Ji et al., “Focal adhesion kinase promotes phospholipase C-γ1 activity,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 16, pp. 9021–9026, 1999. View at Publisher · View at Google Scholar · View at Scopus
- L. Bi, I. Okabe, D. J. Bernard, A. Wynshaw-Boris, and R. L. Nussbaum, “Proliferative defect and embryonic lethality in mice homozygous for a deletion in the p110α subunit of phosphoinositide 3-kinase,” Journal of Biological Chemistry, vol. 274, no. 16, pp. 10963–10968, 1999. View at Publisher · View at Google Scholar · View at Scopus
- E. Lelievre, P. M. Bourbon, L. J. Duan, R. L. Nussbaum, and G. H. Fong, “Deficiency in the p110α subunit of PI3K results in diminished Tie2 expression and Tie2-/–like vascular defects in mice,” Blood, vol. 105, no. 10, pp. 3935–3938, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Graupera, J. Guillermet-Guibert, L. C. Foukas et al., “Angiogenesis selectively requires the p110α isoform of PI3K to control endothelial cell migration,” Nature, vol. 453, no. 7195, pp. 662–666, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Sudhakar, H. Sugimoto, C. Yang, J. Lively, M. Zeisberg, and R. Kalluri, “Human tumstatin and human endostatin exhibit distinct antiangiogenic activities mediated by αvβ and α5β1 integrins,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 8, pp. 4766–4771, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Gupta, A. R. Ramjaun, P. Haiko et al., “Binding of ras to phosphoinositide 3-kinase p110α is required for ras-driven tumorigenesis in mice,” Cell, vol. 129, no. 5, pp. 957–968, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. S. Roberts, A. J. Woods, P. E. Shaw, and J. C. Norman, “ERK1 associates with αvβ3 integrin and regulates cell spreading on vitronectin,” Journal of Biological Chemistry, vol. 278, no. 3, pp. 1975–1985, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. M. Short, G. A. Talbott, and R. L. Juliano, “Integrin-mediated signaling events in human endothelial cells,” Molecular Biology of the Cell, vol. 9, no. 8, pp. 1969–1980, 1998. View at Scopus
- M. Hüser, J. Luckett, A. Chiloeches et al., “MEK kinase activity is not necessary for Raf-1 function,” EMBO Journal, vol. 20, no. 8, pp. 1940–1951, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Giroux, M. Tremblay, D. Bernard et al., “Embryonic death of Mek1-deficient mice reveals a role for this kinase in angiogenesis in the labyrinthine region of the placenta,” Current Biology, vol. 9, no. 7, pp. 369–372, 1999. View at Publisher · View at Google Scholar · View at Scopus
- J. D. Hood, R. Frausto, W. B. Kiosses, M. A. Schwartz, and D. A. Cheresh, “Differential αv integrin-mediated Ras-ERK signaling during two pathways of angiogenesis,” Journal of Cell Biology, vol. 162, no. 5, pp. 933–943, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. K. Wary, F. Mainiero, S. J. Isakoff, E. E. Marcantonio, and F. G. Giancotti, “The adaptor protein Shc couples a class of integrins to the control of cell cycle progression,” Cell, vol. 87, no. 4, pp. 733–743, 1996. View at Publisher · View at Google Scholar · View at Scopus
- A. Pozzi, K. K. Wary, F. G. Giancotti, and H. A. Gardner, “Integrin α1β1 mediates a unique collagen-dependent proliferation pathway in vivo,” Journal of Cell Biology, vol. 142, no. 2, pp. 587–594, 1998. View at Publisher · View at Google Scholar · View at Scopus
- A. K. Fournier, L. E. Campbell, P. Castagnino et al., “Rac-dependent cyclin D1 gene expression regulated by cadherin- and integrin-mediated adhesion,” Journal of Cell Science, vol. 121, no. 2, pp. 226–233, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- E. A. Klein, L. Yin, D. Kothapalli et al., “Cell-cycle control by physiological matrix elasticity and in vivo tissue stiffening,” Current Biology, vol. 19, no. 18, pp. 1511–1518, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Klein, A. R. De Fougerolles, P. Blaikie et al., “α5β1 integrin activates an NF-κB-dependent program of gene expression important for angiogenesis and inflammation,” Molecular and Cellular Biology, vol. 22, no. 16, pp. 5912–5922, 2002. View at Publisher · View at Google Scholar · View at Scopus
- M. Reidy, P. Zihlmann, J. A. Hubbell, and H. Hall, “Activation of cell-survival transcription factor NFκB in L1Ig6-stimulated endothelial cells,” Journal of Biomedical Materials Research Part A, vol. 77, no. 3, pp. 542–550, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Scatena, M. Almeida, M. L. Chaisson, N. Fausto, R. F. Nicosia, and C. M. Giachelli, “NF-κB mediates αvβ3 integrin-induced endothelial cell survival,” Journal of Cell Biology, vol. 141, no. 4, pp. 1083–1093, 1998. View at Publisher · View at Google Scholar · View at Scopus
- O. Dormond, M. Bezzi, A. Mariotti, and C. Rüegg, “Prostaglandin E2 promotes integrin αvβ3-dependent endothelial cell adhesion, Rac-activation, and spreading through cAMP/PKA-dependent signaling,” Journal of Biological Chemistry, vol. 277, no. 48, pp. 45838–45846, 2002. View at Publisher · View at Google Scholar · View at PubMed
- C. S. Boosani, A. P. Mannam, D. Cosgrove et al., “Regulation of COX-2-mediated signaling by α3 type IV noncollagenous domain in tumor angiogenesis,” Blood, vol. 110, no. 4, pp. 1168–1177, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. Kisseleva, L. Song, M. Vorontchikhina, N. Feirt, J. Kitajewski, and C. Schindler, “NF-κB regulation of endothelial cell function during LPS-induced toxemia and cancer,” Journal of Clinical Investigation, vol. 116, no. 11, pp. 2955–2963, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. Lahlou, V. Sanguin-Gendreau, D. Zuo et al., “Mammary epithelial-specific disruption of the focal adhesion kinase blocks mammary tumor progression,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 51, pp. 20302–20307, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Y. Pylayeva, K. M. Gillen, W. Gerald, H. E. Beggs, L. F. Reichardt, and F. G. Giancotti, “Ras- and PI3K-dependent breast tumorigenesis in mice and humans requires focal adhesion kinase signaling,” Journal of Clinical Investigation, vol. 119, no. 2, pp. 252–266, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- V. Samanna, H. Wei, D. Ego-Osuala, and M. A. Chellaiah, “Alpha-V-dependent outside-in signaling is required for the regulation of CD44 surface expression, MMP-2 secretion, and cell migration by osteopontin in human melanoma cells,” Experimental Cell Research, vol. 312, no. 12, pp. 2214–2230, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. M. Zutter, S. A. Santoro, W. D. Staatz, and Y. L. Tsung, “Re-expression of the α2β1 integrin abrogates the malignant phenotype of breast carcinoma cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 16, pp. 7411–7415, 1995. View at Publisher · View at Google Scholar · View at Scopus
- A. Kren, V. Baeriswyl, F. Lehembre et al., “Increased tumor cell dissemination and cellular senescence in the absence of β1-integrin function,” EMBO Journal, vol. 26, no. 12, pp. 2832–2842, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. Zhao, F. P. Ross, and S. L. Teitelbaum, “Unoccupied αvβ3 integrin regulates osteoclast apoptosis by transmitting a positive death signal,” Molecular Endocrinology, vol. 19, no. 3, pp. 771–780, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. M. Frisch and R. A. Screaton, “Anoikis mechanisms,” Current Opinion in Cell Biology, vol. 13, no. 5, pp. 555–562, 2001. View at Publisher · View at Google Scholar · View at Scopus
- D. G. Stupack, T. Teitz, M. D. Potter et al., “Potentiation of neuroblastoma metastasis by loss of caspase-8,” Nature, vol. 439, no. 7072, pp. 95–99, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. S. Desgrosellier, L. A. Barnes, D. J. Shields et al., “An integrin (v)(3)-c-Src oncogenic unit promotes anchorage-independence and tumor progression,” Nature Medicine, vol. 15, no. 10, pp. 1163–1169, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. L. Matter and E. Ruoslahti, “A signaling pathway from the α5β1 and αvβ3 integrins that elevates bcl-2 transcription,” Journal of Biological Chemistry, vol. 276, no. 30, pp. 27757–27763, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- F. Aoudjit and K. Vuori, “Matrix attachment regulates Fas-induced apoptosis in endothelial cells: a role for c-Flip and implications for anoikis,” Journal of Cell Biology, vol. 153, no. 3, pp. 633–643, 2001. View at Scopus
- W. Bao and S. Strömblad, “Integrin αv-mediated inactivation of p53 controls a MEK1-dependent melanoma cell survival pathway in three-dimensional collagen,” Journal of Cell Biology, vol. 167, no. 4, pp. 745–756, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Alavi, J. D. Hood, R. Frausto, D. G. Stupack, and D. A. Cheresh, “Role of Raf in vascular protection from distinct apoptotic stimuli,” Science, vol. 301, no. 5629, pp. 94–96, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- E. Ruoslahti, “Specialization of tumour vasculature,” Nature Reviews Cancer, vol. 2, no. 2, pp. 83–90, 2002. View at Scopus
- N. Alam, H. L. Goel, M. J. Zarif et al., “The integrin—growth factor receptor duet,” Journal of Cellular Physiology, vol. 213, no. 3, pp. 649–653, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. Serini, L. Napione, M. Arese, and F. Bussolino, “Besides adhesion: new perspectives of integrin functions in angiogenesis,” Cardiovascular Research, vol. 78, no. 2, pp. 213–222, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- E. S. Wijelath, S. Rahman, M. Namekata et al., “Heparin-II domain of fibronectin is a vascular endothelial growth factor-binding domain: enhancement of VEGF biological activity by a singular growth factor/matrix protein synergism,” Circulation Research, vol. 99, no. 8, pp. 853–860, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Q. Zhu, S. N. Popova, E. R. S. Brown et al., “Integrin α11 regulates IGF2 expression in fibroblasts to enhance tumorigenicity of human non-small-cell lung cancer cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 28, pp. 11754–11759, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Orecchia, P. M. Lacal, C. Schietroma, V. Morea, G. Zambruno, and C. M. Failla, “Vascular endothelial growth factor receptor-1 is deposited in the extracellular matrix by endothelial cells and is a ligand for the α5β1 integrin,” Journal of Cell Science, vol. 116, no. 17, pp. 3479–3489, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. Kajiya, S. Hirakawa, B. Ma, I. Drinnenberg, and M. Detmar, “Hepatocyte growth factor promotes lymphatic vessel formation and function,” EMBO Journal, vol. 24, no. 16, pp. 2885–2895, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Murakami, A. Elfenbein, and M. Simons, “Non-canonical fibroblast growth factor signalling in angiogenesis,” Cardiovascular Research, vol. 78, no. 2, pp. 223–231, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. Camenisch, M. T. Pisabarro, D. Sherman et al., “ANGPTL3 stimulates endothelial cell adhesion and migration via integrin αvβ3 and induces blood vessel formation in vivo,” Journal of Biological Chemistry, vol. 277, no. 19, pp. 17281–17290, 2002. View at Publisher · View at Google Scholar · View at PubMed
- S. M. Dallabrida, N. Ismail, J. R. Oberle, B. E. Himes, and M. A. Rupnick, “Angiopoietin-1 promotes cardiac and skeletal myocyte survival through integrins,” Circulation research, vol. 96, no. 4, pp. e8–e24, 2005. View at Scopus
- E. C. Finger and A. J. Giaccia, “Hypoxia, inflammation, and the tumor microenvironment in metastatic disease,” Cancer and Metastasis Reviews, vol. 29, no. 2, pp. 285–293, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Billioux, U. Modlich, and R. Bicknell, “Angiogenesis,” in The Cancer Handbook, M. Alison, Ed., vol. 1, pp. 144–154, John Wiley & Sons, 2007.
- P. Carmeliet, “Angiogenesis in health and disease,” Nature Medicine, vol. 9, no. 6, pp. 653–660, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Folkman, K. Watson, D. Ingber, and D. Hanahan, “Induction of angiogenesis during the transition from hyperplasia to neoplasia,” Nature, vol. 339, no. 6219, pp. 58–61, 1989. View at Scopus
- N. Weidner, J. P. Semple, W. R. Welch, and J. Folkman, “Tumor angiogenesis and metastasis—correlation in invasive breast carcinoma,” New England Journal of Medicine, vol. 324, no. 1, pp. 1–8, 1991. View at Scopus
- J. Kandel, E. Bossy-Wetzel, F. Radvanyi, M. Klagsbrun, J. Folkman, and D. Hanahan, “Neovascularization is associated with a switch to the export of bFGF in the multistep development of fibrosarcoma,” Cell, vol. 66, no. 6, pp. 1095–1104, 1991. View at Scopus
- E. Y. Lin and J. W. Pollard, “Tumor-associated macrophages press the angiogenic switch in breast cancer,” Cancer Research, vol. 67, no. 11, pp. 5064–5066, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. C. Schmid and J. A. Varner, “Myeloid cell trafficking and tumor angiogenesis,” Cancer Letters, vol. 250, no. 1, pp. 1–8, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- N. Ferrara, H. P. Gerber, and J. LeCouter, “The biology of VEGF and its receptors,” Nature Medicine, vol. 9, no. 6, pp. 669–676, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- E. C. Keeley, B. Mehrad, and R. M. Strieter, “Chemokines as mediators of tumor angiogenesis and neovascularization,” Experimental Cell Research, vol. 317, no. 5, pp. 685–690, 2011. View at Publisher · View at Google Scholar · View at PubMed
- K. H. Hong, J. Ryu, and K. H. Han, “Monocyte chemoattractant protein-1-induced angiogenesis is mediated by vascular endothelial growth factor-A,” Blood, vol. 105, no. 4, pp. 1405–1407, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Niu, A. Azfer, O. Zhelyabovska, S. Fatma, and P. E. Kolattukudy, “Monocyte chemotactic protein (MCP)-1 promotes angiogenesis via a novel transcription factor, MCP-1-induced protein (MCPIP),” Journal of Biological Chemistry, vol. 283, no. 21, pp. 14542–14551, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. C. Aplin, E. Fogel, and R. F. Nicosia, “MCP-1 promotes mural cell recruitment during angiogenesis in the aortic ring model,” Angiogenesis, vol. 13, no. 3, pp. 219–226, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- E. Iivanainen, V. M. Kähäri, J. Heino, and K. Elenius, “Endothelial cell-matrix interactions,” Microscopy Research and Technique, vol. 60, no. 1, pp. 13–22, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. E. Rundhaug, “Matrix metalloproteinases and angiogenesis,” Journal of Cellular and Molecular Medicine, vol. 9, no. 2, pp. 267–285, 2005. View at Scopus
- G. Murphy and H. Nagase, “Localizing matrix metalloproteinase activities in the pericellular environment,” FEBS Journal, vol. 278, no. 1, pp. 2–15, 2011. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. O. Ahn and J. M. Brown, “Matrix metalloproteinase-9 is required for tumor vasculogenesis but not for angiogenesis: role of bone marrow-derived myelomonocytic cells,” Cancer Cell, vol. 13, no. 3, pp. 193–205, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. M. Eilken and R. H. Adams, “Dynamics of endothelial cell behavior in sprouting angiogenesis,” Current Opinion in Cell Biology, vol. 22, no. 5, pp. 617–625, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W. Risau, “Mechanisms of angiogenesis,” Nature, vol. 386, no. 6626, pp. 671–674, 1997. View at Scopus
- J. Folkman, “Looking for a good endothelial address,” Cancer Cell, vol. 1, no. 2, pp. 113–115, 2002. View at Publisher · View at Google Scholar · View at Scopus
- T. Asahara, T. Murohara, A. Sullivan et al., “Isolation of putative progenitor endothelial cells for angiogenesis,” Science, vol. 275, no. 5302, pp. 964–967, 1997. View at Publisher · View at Google Scholar · View at Scopus
- F. Brellier, R. P. Tucker, and R. Chiquet-Ehrismann, “Tenascins and their implications in diseases and tissue mechanics,” Scandinavian Journal of Medicine and Science in Sports, vol. 19, no. 4, pp. 511–519, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Kaspar, L. Zardi, and D. Neri, “Fibronectin as target for tumor therapy,” International Journal of Cancer, vol. 118, no. 6, pp. 1331–1339, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Midulla, R. Verma, M. Pignatelli, M. A. Ritter, N. S. Courtenay-Luck, and A. J. T. George, “Source of oncofetal ED-B-containing fibronectin: implications of production of both tumor and endothelial cells,” Cancer Research, vol. 60, no. 1, pp. 164–169, 2000. View at Scopus
- K. S. Midwood and G. Orend, “The role of tenascin-C in tissue injury and tumorigenesis,” Journal of Cell Communication and Signaling, vol. 3, no. 3-4, pp. 287–310, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Degen, F. Brellier, S. Schenk et al., “Tenascin-W, a new marker of cancer stroma, is elevated in sera of colon and breast cancer patients,” International Journal of Cancer, vol. 122, no. 11, pp. 2454–2461, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- E. Martina, R. Chiquet-Ehrismann, and F. Brellier, “Tenascin-W: an extracellular matrix protein associated with osteogenesis and cancer,” International Journal of Biochemistry and Cell Biology, vol. 42, no. 9, pp. 1412–1415, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- B. Döme, M. J. C. Hendrix, S. Paku, J. Tóvári, and J. Tímár, “Alternative vascularization mechanisms in cancer: pathology and therapeutic implications,” American Journal of Pathology, vol. 170, no. 1, pp. 1–15, 2007. View at Publisher · View at Google Scholar · View at PubMed
- F. Hillen and A. W. Griffioen, “Tumour vascularization: sprouting angiogenesis and beyond,” Cancer and Metastasis Reviews, vol. 26, no. 3-4, pp. 489–502, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. Lyden, K. Hattori, S. Dias et al., “Impaired recruitment of bone-marrow-derived endothelial and hematopoietic precursor cells blocks tumor angiogenesis and growth,” Nature Medicine, vol. 7, no. 11, pp. 1194–1201, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. Ribatti, “The involvement of endothelial progenitor cells in tumor angiogenesis,” Journal of Cellular and Molecular Medicine, vol. 8, no. 3, pp. 294–300, 2004. View at Scopus
- M. Reyes, A. Dudek, B. Jahagirdar, L. Koodie, P. H. Marker, and C. M. Verfaillie, “Origin of endothelial progenitors in human postnatal bone marrow,” Journal of Clinical Investigation, vol. 109, no. 3, pp. 337–346, 2002. View at Publisher · View at Google Scholar · View at Scopus
- M. L. Iruela-Arispe and G. E. Davis, “Cellular and molecular mechanisms of vascular lumen formation,” Developmental Cell, vol. 16, no. 2, pp. 222–231, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- B. Strilić, T. Kučera, J. Eglinger et al., “The molecular basis of vascular lumen formation in the developing mouse aorta,” Developmental Cell, vol. 17, no. 4, pp. 505–515, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. M. Ghajar, S. C. George, and A. J. Putnam, “Matrix metalloproteinase control of capillary morphogenesis,” Critical Reviews in Eukaryotic Gene Expression, vol. 18, no. 3, pp. 251–278, 2008. View at Scopus
- R. Hildenbrand, H. Allgayer, A. Marx, and P. Stroebel, “Modulators of the urokinase-type plasminogen activation system for cancer,” Expert Opinion on Investigational Drugs, vol. 19, no. 5, pp. 641–652, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- F. Bougatef, C. Quemener, S. Kellouche et al., “EMMPRIN promotes angiogenesis through hypoxia-inducible factor-2α-mediated regulation of soluble VEGF isoforms and their receptor VEGFR-2,” Blood, vol. 114, no. 27, pp. 5547–5556, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. C. Brooks, S. Strömblad, L. C. Sanders et al., “Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin αvβ3,” Cell, vol. 85, no. 5, pp. 683–693, 1996. View at Publisher · View at Google Scholar · View at Scopus
- V. Djonov, M. Schmid, S. A. Tschanz, and P. H. Burri, “Intussusceptive angiogenesis. Its role in embryonic vascular network formation,” Circulation Research, vol. 86, no. 3, pp. 286–292, 2000. View at Scopus
- H. Kurz, P. H. Burri, and V. G. Djonov, “Angiogenesis and vascular remodeling by intussusception: from form to function,” News in Physiological Sciences, vol. 18, no. 2, pp. 65–70, 2003. View at Scopus
- A. N. Makanya, R. Hlushchuk, and V. G. Djonov, “Intussusceptive angiogenesis and its role in vascular morphogenesis, patterning, and remodeling,” Angiogenesis, vol. 12, no. 2, pp. 113–123, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. J. Brat and E. G. Van Meir, “Glomeruloid microvascular proliferation orchestrated by VPF/VEGF: a new world of angiogenesis research,” American Journal of Pathology, vol. 158, no. 3, pp. 789–796, 2001. View at Scopus
- O. Straume, P. O. Chappuis, H. B. Salvesen et al., “Prognostic importance of glomeruloid microvascular proliferation indicates an aggressive angiogenic phenotype in human cancers,” Cancer Research, vol. 62, no. 23, pp. 6808–6811, 2002. View at Scopus
- J. Holash, P. C. Maisonpierre, D. Compton et al., “Vessel cooption, regression, and growth in tumors mediated by angiopoietins and VEGF,” Science, vol. 284, no. 5422, pp. 1994–1998, 1999. View at Publisher · View at Google Scholar · View at Scopus
- B. Döme, S. Paku, B. Somlai, and J. Timar, “Vascularization of cutaneous melanoma involves vessel co-option and has clinical significance,” Journal of Pathology, vol. 197, no. 3, pp. 355–362, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Scharpfenecker, U. Fiedler, Y. Reiss, and H. G. Augustin, “The Tie-2 ligand angiopoietin-2 destabilizes quiescent endothelium through an internal autocrine loop mechanism,” Journal of Cell Science, vol. 118, no. 4, pp. 771–780, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- L. E. Benjamin, D. Golijanin, A. Itin, D. Pode, and E. Keshet, “Selective ablation of immature blood vessels in established human tumors follows vascular endothelial growth factor withdrawal,” Journal of Clinical Investigation, vol. 103, no. 2, pp. 159–165, 1999. View at Scopus
- A. J. Maniotis, R. Folberg, A. Hess et al., “Vascular channel formation by human melanoma cells in vivo and in vitro: vasculogenic mimicry,” American Journal of Pathology, vol. 155, no. 3, pp. 739–752, 1999. View at Scopus
- R. Folberg and A. J. Maniotis, “Vasculogenic mimicry,” Acta Pathologica, Microbiologica. et Immunologica Scandinavica, vol. 112, no. 7-8, pp. 508–525, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. J. G. Pötgens, M. C. Van Altena, N. H. Lubsen, D. J. Ruiter, and R. M. W. De Waal, “Analysis of the tumor vasculature and metastatic behavior of xenografts of human melanoma cell lines transfected with vascular permeability factor,” American Journal of Pathology, vol. 148, no. 4, pp. 1203–1217, 1996. View at Scopus
- R. Clarijs, I. Otte-Höller, D. J. Ruiter, and R. M. W. De Waal, “Presence of a fluid-conducting meshwork in xenografted cutaneous and primary human uveal melanoma,” Investigative Ophthalmology and Visual Science, vol. 43, no. 4, pp. 912–918, 2002. View at Scopus
- T. Kučera and E. Lammert, “Ancestral vascular tube formation and its adoption by tumors,” Biological Chemistry, vol. 390, no. 10, pp. 985–994, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W. Ruf, E. A. Seftor, R. J. Petrovan et al., “Differential role of tissue factor pathway inhibitors 1 and 2 in melanoma vasculogenic mimicry,” Cancer Research, vol. 63, no. 17, pp. 5381–5389, 2003. View at Scopus
- S. Anand, B. K. Majeti, L. M. Acevedo et al., “MicroRNA-132-mediated loss of p120RasGAP activates the endothelium to facilitate pathological angiogenesis,” Nature Medicine, vol. 16, no. 8, pp. 909–914, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Anand and D. A. Cheresh, “MicroRNA-mediated regulation of the angiogenic switch,” Current Opinion in Hematology, vol. 18, no. 3, pp. 171–176, 2011. View at Publisher · View at Google Scholar · View at PubMed
- G. Bellon, L. Martiny, and A. Robinet, “Matrix metalloproteinases and matrikines in angiogenesis,” Critical Reviews in Oncology/Hematology, vol. 49, no. 3, pp. 203–220, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. Nyberg, L. Xie, and R. Kalluri, “Endogenous inhibitors of angiogenesis,” Cancer Research, vol. 65, no. 10, pp. 3967–3979, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Shimaoka and T. A. Springer, “Therapeutic antagonists and conformational regulation of integrin function,” Nature Reviews Drug Discovery, vol. 2, no. 9, pp. 703–716, 2003. View at Scopus
- J. A. Eble and J. Haier, “Integrins in cancer treatment,” Current Cancer Drug Targets, vol. 6, no. 2, pp. 89–105, 2006. View at Publisher · View at Google Scholar · View at Scopus
- S. M. Short, A. Derrien, R. P. Narsimhan, J. Lawler, D. E. Ingber, and B. R. Zetter, “Inhibition of endothelial cell migration by thrombospondin-1 type-1 repeats is mediated by β1 integrins,” Journal of Cell Biology, vol. 168, no. 4, pp. 643–653, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- X. Zhang and J. Lawler, “Thrombospondin-based antiangiogenic therapy,” Microvascular Research, vol. 74, no. 2-3, pp. 90–99, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. C. Colorado, A. Torre, G. Kamphaus et al., “Anti-angiogenic cues from vascular basement membrane collagen,” Cancer Research, vol. 60, no. 9, pp. 2520–2526, 2000. View at Scopus
- P. Nyberg, L. Xie, H. Sugimoto et al., “Characterization of the anti-angiogenic properties of arresten, an α1β1 integrin-dependent collagen-derived tumor suppressor,” Experimental Cell Research, vol. 314, no. 18, pp. 3292–3305, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- B. P. Woodall, A. Nyström, R. A. Iozzo et al., “Integrin α2β1 is the required receptor for endorepellin angiostatic activity,” Journal of Biological Chemistry, vol. 283, no. 4, pp. 2335–2343, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Mongiat, S. M. Sweeney, J. D. San Antonio, J. Fu, and R. V. Iozzo, “Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan,” Journal of Biological Chemistry, vol. 278, no. 6, pp. 4238–4249, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Marcinkiewicz, P. H. Weinreb, J. J. Calvete et al., “Obtu-statin: a potent selective inhibitor of α1β1 integrin in vitro and angiogenesis in vivo,” Cancer Research, vol. 63, no. 9, pp. 2020–2023, 2003. View at Scopus
- M. C. Brown, I. Staniszewska, L. Del Valle, G. P. Tuszynski, and C. Marcinkiewicz, “Angiostatic activity of obtustatin as α1β1 integrin inhibitor in experimental melanoma growth,” International Journal of Cancer, vol. 123, no. 9, pp. 2195–2203, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. A. Eble, B. Beermann, H.-J. Hinz, and A. Schmidt-Hederich, “α2β1 integrin is not recognized by rhodocytin but is the specific, high affinity target of rhodocetin, an RGD-independent disintegrin and potent inhibitor of cell adhesion to collagen,” Journal of Biological Chemistry, vol. 276, no. 15, pp. 12274–12284, 2001. View at Publisher · View at Google Scholar · View at PubMed
- J. A. Eble, S. Niland, A. Dennes, A. Schmidt-Hederich, P. Bruckner, and G. Brunner, “Rhodocetin antagonizes stromal tumor invasion in vitro and other α2β1 integrin-mediated cell functions,” Matrix Biology, vol. 21, no. 7, pp. 547–558, 2002. View at Publisher · View at Google Scholar · View at Scopus
- J. Zhou, V. L. Rothman, I. Sargiannidou et al., “Cloning and characterization of angiocidin, a tumor cell binding protein for thrombospondin-1,” Journal of Cellular Biochemistry, vol. 92, no. 1, pp. 125–146, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Y. Sabherwal, V. L. Rothman, S. Dimitrov et al., “Integrinα2β1 mediates the anti-angiogenic and anti-tumor activities of angiocidin, a novel tumor-associated protein,” Experimental Cell Research, vol. 312, no. 13, pp. 2443–2453, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. C. Pandey, M. W. Toussaint, J. C. McGuire, and M. C. Thomas, “Maggiemycin and anhydromaggiemycin: two novel anthracyclinone antitumor antibiotics—isolation, structures, partial synthesis and biological properties,” Journal of Antibiotics, vol. 42, no. 11, pp. 1567–1577, 1989. View at Scopus
- J. Käpylä, O. T. Pentikäinen, T. Nyrönen et al., “Small molecule designed to target metal binding site in the α2I domain inhibits integrin function,” Journal of Medicinal Chemistry, vol. 50, no. 11, pp. 2742–2746, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- L. Nissinen, O. T. Pentikäinen, A. Jouppila et al., “A small-molecule inhibitor of integrin α2β1 introduces a new strategy for antithrombotic therapy,” Thrombosis and Haemostasis, vol. 103, no. 2, pp. 387–397, 2010. View at Publisher · View at Google Scholar · View at PubMed
- Y. Funahashi, N. H. Sugi, T. Semba et al., “Sulfonamide derivative, E7820, is a unique angiogenesis inhibitor suppressing an expression of integrin α2 subunit on endothelium,” Cancer Research, vol. 62, no. 21, pp. 6116–6123, 2002. View at Scopus
- M. S. O'Reilly, T. Boehm, Y. Shing et al., “Endostatin: an endogenous inhibitor of angiogenesis and tumor growth,” Cell, vol. 88, no. 2, pp. 277–285, 1997. View at Publisher · View at Google Scholar · View at Scopus
- R. S. Herbst, K. R. Hess, H. T. Tran et al., “Phase I study of recombinant human endostatin in patients with advanced solid tumors,” Journal of Clinical Oncology, vol. 20, no. 18, pp. 3792–3803, 2002. View at Publisher · View at Google Scholar · View at Scopus
- J. Dixelius, H. Larsson, T. Sasaki et al., “Endostatin-induced tyrosine kinase signaling through the Shb adaptor protein regulates endothelial cell apoptosis,” Blood, vol. 95, no. 11, pp. 3403–3411, 2000. View at Scopus
- S. A. Karumanchi, V. Jha, R. Ramchandran et al., “Cell surface glypicans are low-affinity endostatin receptors,” Molecular Cell, vol. 7, no. 4, pp. 811–822, 2001. View at Publisher · View at Google Scholar · View at Scopus
- S. A. Wickström, K. Alitalo, and J. Keski-Oja, “An endostatin-derived peptide interacts with integrins and regulates actin cytoskeleton and migration of endothelial cells,” Journal of Biological Chemistry, vol. 279, no. 19, pp. 20178–20185, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. E. Cianfrocca, K. A. Kimmel, J. Gallo et al., “Phase 1 trial of the antiangiogenic peptide ATN-161 (Ac-PHSCN-NH 2), a beta integrin antagonist, in patients with solid tumours,” British Journal of Cancer, vol. 94, no. 11, pp. 1621–1626, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. P. Mould, L. Burrows, and M. J. Humphries, “Identification of amino acid residues that form part of the ligand- binding pocket of integrin α5β1,” Journal of Biological Chemistry, vol. 273, no. 40, pp. 25664–25672, 1998. View at Publisher · View at Google Scholar
- L. Marinelli, A. Meyer, D. Heckmann, A. Lavecchia, E. Novellino, and H. Kessler, “Ligand binding analysis for human α5β1 integrin: strategies for designing new α5β1 integrin antagonists,” Journal of Medicinal Chemistry, vol. 48, no. 13, pp. 4204–4207, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- N. Umeda, S. Kachi, H. Akiyama et al., “Suppression and regression of choroidal neovascularization by systemic administration of an α5β1 integrin antagonist,” Molecular Pharmacology, vol. 69, no. 6, pp. 1820–1828, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. K. Kuwada, “Volociximab, an angiogenesis-inhibiting chimeric monoclonal antibody,” Current Opinion in Molecular Therapeutics, vol. 9, no. 1, pp. 92–98, 2007. View at Scopus
- M. L. Wahl, T. L. Moser, and S. V. Pizzo, “Angiostatin and anti-angiogenic therapy in human disease,” Recent Progress in Hormone Research, vol. 59, pp. 73–104, 2004. View at Publisher · View at Google Scholar · View at Scopus
- D. Zhang, P. L. Kaufman, G. Gao, R. A. Saunders, and J. X. Ma, “Intravitreal injection of plasminogen kringle 5, an endogenous angiogenic inhibitor, arrests retinal neovascularization in rats,” Diabetologia, vol. 44, no. 6, pp. 757–765, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W.R. Ji, F. J. Castellino, Y. Chang et al., “Characterization of kringle domains of angiostatin as antagonists of endothelial cell migration, an important process in angiogenesis,” FASEB Journal, vol. 12, no. 15, pp. 1731–1738, 1998. View at Scopus
- Y. Hamano and R. Kalluri, “Tumstatin, the NC1 domain of α3 chain of type IV collagen, is an endogenous inhibitor of pathological angiogenesis and suppresses tumor growth,” Biochemical and Biophysical Research Communications, vol. 333, no. 2, pp. 292–298, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Y. Maeshima, P. C. Colorado, and R. Kalluri, “Two RGD-independent α(v)β3 integrin binding sites on tumstatin regulate distinct anti-tumor properties,” Journal of Biological Chemistry, vol. 275, no. 31, pp. 23745–23750, 2000. View at Publisher · View at Google Scholar · View at PubMed
- N. Floquet, S. Pasco, L. Ramont et al., “The antitumor properties of the α3(IV)-(185–203) peptide from the NC1 domain of type IV collagen (tumstatin) are conformation-dependent,” Journal of Biological Chemistry, vol. 279, no. 3, pp. 2091–2100, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Magnon, A. Galaup, B. Mullan et al., “Canstatin acts on endothelial and tumor cells via mitochondrial damage initiated through interaction with αvβ3 and αvβ5 integrins,” Cancer Research, vol. 65, no. 10, pp. 4353–4361, 2005. View at Publisher · View at Google Scholar · View at PubMed
- E. Petitclerc, A. Boutaud, A. Prestayko et al., “New functions for non-collagenous domains of human collagen type IV. Novel integrin ligands inhibiting angiogenesis and tumor growth in vivo,” Journal of Biological Chemistry, vol. 275, no. 11, pp. 8051–8061, 2000. View at Publisher · View at Google Scholar · View at Scopus
- P. C. Brooks, S. Silletti, T. L. Von Schalscha, M. Friedlander, and D. A. Cheresh, “Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity,” Cell, vol. 92, no. 3, pp. 391–400, 1998. View at Publisher · View at Google Scholar · View at Scopus
- L. Bello, V. Lucini, G. Carrabba et al., “Simultaneous inhibition of glioma angiogenesis, cell proliferation, and invasion by a naturally occurring fragment of human metalloproteinase-2,” Cancer Research, vol. 61, no. 24, pp. 8730–8736, 2001. View at Scopus
- J.-O. Nam, H.-W. Jeong, B.-H. Lee, R.-W. Park, and I.-S. Kim, “Regulation of tumor angiogenesis by fastatin, the fourth FAS1 domain of βig-h3, via αvβ3 integrin,” Cancer Research, vol. 65, no. 10, pp. 4153–4161, 2005. View at Publisher · View at Google Scholar · View at PubMed
- C. Mas-Moruno, F. Rechenmacher, and H. Kessler, “Cilengitide: the first anti-angiogenic small molecule drug candidate. Design, synthesis and clinical evaluation,” Anti-Cancer Agents in Medicinal Chemistry, vol. 10, no. 10, pp. 753–768, 2010.
- K. E. Shannon, J. L. Keene, S. L. Settle et al., “Anti-metastatic properties of RGD-peptidomimetic agents S137 and S247,” Clinical and Experimental Metastasis, vol. 21, no. 2, pp. 129–138, 2004. View at Publisher · View at Google Scholar · View at Scopus
- A. Abdollahi, D. W. Griggs, H. Zieher et al., “Inhibition of αvβ3 integrin survival signaling enhances antiangiogenic and antitumor effects of radiotherapy,” Clinical Cancer Research, vol. 11, no. 17, pp. 6270–6279, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- N. E. Tsopanoglou, M. E. Papaconstantinou, C. S. Flordellis, and M. E. Maragoudakis, “On the mode of action of thrombin-induced angiogenesis: thrombin peptide, TP508, mediates effects in endothelial cells via α vβ3 integrin,” Thrombosis and Haemostasis, vol. 92, no. 4, pp. 846–857, 2004. View at Publisher · View at Google Scholar · View at Scopus
- K. Meerovitch, F. Bergeron, L. Leblond et al., “A novel RGD antagonist that targets both αvβ3 and α5β1 induces apoptosis of angiogenic endothelial cells on type I collagen,” Vascular Pharmacology, vol. 40, no. 2, pp. 77–89, 2003. View at Publisher · View at Google Scholar · View at Scopus
- C. C. Kumar, M. Malkowski, Z. Yin et al., “Inhibition of angiogenesis and tumor growth by SCH 221153, a dual αvβ3 and αvβ5 integrin receptor antagonist,” Cancer Research, vol. 61, no. 5, pp. 2232–2238, 2001. View at Scopus
- L. Belvisi, T. Riccioni, M. Marcellini et al., “Biological and molecular properties of a new αvβ3/αvβ5 integrin antagonist,” Molecular Cancer Therapeutics, vol. 4, no. 11, pp. 1670–1680, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. Minamiguchi, H. Kumagai, T. Masuda, M. Kawada, M. Ishizuka, and T. Takeuchi, “Thiolutin, an inhibitor of huvec adhesion to vitronectin, reduces paxillin in huvecs and suppresses tumor cell-induced angiogenesis,” International Journal of Cancer, vol. 93, no. 3, pp. 307–316, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. Soldi, S. Mitola, M. Strasly, P. Defilippi, G. Tarone, and F. Bussolino, “Role of α(v)β3 integrin in the activation of vascular endothelial growth factor receptor-2,” EMBO Journal, vol. 18, no. 4, pp. 882–892, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. C. Gutheil, T. N. Campbell, P. R. Pierce et al., “Targeted antiangiogenic therapy for cancer using vitaxin: a humanized monoclonal antibody to the integrin α(v)β3,” Clinical Cancer Research, vol. 6, no. 8, pp. 3056–3061, 2000. View at Scopus
- D. G. McNeel, J. Eickhoff, F. T. Lee et al., “Phase I trial of a monoclonal antibody specific for α vβ3 integrin (MEDI-522) in patients with advanced malignancies, including an assessment of effect on tumor perfusion,” Clinical Cancer Research, vol. 11, no. 21, pp. 7851–7860, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. Zhang, T. Pier, D. G. McNeel, G. Wilding, and A. Friedl, “Effects of a monoclonal anti-αvβ3 integrin antibody on blood vessels—a pharmacodynamic study,” Investigational New Drugs, vol. 25, no. 1, pp. 49–55, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. Hersey, J. Sosman, S. O'Day et al., “A randomized phase 2 study of etaracizumab, a monoclonal antibody against integrin alpha(v)beta(3), + or - dacarbazine in patients with stage IV metastatic melanoma,” Cancer, vol. 116, no. 6, pp. 1526–1534, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. J. O'Day, A. C. Pavlick, M. R. Albertini, et al., “Clinical and pharmacologic evaluation of two dose levels of intetumumab (CNTO 95) in patients with melanoma or angiosarcoma,” Investigational New Drugs. In press. View at Publisher · View at Google Scholar · View at PubMed
- J. A. Varner, M. T. Nakada, R. E. Jordan, and B. S. Coller, “Inhibition of angiogenesis and tumor growth by murine 7E3, the parent antibody of c7E3 Fab (abciximab; ReoPro),” Angiogenesis, vol. 3, no. 1, pp. 53–60, 1999. View at Scopus
- M. T. Nakada, G. Cao, P. M. Sassoli, and H. M. DeLisser, “c7E3 Fab inhibits human tumor angiogenesis in a SCID mouse human skin xenograft model,” Angiogenesis, vol. 9, no. 4, pp. 171–176, 2006. View at Scopus
- F. Mitjans, T. Meyer, C. Fittschen et al., “In vivo therapy of malignant melanoma by means of antagonists of αv integrins,” International Journal of Cancer, vol. 87, no. 5, pp. 716–723, 2000. View at Publisher · View at Google Scholar · View at Scopus
- A. R. Reynolds, I. R. Hart, A. R. Watson et al., “Stimulation of tumor growth and angiogenesis by low concentrations of RGD-mimetic integrin inhibitors,” Nature Medicine, vol. 15, no. 4, pp. 392–400, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. Hanahan, “A flanking attack on cancer,” Nature Medicine, vol. 4, no. 1, pp. 13–14, 1998. View at Publisher · View at Google Scholar · View at Scopus
- R. K. Jain, “Normalization of tumor vasculature: an emerging concept in antiangiogenic therapy,” Science, vol. 307, no. 5706, pp. 58–62, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. Huang and L. Chen, “Tumor vasculature and microenvironment normalization: a possible mechanism of antiangiogenesis therapy,” Cancer Biotherapy and Radiopharmaceuticals, vol. 23, no. 5, pp. 661–667, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. Bergers and D. Hanahan, “Modes of resistance to anti-angiogenic therapy,” Nature Reviews Cancer, vol. 8, no. 8, pp. 592–603, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. Fraisl, M. Mazzone, T. Schmidt, and P. Carmeliet, “Regulation of angiogenesis by oxygen and metabolism,” Developmental Cell, vol. 16, no. 2, pp. 167–179, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Rapisarda and G. Melillo, “Role of the hypoxic tumor microenvironment in the resistance to anti-angiogenic therapies,” Drug Resistance Updates, vol. 12, no. 3, pp. 74–80, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. J. Lunt, N. Chaudary, and R. P. Hill, “The tumor microenvironment and metastatic disease,” Clinical and Experimental Metastasis, vol. 26, no. 1, pp. 19–34, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. De Bock, S. Cauwenberghs, and P. Carmeliet, “Vessel abnormalization: another hallmark of cancer? Molecular mechanisms and therapeutic implications,” Current Opinion in Genetics and Development, vol. 21, no. 1, pp. 73–79, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. R. Reynolds, “Potential relevance of bell-shaped and u-shaped dose-responses for the therapeutic targeting of angiogenesis in cancer,” Dose-Response, vol. 8, no. 3, pp. 253–284, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. De, O. Razorenova, N. P. McCabe, T. O'Toole, J. Qin, and T. V. Byzova, “VEGF—integrin interplay controls tumor growth and vascularization,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 21, pp. 7589–7594, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. H. Mahabeleshwar, J. Chen, W. Feng, P. R. Somanath, O. V. Razorenova, and T. V. Byzova, “Integrin affinity modulation in angiogenesis,” Cell Cycle, vol. 7, no. 3, pp. 335–347, 2008. View at Scopus
- P. R. Somanath, A. Ciocea, and T. V. Byzova, “Integrin and growth factor receptor alliance in angiogenesis,” Cell Biochemistry and Biophysics, vol. 53, no. 2, pp. 53–64, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. R. Somanath, N. L. Malinin, and T. V. Byzova, “Cooperation between integrin ανβ3 and VEGFR2 in angiogenesis,” Angiogenesis, vol. 12, no. 2, pp. 177–185, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Cretu, J. M. Roth, M. Caunt et al., “Disruption of endothelial cell interactions with the novel Hu177 cryptic collagen epitope inhibits angiogenesis,” Clinical Cancer Research, vol. 13, no. 10, pp. 3068–3078, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. Chen and X. Chen, “Integrin targeted delivery of chemotherapeutics,” Theranostics, vol. 1, pp. 189–200, 2011.
- Z. Wang, W. K. Chui, and P. C. Ho, “Integrin targeted drug and gene delivery,” Expert Opinion on Drug Delivery, vol. 7, no. 2, pp. 159–171, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. N. Sugahara, T. Teesalu, P. Prakash Karmali et al., “Coadministration of a tumor-penetrating peptide enhances the efficacy of cancer drugs,” Science, vol. 328, no. 5981, pp. 1031–1035, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. J. Strijkers, E. Kluza, G. A. F. Van Tilborg et al., “Paramagnetic and fluorescent liposomes for target-specific imaging and therapy of tumor angiogenesis,” Angiogenesis, vol. 13, no. 2, pp. 161–173, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. J. Beer, H. Kessler, H. J. Wester, and M. Schwaiger, “PET Imaging of Integrin alphaVbeta3 expression,” Theranostics, vol. 1, pp. 48–57, 2011.
- F. Kiessling, J. Gaetjens, and M. Palmowski, “Application of molecular ultrasound for imaging integrin expression,” Theranostics, vol. 1, pp. 127–134, 2011.
- E. Mery, E. Jouve, S. Guillermet et al., “Intraoperative fluorescence imaging of peritoneal dissemination of ovarian carcinomas. A preclinical study,” Gynecologic Oncology, vol. 122, no. 1, pp. 155–162, 2011. View at Publisher · View at Google Scholar · View at PubMed