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BioMed Research International
Volume 2015 (2015), Article ID 654765, 11 pages
http://dx.doi.org/10.1155/2015/654765
Review Article

Decorin: A Growth Factor Antagonist for Tumor Growth Inhibition

1School of Medicine, University of Tampere, 33014 Tampere, Finland
2Department of Orthopedics & Traumatology, Tampere University Hospital, 33521 Tampere, Finland

Received 27 July 2015; Accepted 21 October 2015

Academic Editor: Jean Claude Dussaule

Copyright © 2015 Tero A. H. Järvinen and Stuart Prince. 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

  1. T. Krusius and E. Ruoslahti, “Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA,” Proceedings of the National Academy of Sciences of the United States of America, vol. 83, no. 20, pp. 7683–7687, 1986. View at Publisher · View at Google Scholar · View at Scopus
  2. E. Ruoslahti and Y. Yamaguchi, “Proteoglycans as modulators of growth factor activities,” Cell, vol. 64, no. 5, pp. 867–869, 1991. View at Publisher · View at Google Scholar · View at Scopus
  3. Y. Yamaguchi and E. Ruoslahti, “Expression of human proteoglycan in Chinese hamster ovary cells inhibits cell proliferation,” Nature, vol. 336, no. 6196, pp. 244–246, 1988. View at Publisher · View at Google Scholar · View at Scopus
  4. W. A. Border, N. A. Noble, T. Yamamoto et al., “Natural inhibitor of transforming growth factor-β protects against scarring in experimental kidney disease,” Nature, vol. 360, no. 6402, pp. 361–364, 1992. View at Publisher · View at Google Scholar · View at Scopus
  5. Y. Yamaguchi, D. M. Mann, and E. Ruoslahti, “Negative regulation of transforming growth factor-β by the proteoglycan decorin,” Nature, vol. 346, no. 6281, pp. 281–284, 1990. View at Publisher · View at Google Scholar · View at Scopus
  6. D. D. Sofeu Feugaing, M. Götte, and M. Viola, “More than matrix: the multifaceted role of decorin in cancer,” European Journal of Cell Biology, vol. 92, no. 1, pp. 1–11, 2013. View at Publisher · View at Google Scholar · View at Scopus
  7. D. M. Mann, Y. Yamaguchi, M. A. Bourdon, and E. Ruoslahiti, “Analysis of glycosaminoglycan substitution in decorin by site-directed mutagenesis,” Journal of Biological Chemistry, vol. 265, no. 9, pp. 5317–5323, 1990. View at Google Scholar · View at Scopus
  8. P. A. McEwan, P. G. Scott, P. N. Bishop, and J. Bella, “Structural correlations in the family of small leucine-rich repeat proteins and proteoglycans,” Journal of Structural Biology, vol. 155, no. 2, pp. 294–305, 2006. View at Publisher · View at Google Scholar · View at Scopus
  9. P. G. Scott, P. A. McEwan, C. M. Dodd, E. M. Bergmann, P. N. Bishop, and J. Bella, “Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 44, pp. 15633–15638, 2004. View at Publisher · View at Google Scholar · View at Scopus
  10. M. Islam, J. Gor, S. J. Perkins, Y. Ishikawa, H. P. Bächinger, and E. Hohenester, “The concave face of decorin mediates reversible dimerization and collagen binding,” Journal of Biological Chemistry, vol. 288, no. 49, pp. 35526–35533, 2013. View at Publisher · View at Google Scholar · View at Scopus
  11. P. Lorenzo, A. Aspberg, P. Önnerfjord, M. T. Bayliss, P. J. Neame, and D. Heinegård, “Identification and characterization of asporin. A novel member of the leucine-rich repeat protein family closely related to decorin and biglycan,” The Journal of Biological Chemistry, vol. 276, no. 15, pp. 12201–12211, 2001. View at Publisher · View at Google Scholar · View at Scopus
  12. A. Corsi, T. Xu, X.-D. Chen et al., “Phenotypic effects of biglycan deficiency are linked to collagen fibril abnormalities, are synergized by decorin deficiency, and mimic Ehlers-Danlos-like changes in bone and other connective tissues,” Journal of Bone and Mineral Research, vol. 17, no. 7, pp. 1180–1189, 2002. View at Publisher · View at Google Scholar · View at Scopus
  13. S. Kalamajski, A. Aspberg, K. Lindblom, D. Heinegård, and Å. Oldberg, “Asporin competes with decorin for collagen binding, binds calcium and promotes osteoblast collagen mineralization,” Biochemical Journal, vol. 423, no. 1, pp. 53–59, 2009. View at Publisher · View at Google Scholar · View at Scopus
  14. K. G. Danielson, H. Baribault, D. F. Holmes, H. Graham, K. E. Kadler, and R. V. Iozzo, “Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility,” Journal of Cell Biology, vol. 136, no. 3, pp. 729–743, 1997. View at Publisher · View at Google Scholar · View at Scopus
  15. L. Ameye and M. F. Young, “Mice deficient in small leucine-rich proteoglycans: novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases,” Glycobiology, vol. 12, no. 9, pp. 107R–116R, 2002. View at Google Scholar · View at Scopus
  16. X. Bi, C. Tong, A. Dockendorff et al., “Genetic deficiency of decorin causes intestinal tumor formation through disruption of intestinal cell maturation,” Carcinogenesis, vol. 29, no. 7, pp. 1435–1440, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. R. V. Iozzo, F. Chakrani, D. Perrotti et al., “Cooperative action of germ-line mutations in decorin and p53 accelerates lymphoma tumorigenesis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 6, pp. 3092–3097, 1999. View at Publisher · View at Google Scholar · View at Scopus
  18. Z. Horváth, I. Kovalszky, A. Fullár et al., “Decorin deficiency promotes hepatic carcinogenesis,” Matrix Biology, vol. 35, pp. 194–205, 2014. View at Publisher · View at Google Scholar · View at Scopus
  19. K. Baghy, Z. Horváth, E. Regos et al., “Decorin interferes with platelet-derived growth factor receptor signaling in experimental hepatocarcinogenesis,” FEBS Journal, vol. 280, no. 10, pp. 2150–2164, 2013. View at Publisher · View at Google Scholar · View at Scopus
  20. S. Chen, M. Sun, R. V. Iozzo, W. W.-Y. Kao, and D. E. Birk, “Intracellularly-retained decorin lacking the C-terminal ear repeat causes ER stress: a cell-based etiological mechanism for congenital stromal corneal dystrophy,” The American Journal of Pathology, vol. 183, no. 1, pp. 247–256, 2013. View at Publisher · View at Google Scholar · View at Scopus
  21. B. Bozoky, A. Savchenko, H. Guven, F. Ponten, G. Klein, and L. Szekely, “Decreased decorin expression in the tumor microenvironment,” Cancer Medicine, vol. 3, no. 3, pp. 485–491, 2014. View at Publisher · View at Google Scholar
  22. S. Liang, J.-F. Xu, W.-J. Cao, H.-P. Li, and C.-P. Hu, “Human decorin regulates proliferation and migration of human lung cancer A549 cells,” Chinese Medical Journal, vol. 126, no. 24, pp. 4736–4741, 2013. View at Publisher · View at Google Scholar · View at Scopus
  23. P. Boström, A. Sainio, T. Kakko, M. Savontaus, M. Söderström, and H. Järveläinen, “Localization of decorin gene expression in normal human breast tissue and in benign and malignant tumors of the human breast,” Histochemistry and Cell Biology, vol. 139, no. 1, pp. 161–171, 2013. View at Publisher · View at Google Scholar · View at Scopus
  24. A. Sainio, M. Nyman, R. Lund et al., “Lack of decorin expression by human bladder cancer cells offers new tools in the therapy of urothelial malignancies,” PLoS ONE, vol. 8, no. 10, Article ID e76190, 2013. View at Publisher · View at Google Scholar · View at Scopus
  25. H. H. Salomäki, A. O. Sainio, M. Söderström, S. Pakkanen, J. Laine, and H. T. Järveläinen, “Differential expression of decorin by human malignant and benign vascular tumors,” Journal of Histochemistry and Cytochemistry, vol. 56, no. 7, pp. 639–646, 2008. View at Publisher · View at Google Scholar · View at Scopus
  26. M. C. Nyman, A. O. Sainio, M. M. Pennanen et al., “Decorin in human colon cancer-localization in vivo and effect on cancer cell behavior in vitro,” Journal of Histochemistry & Cytochemistry, vol. 63, no. 9, pp. 710–720, 2015. View at Publisher · View at Google Scholar
  27. A. D. Theocharis, S. S. Skandalis, T. Neill et al., “Insights into the key roles of proteoglycans in breast cancer biology and translational medicine,” Biochimica et Biophysica Acta—Reviews on Cancer, vol. 1855, no. 2, pp. 276–300, 2015. View at Publisher · View at Google Scholar
  28. S.-Y. Huang, H.-H. Lin, M. Yao et al., “Higher decorin levels in bone marrow plasma are associated with superior treatment response to novel agent-based induction in patients with newly diagnosed myeloma—a retrospective study,” PLoS ONE, vol. 10, no. 9, Article ID e0137552, 2015. View at Publisher · View at Google Scholar
  29. X. Li, A. Pennisi, and S. Yaccoby, “Role of decorin in the antimyeloma effects of osteoblasts,” Blood, vol. 112, no. 1, pp. 159–168, 2008. View at Publisher · View at Google Scholar · View at Scopus
  30. T. Ishiba, M. Nagahara, T. Nakagawa et al., “Periostin suppression induces decorin secretion leading to reduced breast cancer cell motility and invasion,” Scientific Reports, vol. 4, article 7069, 2014. View at Publisher · View at Google Scholar
  31. N. Nemani, L. Santo, H. Eda et al., “Role of decorin in multiple myeloma (MM) bone marrow microenvironment,” Journal of Bone and Mineral Research, vol. 30, no. 3, pp. 533–538, 2015. View at Publisher · View at Google Scholar · View at Scopus
  32. I. B. Kristensen, L. Pedersen, T. B. Rø et al., “Decorin is down-regulated in multiple myeloma and MGUS bone marrow plasma and inhibits HGF-induced myeloma plasma cell viability and migration,” European Journal of Haematology, vol. 91, no. 3, pp. 196–200, 2013. View at Publisher · View at Google Scholar · View at Scopus
  33. D. F. Lee, J. Su, H. S. Kim et al., “Modeling familial cancer with induced pluripotent stem cells,” Cell, vol. 161, no. 2, pp. 240–254, 2015. View at Publisher · View at Google Scholar
  34. T. A. H. Järvinen and E. Ruoslahti, “Target-seeking antifibrotic compound enhances wound healing and suppresses scar formation in mice,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 50, pp. 21671–21676, 2010. View at Publisher · View at Google Scholar · View at Scopus
  35. W. A. Border and E. Ruoslahti, “Transforming growth factor-β in disease: the dark side of tissue repair,” The Journal of Clinical Investigation, vol. 90, no. 1, pp. 1–7, 1992. View at Publisher · View at Google Scholar · View at Scopus
  36. T. A. H. Järvinen and E. Ruoslahti, “Targeted antiscarring therapy for tissue injuries,” Advances in Wound Care, vol. 2, no. 2, pp. 50–54, 2013. View at Publisher · View at Google Scholar
  37. J. Zhu, Y. Li, W. Shen et al., “Relationships between transforming growth factor-beta1, myostatin, and decorin: implications for skeletal muscle fibrosis,” The Journal of Biological Chemistry, vol. 282, no. 35, pp. 25852–25863, 2007. View at Publisher · View at Google Scholar · View at Scopus
  38. R. R. Mohan, J. C. K. Tovey, R. Gupta, A. Sharma, and A. Tandon, “Decorin biology, expression, function and therapy in the cornea,” Current Molecular Medicine, vol. 11, no. 2, pp. 110–128, 2011. View at Publisher · View at Google Scholar · View at Scopus
  39. A. Hildebrand, M. Romaris, M. Rasmussen et al., “Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor β,” Biochemical Journal, vol. 302, no. 2, pp. 527–534, 1994. View at Publisher · View at Google Scholar · View at Scopus
  40. T. Miura, Y. Kishioka, J.-I. Wakamatsu et al., “Decorin binds myostatin and modulates its activity to muscle cells,” Biochemical and Biophysical Research Communications, vol. 340, no. 2, pp. 675–680, 2006. View at Publisher · View at Google Scholar · View at Scopus
  41. T. Kanzleiter, M. Rath, S. W. Görgens et al., “The myokine decorin is regulated by contraction and involved in muscle hypertrophy,” Biochemical and Biophysical Research Communications, vol. 450, no. 2, pp. 1089–1094, 2014. View at Publisher · View at Google Scholar · View at Scopus
  42. H. Järveläinen, P. Puolakkainen, S. Pakkanen et al., “A role for decorin in cutaneous wound healing and angiogenesis,” Wound Repair and Regeneration, vol. 14, no. 4, pp. 443–452, 2006. View at Publisher · View at Google Scholar · View at Scopus
  43. H. Järveläinen, A. Sainio, M. Koulu, T. N. Wight, and R. Penttinen, “Extracellular matrix molecules: potential targets in pharmacotherapy,” Pharmacological Reviews, vol. 61, no. 2, pp. 198–223, 2009. View at Publisher · View at Google Scholar · View at Scopus
  44. T. A. H. Järvinen and E. T. Liu, “HER-2/neu and topoisomerase IIα–simultaneous drug targets in cancer,” Combinatorial Chemistry and High Throughput Screening, vol. 6, no. 5, pp. 455–470, 2003. View at Publisher · View at Google Scholar · View at Scopus
  45. T. A. H. Järvinen and E. T. Liu, “Simultaneous amplification of HER-2 (ERBB2) and topoisomerase IIα (TOP2A) genes—molecular basis for combination chemotherapy in cancer,” Current Cancer Drug Targets, vol. 6, no. 7, pp. 579–602, 2006. View at Publisher · View at Google Scholar · View at Scopus
  46. G. Csordas, M. Santra, C. C. Reed et al., “Sustained down-regulation of the epidermal growth factor receptor by decorin. A mechanism for controlling tumor growth in vivo,” The Journal of Biological Chemistry, vol. 275, no. 42, pp. 32879–32887, 2000. View at Publisher · View at Google Scholar · View at Scopus
  47. R. V. Iozzo, D. K. Moscatello, D. J. McQuillan, and I. Eichstetter, “Decorin is a biological ligand for the epidermal growth factor receptor,” The Journal of Biological Chemistry, vol. 274, no. 8, pp. 4489–4492, 1999. View at Publisher · View at Google Scholar · View at Scopus
  48. D. K. Moscatello, M. Santra, D. M. Mann, D. J. McQuillan, A. J. Wong, and R. V. Iozzo, “Decorin suppresses tumor cell growth by activating the epidermal growth factor receptor,” Journal of Clinical Investigation, vol. 101, no. 2, pp. 406–412, 1998. View at Publisher · View at Google Scholar · View at Scopus
  49. M. Santra, I. Eichstetter, and R. V. Iozzo, “An anti-oncogenic role for decorin. Down-regulation of ErbB2 leads to growth suppression and cytodifferentiation of mammary carcinoma cells,” Journal of Biological Chemistry, vol. 275, no. 45, pp. 35153–35161, 2000. View at Publisher · View at Google Scholar · View at Scopus
  50. M. Santra, C. C. Reed, and R. V. Iozzo, “Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope,” The Journal of Biological Chemistry, vol. 277, no. 38, pp. 35671–35681, 2002. View at Publisher · View at Google Scholar · View at Scopus
  51. S. Buraschi, N. Pal, N. Tyler-Rubinstein, R. T. Owens, T. Neill, and R. V. Iozzo, “Decorin antagonizes Met receptor activity and down-regulates β-catenin and Myc levels,” The Journal of Biological Chemistry, vol. 285, no. 53, pp. 42075–42085, 2010. View at Publisher · View at Google Scholar · View at Scopus
  52. S. Goldoni, A. Humphries, A. Nyström et al., “Decorin is a novel antagonistic ligand of the Met receptor,” The Journal of Cell Biology, vol. 185, no. 4, pp. 743–754, 2009. View at Publisher · View at Google Scholar · View at Scopus
  53. E. Schönherr, C. Sunderkötter, R. V. Iozzo, and L. Schaefer, “Decorin, a novel player in the insulin-like growth factor system,” The Journal of Biological Chemistry, vol. 280, no. 16, pp. 15767–15772, 2005. View at Publisher · View at Google Scholar · View at Scopus
  54. G. A. Khan, G. V. Girish, N. Lala, G. M. Di Guglielmo, and P. K. Lala, “Decorin is a novel VEGFR-2-binding antagonist for the human extravillous trophoblast,” Molecular Endocrinology, vol. 25, no. 8, pp. 1431–1443, 2011. View at Publisher · View at Google Scholar · View at Scopus
  55. N. Nili, A. N. Cheema, F. J. Giordano et al., “Decorin inhibition of PDGF-stimulated vascular smooth muscle cell function: potential mechanism for inhibition of intimal hyperplasia after balloon angioplasty,” The American Journal of Pathology, vol. 163, no. 3, pp. 869–878, 2003. View at Publisher · View at Google Scholar · View at Scopus
  56. C. Cabello-Verrugio and E. Brandan, “A novel modulatory mechanism of transforming growth factor-β signaling through decorin and LRP-1,” The Journal of Biological Chemistry, vol. 282, no. 26, pp. 18842–18850, 2007. View at Publisher · View at Google Scholar · View at Scopus
  57. C. Cabello-Verrugio, C. Santander, C. Cofré, M. J. Acuña, F. Melo, and E. Brandan, “The internal region leucine-rich repeat 6 of decorin interacts with low density lipoprotein receptor-related protein-1, modulates Transforming Growth Factor (TGF)-β-dependent signaling, and inhibits TGF-β-dependent fibrotic response in skeletal muscles,” The Journal of Biological Chemistry, vol. 287, no. 9, pp. 6773–6787, 2012. View at Publisher · View at Google Scholar · View at Scopus
  58. L. Desnoyers, D. Arnott, and D. Pennica, “WISP-1 binds to decorin and biglycan,” The Journal of Biological Chemistry, vol. 276, no. 50, pp. 47599–47607, 2001. View at Publisher · View at Google Scholar · View at Scopus
  59. C. Vial, J. Gutiérrez, C. Santander, D. Cabrera, and E. Brandan, “Decorin interacts with connective tissue growth factor (CTGF)/CCN2 by LRR12 inhibiting its biological activity,” Journal of Biological Chemistry, vol. 286, no. 27, pp. 24242–24252, 2011. View at Publisher · View at Google Scholar
  60. P. Stapor, X. Wang, J. Goveia, S. Moens, and P. Carmeliet, “Angiogenesis revisited—role and therapeutic potential of targeting endothelial metabolism,” Journal of Cell Science, vol. 127, part 20, pp. 4331–4341, 2014. View at Publisher · View at Google Scholar · View at Scopus
  61. J. Goveia, P. Stapor, and P. Carmeliet, “Principles of targeting endothelial cell metabolism to treat angiogenesis and endothelial cell dysfunction in disease,” EMBO Molecular Medicine, vol. 6, no. 9, pp. 1105–1120, 2014. View at Publisher · View at Google Scholar · View at Scopus
  62. T. Neill, L. Schaefer, and R. V. Iozzo, “Instructive roles of extracellular matrix on autophagy,” The American Journal of Pathology, vol. 184, no. 8, pp. 2146–2153, 2014. View at Publisher · View at Google Scholar · View at Scopus
  63. T. Neill, H. R. Jones, Z. Crane-Smith, R. T. Owens, L. Schaefer, and R. V. Iozzo, “Decorin induces rapid secretion of thrombospondin-1 in basal breast carcinoma cells via inhibition of Ras homolog gene family, member A/Rho-associated coiled-coil containing protein kinase 1,” The FEBS Journal, vol. 280, no. 10, pp. 2353–2368, 2013. View at Publisher · View at Google Scholar · View at Scopus
  64. T. Neill, H. Painter, S. Buraschi et al., “Decorin antagonizes the angiogenic network: concurrent inhibition of met, hypoxia inducible factor 1α, vascular endothelial growth factor A, and induction of thrombospondin-1 and tiMP3,” The Journal of Biological Chemistry, vol. 287, no. 8, pp. 5492–5506, 2012. View at Publisher · View at Google Scholar · View at Scopus
  65. S. Buraschi, T. Neill, A. Goyal et al., “Decorin causes autophagy in endothelial cells via Peg3,” Proceedings of the National Academy of Sciences of the United States of America, vol. 110, no. 28, pp. E2582–E2591, 2013. View at Publisher · View at Google Scholar · View at Scopus
  66. E. Schönherr, C. Sunderkötter, L. Schaefer et al., “Decorin deficiency leads to impaired angiogenesis in injured mouse cornea,” Journal of Vascular Research, vol. 41, no. 6, pp. 499–508, 2004. View at Publisher · View at Google Scholar · View at Scopus
  67. M. Santra, S. Santra, J. Zhang, and M. Chopp, “Ectopic decorin expression up-regulates VEGF expression in mouse cerebral endothelial cells via activation of the transcription factors Sp1, HIF1α, and Stat3,” Journal of Neurochemistry, vol. 105, no. 2, pp. 324–337, 2008. View at Publisher · View at Google Scholar · View at Scopus
  68. L. R. Fiedler, E. Schönherr, R. Waddington et al., “Decorin regulates endothelial cell motility on collagen I through activation of insulin-like growth factor I receptor and modulation of α2β1 integrin activity,” Journal of Biological Chemistry, vol. 283, no. 25, pp. 17406–17415, 2008. View at Publisher · View at Google Scholar · View at Scopus
  69. R. A. Scott, A. K. Ramaswamy, K. Park, and A. Panitch, “Decorin mimic promotes endothelial cell health in endothelial monolayers and endothelial-smooth muscle co-cultures,” Journal of Tissue Engineering and Regenerative Medicine, 2015. View at Publisher · View at Google Scholar
  70. D. J. Nolan, M. Ginsberg, E. Israely et al., “Molecular signatures of tissue-specific microvascular endothelial cell heterogeneity in organ maintenance and regeneration,” Developmental Cell, vol. 26, no. 2, pp. 204–219, 2013. View at Publisher · View at Google Scholar · View at Scopus
  71. H. Järveläinen, A. Sainio, and T. N. Wight, “Pivotal role for decorin in angiogenesis,” Matrix Biology, vol. 43, pp. 15–26, 2015. View at Publisher · View at Google Scholar
  72. C. C. Reed, J. Gauldie, and R. V. Iozzo, “Suppression of tumorigenicity by adenovirus-mediated gene transfer of decorin,” Oncogene, vol. 21, no. 23, pp. 3688–3695, 2002. View at Publisher · View at Google Scholar · View at Scopus
  73. K. Shintani, A. Matsumine, K. Kusuzaki et al., “Decorin suppresses lung metastases of murine osteosarcoma,” Oncology Reports, vol. 19, no. 6, pp. 1533–1539, 2008. View at Google Scholar · View at Scopus
  74. J. G. Tralhão, L. Schaefer, M. Micegova et al., “In vivo selective and distant killing of cancer cells using adenovirus-mediated decorin gene transfer,” The FASEB Journal, vol. 17, no. 3, pp. 464–466, 2003. View at Google Scholar · View at Scopus
  75. K. Araki, H. Wakabayashi, K. Shintani et al., “Decorin suppresses bone metastasis in a breast cancer cell line,” Oncology, vol. 77, no. 2, pp. 92–99, 2008. View at Publisher · View at Google Scholar · View at Scopus
  76. Y. Yang, W. W. Xu, T. Neill et al., “Systemic delivery of an oncolytic adenovirus expressing decorin for the treatment of breast cancer bone metastases,” Human Gene Therapy, 2015. View at Publisher · View at Google Scholar
  77. W. Xu, T. Neill, Y. Yang et al., “The systemic delivery of an oncolytic adenovirus expressing decorin inhibits bone metastasis in a mouse model of human prostate cancer,” Gene Therapy, vol. 22, no. 3, pp. 31–40, 2015. View at Publisher · View at Google Scholar · View at Scopus
  78. H.-I. Ma, D.-Y. Hueng, H.-A. Shui et al., “Intratumoral decorin gene delivery by AAV vector inhibits brain glioblastomas and prolongs survival of animals by inducing cell differentiation,” International Journal of Molecular Sciences, vol. 15, no. 3, pp. 4393–4414, 2014. View at Publisher · View at Google Scholar · View at Scopus
  79. Y. Hu, H. Sun, R. T. Owens et al., “Decorin suppresses prostate tumor growth through inhibition of epidermal growth factor and androgen receptor pathways,” Neoplasia, vol. 11, no. 10, pp. 1042–1053, 2009. View at Publisher · View at Google Scholar · View at Scopus
  80. Y. Na, J. W. Choi, D. Kasala et al., “Potent antitumor effect of neurotensin receptor-targeted oncolytic adenovirus co-expressing decorin and Wnt antagonist in an orthotopic pancreatic tumor model,” Journal of Controlled Release, 2015. View at Publisher · View at Google Scholar
  81. D. S. Grant, C. Yenisey, R. W. Rose, M. Tootell, M. Santra, and R. V. Iozzo, “Decorin suppresses tumor cell-mediated angiogenesis,” Oncogene, vol. 21, no. 31, pp. 4765–4777, 2002. View at Publisher · View at Google Scholar · View at Scopus
  82. D. G. Seidler, S. Goldoni, C. Agnew et al., “Decorin protein core inhibits in vivo cancer growth and metabolism by hindering epidermal growth factor receptor function and triggering apoptosis via caspase-3 activation,” Journal of Biological Chemistry, vol. 281, no. 36, pp. 26408–26418, 2006. View at Publisher · View at Google Scholar · View at Scopus
  83. K. Imai, A. Hiramatsu, D. Fukushima, M. D. Pierschbacher, and Y. Okada, “Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-β1 release,” Biochemical Journal, vol. 322, no. 3, pp. 809–814, 1997. View at Publisher · View at Google Scholar · View at Scopus
  84. C. Gendron, M. Kashiwagi, N. H. Lim et al., “Proteolytic activities of human ADAMTS-5: comparative studies with ADAMTS-4,” The Journal of Biological Chemistry, vol. 282, no. 25, pp. 18294–18306, 2007. View at Publisher · View at Google Scholar · View at Scopus
  85. T. Mimura, K. Y. Han, T. Onguchi et al., “MT1-MMP-mediated cleavage of decorin in corneal angiogenesis,” Journal of Vascular Research, vol. 46, no. 6, pp. 541–550, 2009. View at Publisher · View at Google Scholar · View at Scopus
  86. M. J. Peffers, D. J. Thornton, and P. D. Clegg, “Characterization of neopeptides in equine articular cartilage degradation,” Journal of Orthopaedic Research, 2015. View at Publisher · View at Google Scholar
  87. L. G. Parkinson, A. Toro, H. Zhao, K. Brown, S. J. Tebbutt, and D. J. Granville, “Granzyme B mediates both direct and indirect cleavage of extracellular matrix in skin after chronic low-dose ultraviolet light irradiation,” Aging Cell, vol. 14, no. 1, pp. 67–77, 2015. View at Publisher · View at Google Scholar · View at Scopus
  88. L. S. Ang, W. A. Boivin, S. J. Williams et al., “Serpina3n attenuates granzyme B-mediated decorin cleavage and rupture in a murine model of aortic aneurysm,” Cell Death and Disease, vol. 2, no. 9, article e209, 2011. View at Publisher · View at Google Scholar · View at Scopus
  89. W. A. Boivin, M. Shackleford, A. V. Hoek et al., “Granzyme B cleaves decorin, biglycan and soluble betaglycan, releasing active transforming growth factor-β1,” PLoS ONE, vol. 7, no. 3, Article ID e33163, 2012. View at Publisher · View at Google Scholar · View at Scopus
  90. Y. Li, W. Xia, Y. Liu, H. A. Remmer, J. Voorhees, and G. J. Fisher, “Solar ultraviolet irradiation induces decorin degradation in human skin likely via neutrophil elastase,” PLoS ONE, vol. 8, no. 8, Article ID e72563, 2013. View at Publisher · View at Google Scholar · View at Scopus
  91. L. Schaefer, “Complexity of danger: the diverse nature of damage-associated molecular patterns,” Journal of Biological Chemistry, vol. 289, no. 51, pp. 35237–35245, 2014. View at Publisher · View at Google Scholar · View at Scopus
  92. E. Ruoslahti, Y. Yamaguchi, A. Hildebrand, and W. A. Border, “Extracellular matrix/growth factor interactions,” Cold Spring Harbor Symposia on Quantitative Biology, vol. 57, pp. 309–316, 1992. View at Publisher · View at Google Scholar · View at Scopus
  93. D. A. Carrino, S. Mesiano, N. M. Barker, W. W. Hurd, and A. I. Caplan, “Proteoglycans of uterine fibroids and keloid scars: similarity in their proteoglycan composition,” Biochemical Journal, vol. 443, no. 2, pp. 361–368, 2012. View at Publisher · View at Google Scholar · View at Scopus
  94. D. A. Carrino, P. Önnerfjord, J. D. Sandy et al., “Age-related changes in the proteoglycans of human skin. Specific cleavage of decorin to yield a major catabolic fragment in adult skin,” The Journal of Biological Chemistry, vol. 278, no. 19, pp. 17566–17572, 2003. View at Publisher · View at Google Scholar · View at Scopus
  95. D. A. Carrino, A. Calabro, A. B. Darr et al., “Age-related differences in human skin proteoglycans,” Glycobiology, vol. 21, no. 2, pp. 257–268, 2011. View at Publisher · View at Google Scholar · View at Scopus
  96. T. A. H. Järvinen and E. Ruoslahti, “Uusi lääkeaine estää arven muodostusta,” Duodecim, vol. 127, no. 2, pp. 146–147, 2011. View at Google Scholar
  97. T. A. H. Järvinen, “Design of target-seeking antifibrotic compounds,” Methods in Enzymology, vol. 509, pp. 243–261, 2012. View at Publisher · View at Google Scholar · View at Scopus
  98. T. A. H. Järvinen, U. May, and S. Prince, “Systemically administered, target organ-specific therapies for regenerative medicine,” International Journal of Molecular Sciences, vol. 16, no. 10, pp. 23556–23571, 2015. View at Publisher · View at Google Scholar
  99. T. A. H. Järvinen and E. Ruoslahti, “Molecular changes in the vasculature of injured tissues,” The American Journal of Pathology, vol. 171, no. 2, pp. 702–711, 2007. View at Publisher · View at Google Scholar · View at Scopus
  100. T. Urakami, T. A. H. Järvinen, M. Toba et al., “Peptide-directed highly selective targeting of pulmonary arterial hypertension,” The American Journal of Pathology, vol. 178, no. 6, pp. 2489–2495, 2011. View at Publisher · View at Google Scholar · View at Scopus
  101. M. Toba, A. Alzoubi, K. O'Neill et al., “A novel vascular homing peptide strategy to selectively enhance pulmonary drug efficacy in pulmonary arterial hypertension,” American Journal of Pathology, vol. 184, no. 2, pp. 369–375, 2014. View at Publisher · View at Google Scholar · View at Scopus
  102. N. Gupta, B. Patel, K. Nahar, and F. Ahsan, “Cell permeable peptide conjugated nanoerythrosomes of fasudil prolong pulmonary arterial vasodilation in PAH rats,” European Journal of Pharmaceutics and Biopharmaceutics, vol. 88, no. 3, pp. 1046–1055, 2014. View at Publisher · View at Google Scholar · View at Scopus
  103. N. Gupta, H. M. Ibrahim, and F. Ahsan, “Peptide-micelle hybrids containing fasudil for targeted delivery to the pulmonary arteries and arterioles to treat pulmonary arterial hypertension,” Journal of Pharmaceutical Sciences, vol. 103, no. 11, pp. 3743–3753, 2014. View at Publisher · View at Google Scholar · View at Scopus
  104. K. Nahar, S. Absar, N. Gupta et al., “Peptide-coated liposomal fasudil enhances site specific vasodilation in pulmonary arterial hypertension,” Molecular Pharmaceutics, vol. 11, no. 12, pp. 4374–4384, 2014. View at Publisher · View at Google Scholar · View at Scopus
  105. N. Gupta, F. I. Al-Saikhan, B. Patel, J. Rashid, and F. Ahsan, “Fasudil and SOD packaged in peptide-studded-liposomes: properties, pharmacokinetics and ex-vivo targeting to isolated perfused rat lungs,” International Journal of Pharmaceutics, vol. 488, no. 1-2, pp. 33–43, 2015. View at Publisher · View at Google Scholar
  106. T. J. Kean, L. Duesler, R. G. Young et al., “Development of a peptide-targeted, myocardial ischemia-homing, mesenchymal stem cell,” Journal of Drug Targeting, vol. 20, no. 1, pp. 23–32, 2012. View at Publisher · View at Google Scholar · View at Scopus
  107. T. J. Kean, P. Lin, A. I. Caplan, and J. E. Dennis, “MSCs: delivery routes and engraftment, cell-targeting strategies, and immune modulation,” Stem Cells International, vol. 2013, Article ID 732742, 13 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus