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Journal of Biomedicine and Biotechnology
Volume 2012 (2012), Article ID 136302, 8 pages
Potential Role of Kringle-Integrin Interaction in Plasmin and uPA Actions (A Hypothesis)
Department of Dermatology, and Biochemistry and Molecular Medicine, University of California Davis School of Medicine, Research III Suite 3300, 4645 Second Avenue, Sacramento, CA 95817, USA
Received 24 March 2012; Revised 21 June 2012; Accepted 21 June 2012
Academic Editor: Edward F. Plow
Copyright © 2012 Yoshikazu Takada. 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.
- Y. Takada, X. Ye, and S. Simon, “The integrins,” Genome Biology, vol. 8, no. 5, article 215, 2007.
- M. S. O'Reilly, L. Holmgren, Y. Shing et al., “Angiostatin: a circulating endothelial cell inhibitor that suppresses angiogenesis and tumor growth,” Cold Spring Harbor Symposia on Quantitative Biology, vol. 59, pp. 471–482, 1994.
- Y. Cao, M. S. O'Reilly, B. Marshall, E. Flynn, R. W. Ji, and J. Folkman, “Expression of angiostatin cDNA in a murine fibrosarcoma suppresses primary tumor growth and produces long-term dormancy of metastases,” Journal of Clinical Investigation, vol. 101, no. 5, pp. 1055–1063, 1998.
- S. Gately, P. Twardowski, M. S. Stack et al., “The mechanism of cancer-mediated conversion of plasminogen to the angiogenesis inhibitor angiostatin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 20, pp. 10868–10872, 1997.
- A. J. Lay, X. M. Jiang, O. Kisker et al., “Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase,” Nature, vol. 408, no. 6814, pp. 869–873, 2000.
- Y. Cao, R. W. Ji, D. Davidson et al., “Kringle domains of human angiostatin: characterization of the anti- proliferative activity on endothelial cells,” Journal of Biological Chemistry, vol. 271, no. 46, pp. 29461–29467, 1996.
- T. Tarui, L. A. Miles, and Y. Takada, “Specific interaction of angiostatin with integrin αvβ3 in endothelial cells,” Journal of Biological Chemistry, vol. 276, no. 43, pp. 39562–39568, 2001.
- T. Syrovets, B. Tippler, M. Rieks, and T. Simmet, “Plasmin is a potent and specific chemoattractant for human peripheral monocytes acting via a cyclic guanosine monophosphate-dependent pathway,” Blood, vol. 89, no. 12, pp. 4574–4583, 1997.
- T. Tarui, M. Majumdar, L. A. Miles, W. Ruf, and Y. Takada, “Plasmin-induced migration of endothelial cells: a potential target for the anti-angiogenic action of angiostatin,” Journal of Biological Chemistry, vol. 277, no. 37, pp. 33564–33570, 2002.
- M. Majumdar, T. Tarui, B. Shi, N. Akakura, W. Ruf, and Y. Takada, “Plasmin-induced migration requires signaling through protease-activated receptor 1 and integrin α9β1,” Journal of Biological Chemistry, vol. 279, no. 36, pp. 37528–37534, 2004.
- E. Pluskota, D. A. Soloviev, K. Bdeir, D. B. Cines, and E. F. Plow, “Integrin αMβ2 orchestrates and accelerates plasminogen activation and fibrinolysis by neutrophils,” Journal of Biological Chemistry, vol. 279, no. 17, pp. 18063–18072, 2004.
- V. P. Yakubenko, S. P. Yadav, and T. P. Ugarova, “Integrin αDβ2, an adhesion receptor up-regulated on macrophage foam cells, exhibits multiligand-binding properties,” Blood, vol. 107, no. 4, pp. 1643–1650, 2006.
- V. K. Lishko, V. V. Novokhatny, V. P. Yakubenko, H. V. Skomorovska-Prokvolit, and T. P. Ugarova, “Characterization of plasminogen as an adhesive ligand for integrins αMβ2 (Mac-1) and α5β 1,” Blood, vol. 104, no. 3, pp. 719–726, 2004.
- H. K. Kim, D. S. Oh, S. B. Lee, J. M. Ha, and A. J. Young, “Antimigratory effect of TK1-2 is mediated in part by interfering with integrin α2β1,” Molecular Cancer Therapeutics, vol. 7, no. 7, pp. 2133–2141, 2008.
- L. Liu, A. W. Craig, H. D. Meldrum, S. M. Marcovina, B. E. Elliott, and M. L. Koschinsky, “Apolipoprotein(a) stimulates vascular endothelial cell growth and migration and signals through integrin αVβ3,” Biochemical Journal, vol. 418, no. 2, pp. 325–336, 2009.
- H. A. Chapman, “Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration,” Current Opinion in Cell Biology, vol. 9, no. 5, pp. 714–724, 1997.
- P. A. Andreasen, L. Kjoller, L. Christensen, and M. J. Duffy, “The urokinase-type plasminogen activator system in cancer metastasis: a review,” International Journal of Cancer, vol. 72, no. 1, pp. 1–22, 1997.
- K. Danø, J. Rømer, B. S. Nielsen et al., “Cancer invasion and tissue remodeling—cooperation of protease systems and cell types,” Acta Pathologica, Microbiologica et Immunologica Scandinavica, vol. 107, no. 1, pp. 120–127, 1999.
- A. Mondino and F. Blasi, “uPA and uPAR in fibrinolysis, immunity and pathology,” Trends in Immunology, vol. 25, no. 8, pp. 450–455, 2004.
- E. Appella, E. A. Robinson, and S. J. Ullrich, “The receptor-binding sequence of urokinase. A biological function for the growth-factor module of proteases,” Journal of Biological Chemistry, vol. 262, no. 10, pp. 4437–4440, 1987.
- K. Bdeir, A. Kuo, B. S. Sachais et al., “The kringle stabilizes urokinase binding to the urokinase receptor,” Blood, vol. 102, no. 10, pp. 3600–3608, 2003.
- D. A. Waltz, R. M. Fujita, X. Yang et al., “Nonproteolytic role for the urokinase receptor in cellular migration in vivo,” American Journal of Respiratory Cell and Molecular Biology, vol. 22, no. 3, pp. 316–322, 2000.
- V. Ellis, C. Pyke, J. Eriksen, H. Solberg, and K. Dano, “The urokinase receptor: involvement in cell surface proteolysis and cancer invasion,” Annals of the New York Academy of Sciences, vol. 667, pp. 13–31, 1992.
- P. Carmeliet, L. Schoonjans, L. Kieckens et al., “Physiological consequences of loss of plasminogen activator gene function in mice,” Nature, vol. 368, no. 6470, pp. 419–424, 1994.
- T. H. Bugge, M. J. Flick, M. J. S. Danton et al., “Urokinase-type plasminogen activator is effective in fibrin clearance in the absence of its receptor or tissue-type plasminogen activator,” Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 12, pp. 5899–5904, 1996.
- D. A. Waltz, L. Z. Sailor, and H. A. Chapman, “Cytokines induce urokinase-dependent adhesion of human myeloid cells. A regulatory role for plasminogen activator inhibitors,” Journal of Clinical Investigation, vol. 91, no. 4, pp. 1541–1552, 1993.
- M. R. Gyetko, R. F. Todd, C. C. Wilkinson, and R. G. Sitrin, “The urokinase receptor is required for human monocyte chemotaxis in vitro,” Journal of Clinical Investigation, vol. 93, no. 4, pp. 1380–1387, 1994.
- N. Busso, S. K. Masur, D. Lazega, S. Waxman, and L. Ossowski, “Induction of cell migration by pro-urokinase binding to its receptor: possible mechanism for signal transduction in human epithelial cells,” Journal of Cell Biology, vol. 126, no. 1, pp. 259–270, 1994.
- L. E. Odekon, N. Gilboa, P. Del Vecchio, and P. W. Gudewicz, “Urokinase in conditioned medium from phorbol ester-pretreated endothelial cells promotes polymorphonuclear leukocyte migration,” Circulatory Shock, vol. 37, no. 2, pp. 169–175, 1992.
- S. A. Rabbani, A. P. Mazar, S. M. Bernier et al., “Structural requirements for the growth factor activity of the amino- terminal domain of urokinase,” Journal of Biological Chemistry, vol. 267, no. 20, pp. 14151–14156, 1992.
- J. A. Aguirre Ghiso, K. Kovalski, and L. Ossowski, “Tumor dormancy induced by downregulation of urokinase receptor in human carcinoma involves integrin and MAPK signaling,” Journal of Cell Biology, vol. 147, no. 1, pp. 89–103, 1999.
- K. Fischer, V. Lutz, O. Wilhelm et al., “Urokinase induces proliferation of human ovarian cancer cells: characterization of structural elements required for growth factor function,” FEBS Letters, vol. 438, no. 1-2, pp. 101–105, 1998.
- S. M. Kanse, O. Benzakour, C. Kanthou, C. Kost, H. Roger Lijnen, and K. T. Preissner, “Induction of vascular SMC proliferation by urokinase indicates a novel mechanism of action in vasoproliferative disorders,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 17, no. 11, pp. 2848–2854, 1997.
- J. L. Koopman, J. Slomp, A. C. W. de Bart, P. H. A. Quax, and J. H. Verheijent, “Mitogenic effects of urokinase on melanoma cells are independent of high affinity binding to the urokinase receptor,” Journal of Biological Chemistry, vol. 273, no. 50, pp. 33267–33272, 1998.
- S. Mukhina, V. Stepanova, D. Traktouev et al., “The chemotactic action of urokinase on smooth muscle cells is dependent on its kringle domain. Characterization of interactions and contribution to chemotaxis,” Journal of Biological Chemistry, vol. 275, no. 22, pp. 16450–16458, 2000.
- A. Haj-Yehia, T. Nassar, B. S. Sachais et al., “Urokinase-derived peptides regulate vascular smooth muscle contraction in vitro and in vivo,” The FASEB Journal, vol. 14, no. 10, pp. 1411–1422, 2000.
- T. Nassar, A. Haj-Yehia, S. Akkawi et al., “Binding of urokinase to low density lipoprotein-related receptor (LRP) regulates vascular smooth muscle cell contraction,” Journal of Biological Chemistry, vol. 277, no. 43, pp. 40499–40504, 2002.
- T. Tarui, N. Akakura, M. Majumdar et al., “Direct interaction of the kringle domain of urokinase-type plasminogen activator (uPA) and integrin αvβ3 induces signal transduction and enhances plasminogen activation,” Thrombosis and Haemostasis, vol. 95, no. 3, pp. 524–534, 2006.
- A. P. Mazar, “Urokinase plasminogen activator receptor choreographs multiple ligand interactions: implications for tumor progression and therapy,” Clinical Cancer Research, vol. 14, no. 18, pp. 5649–5655, 2008.
- S. H. Kwak, S. Mitra, K. Bdeir et al., “The kringle domain of urokinase-type plasminogen activator potentiates LPS-induced neutrophil activation through interaction with α vβ3 integrins,” Journal of Leukocyte Biology, vol. 78, no. 4, pp. 937–945, 2005.
- B. Degryse, J. Fernandez-Recio, V. Citro, F. Blasi, and M. V. Cubellis, “In silico docking of urokinase plasminogen activator and integrins,” BMC Bioinformatics, vol. 9, no. 2, article S8, 2008.
- Y. Wei, J. A. Eble, Z. Wang, J. A. Kreidberg, and H. A. Chapman, “Urokinase receptors promote β1 integrin function through interactions with integrin α3β1,” Molecular Biology of the Cell, vol. 12, no. 10, pp. 2975–2986, 2001.
- D. I. Simon, N. K. Rao, H. Xu et al., “Mac-1 (CD11b/CD18) and the urokinase receptor (CD87) form a functional unit on monocytic cells,” Blood, vol. 88, no. 8, pp. 3185–3194, 1996.
- Y. Wei, M. Lukashev, D. I. Simon et al., “Regulation of integrin function by the urokinase receptor,” Science, vol. 273, no. 5281, pp. 1551–1555, 1996.