SPARC deficiency results in improved surgical survival in a novel mouse model of glaucoma filtration surgery

PLoS ONE

Volumn 5, Issue 2, 2010, Pages

  Seet, Li Fong ^a   Su, Roseline ^a   Barathi, V A ^a   Lee, Wing Sum ^a   Poh, Rebekah ^a   Heng, Yee Meng ^d   Manser, Ed ^d   Vithana, Eranga N ^a   Aung, Tin ^a,b,c   Weaver, Matt ^e   Sage, E Helene ^e   Wong, Tina T ^a,b,c  

^a SINGAPORE EYE RESEARCH INSTITUTE   (Singapore)

^b SINGAPORE NATIONAL EYE CENTRE   (Singapore)

^c NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^d INSTITUTE OF MEDICAL BIOLOGY   (Singapore)

^e BENAROYA RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN FIBRIL; OSTEONECTIN; PROTEIN; RNA; COLLAGEN; SCLEROPROTEIN; TRANSFORMING GROWTH FACTOR BETA2;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; C57BL 6 MOUSE; CONJUNCTIVA; CONTROLLED STUDY; EXTRACELLULAR MATRIX; FIBROBLAST; FILTERING OPERATION; GENE EXPRESSION; GLAUCOMA DRAINAGE IMPLANT; IMMUNOLOCALIZATION; IN VITRO SELECTION; MOUSE; NONHUMAN; POSTOPERATIVE PERIOD; PROTEIN ANALYSIS; PROTEIN DEPLETION; RNA ISOLATION; SURGICAL WOUND; SURVIVAL; SURVIVAL RATE; WESTERN BLOTTING; WOUND HEALING; ZYMOGRAPHY; ANIMAL; C57BL MOUSE; CELL CULTURE; CELL DIFFERENTIATION; CONFOCAL MICROSCOPY; CYTOLOGY; DISEASE MODEL; DRUG EFFECT; GENETICS; GLAUCOMA; HUMAN; METABOLISM; METHODOLOGY; MORTALITY; MOUSE MUTANT; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; TRANSMISSION ELECTRON MICROSCOPY; ULTRASTRUCTURE;

MUS;

ANIMALS; BLOTTING, WESTERN; CELL DIFFERENTIATION; CELLS, CULTURED; COLLAGEN; CONJUNCTIVA; DISEASE MODELS, ANIMAL; EXTRACELLULAR MATRIX PROTEINS; FIBROBLASTS; FILTERING SURGERY; GENE EXPRESSION; GLAUCOMA; HUMANS; MICE; MICE, INBRED C57BL; MICE, KNOCKOUT; MICROSCOPY, CONFOCAL; MICROSCOPY, ELECTRON, TRANSMISSION; OSTEONECTIN; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SURVIVAL RATE; TRANSFORMING GROWTH FACTOR BETA2;

EID: 77949661954     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0009415     Document Type: Article

References (48)

1. Resnikoff S, Pascolini D, Etya'ale D, Kocur I, Pararajasegaram R, et al. (2004) Global data on visual impairment in the year 2002. Bull World Health Organ 82: 844-851.
2. Quigley HA, Broman A (2006) The number of persons with glaucoma worldwide in 2010 and 2020. Br J Ophthalmol 90: 151-156.
3. The AGIS Investigators (2000) The advanced glaucoma intervention study (AGIS): 7. The relationship between control of intraocular pressure and visual field deterioration. Am J Ophthalmol 130: 429-440.
4. Reddick R, Merritt JC, Ross G, Avery A, Peiffer RL (1985) Myofibroblasts in filtration operations. Ann Ophthalmol 17: 200-203.
5. The Fluorouracil Filtering Surgery Study Group (1989) Fluorouracil filtering surgery study one-year follow-up. Am J Ophthalmol 108: 625-635.
6. Kitazawa Y, Kawase K, Matsushita H, Minobe M (1991) Trabeculectomy with mitomycin. A comparative study with fluorouracil. Arch Ophthalmol 109: 1693-1698.
7. Skuta GL, Beeson CC, Higginbotham EJ (1992) Intraoperative mitomycin versus postoperative 5-fluorouracil in high- risk glaucoma filtering surgery. Ophthalmol 99: 438-444.
8. Higginbotham EJ, Stevens RK, Musch DC (1996) Bleb-related endophthalmitis after trabeculectomy with mitomycin C. Ophthalmol 103: 650-656.
9. Greenfield DS, Suner IJ, Miller MP (1996) Endophthalmitis after filtering surgery with mitomycin. Arch Ophthalmol 114: 943-949.
10. Brekken RA, Sage EH (2001) SPARC, a matricellular protein: at the crossroads of cell-matrix communication. Matrix Biol 19: 816-827.
11. Bornstein P, Sage EH (2002) Matricellular proteins: extracellular modulators of cell function. Curr Opin Cell Biol 14: 608-616.
12. Zhou XD, Tan FK, Reveille JD, Wallis D, Milewicz DM, et al. (2002) Association of novel polymorphisms with the expression of SPARC in normal fibroblasts and with susceptibility to scleroderma. Arthritis Rheum 46: 2990-2999.
13. Zhou X, Tan FK, Guo X, Arnett FC (2006) Attenuation of collagen production with small interfering RNA of SPARC in cultured fibroblasts from the skin of patients with scleroderma. Arthritis Rheum 54: 2626-2631.
14. Kuhn C, Mason RJ (1995) Immunolocalization of SPARC, tenascin, and thrombospondin in pulmonary fibrosis. Am J Pathol 147: 1759-1769.
15. Pichler RH, Hugo C, Shankland SJ, Reed MJ, Bassuk JA, et al. (1996) SPARC is expressed in renal interstitial fibrosis and in renal vascular injury. Kidney Int 50: 1978-1989.
16. Kanauchi M, Nishioka M, Dohi K (2000) Secreted protein acidic and rich in cysteine (SPARC) in patients with diabetic nephropathy and tubulointerstitial injury. Diabetologia 43: 1076-1077.
17. Frizell E, Liu SL, Abraham A, Ozaki I, Eghbali M, et al. (1995) Expression of SPARC in normal and fibrotic livers. Hepatol 21: 847-854.
18. Dhore CR, Cleutjens JPM, Lutgens E, Cleutjens KBJM, Geusens PPM, et al. (2001) Differential expression of bone matrix regulatory proteins in human atherosclerotic plaques. Arterioscler Thromb Vasc Biol 21: 1998-2003.
19. Strandjord TP, Madtes DK, Weiss DJ, Sage EH (1999) Collagen accumulation is decreased in SPARC-null mice with bleomycin-induced pulmonary fibrosis. Am J Physiol 277: 628-635.
20. Bradshaw AD, Puolakkainen P, Dasgupta J, Davidson JM, Wight TN, et al. (2003) SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength. J Invest Dermat 120: 949-955.
21. Arora PD, Narani N, McCulloch CA (1999) The compliance of collagen gels regulates transforming growth factor-b induction of α-smooth muscle actin in fibroblasts. Am J Pathol 154: 871-882.
22. Junqueira LC, Bignolas G, Brentani RR (1979) Picrosirius staining plus polarization microscopy, a specific method for collagen detection in tissue sections. Histochem J 11: 447-455.
23. Mehta JS, Chua J, Poh R, Beuerman RW, Tan D (2008) Primary graft failure after descemet-stripping automated endothelial keratoplasty. Cornea 27: 722-726.
24. Branton MH, Kopp JB (1999) TGF-β and fibrosis. Microbes and Infection 1: 1349-1365.
25. Willis BC, Borok Z (2007) TGF-β-induced EMT: mechanisms and implications for fibrotic lung disease. Am J Physiol Lung Cell Mol Physiol 293: L525-L534.
26. Clark RAF (1996) Wound repair: overview and general considerations. In: Clark RAF, ed. The Molecular and Cellular Biology of Wound Repair. New York: Plenum Press. pp 3-50 .
27. Tamariz E, Grinnell F (2002) Modulation of fibroblast morphology and adhesion during collagen matrix remodeling. Mol Biol Cell 13: 3915-3929.
28. Grinnell F (1994) Fibroblasts, myofibroblasts, and wound contraction. J Cell Biol 124: 401-404.
29. Grinnell F (2003) Fibroblast biology in three-dimensional collagen matrices. Trends Cell Biol 13: 264-269.
30. Ehrlich HP, Rajaratnam JB (1990) Cell locomotion forces versus cell contraction forces for collagen lattice contraction: an in vitro model of wound contraction. Tiss Cell 22: 407-417.
31. Daniels JT, Schultz GS, Blalock TD, Garrett Q, Grotendorst GR, et al. (2003) Mediation of transforming growth factor-β1-stimulated matrix contraction by fibroblasts. Am J Pathol 163: 2043-2052.
32. Sato H, Takino T, Okada Y, Cao J, Shinagawa A, et al. (1994) A matrix metalloproteinase expressed on the surface of invasive tumor cells. Nature 370: 61-65.
33. Diegelmann R (1997) Cellular and biochemical aspects of normal and abnormal wound healing: an overview. J Urol 157: 298-302.
34. Esson DW, Neelankantan A, Iyer SA, Blalock TD, Balasubramian L, et al. (2004) Expression of connective tissue growth factor after glaucoma filtration surgery in a rabbit model. Invest Ophthalmol Vis Sci 45: 485-491.
35. Rentz TJ, Poobalarahi F, Bornstein P, Sage EH, Bradshaw AD (2007) SPARC regulates processing of procollagen I and collagen fibrillogenesis in dermal fibroblasts. J Biol Chem 282: 22062-22071.
36. Basu A, Kligman LH, Samulewicz SJ, Howe CC (2001) Impaired wound healing in mice deficient in a matricellular protein SPARC (osteonectin, BM-40). BMC Cell Biol 2: 15.
37. Schellings MWM, Vanhoutte D, Swinnen M, Cleutjens JP, Debets J, et al. (2008) Absence of SPARC results in increased cardiac rupture and dysfunction after acute myocardial infarction. J Exp Med 206: 113-123.
38. Martinek N, Shahab J, Sodek J, Ringuette M (2007) Is SPARC an evolutionarily conserved collagen chaperone? J Dent Res 86: 296-305.
39. Ramirez F, Tanaka S, Bou-Gharios G (2006) Transcriptional regulation of the human α2(I) collagen gene (COL1A2), an informative model system to study fibrotic diseases. Matrix Biol 25: 365-372.
40. Ko MK, Kay EP (2005) Regulatory role of FGF-2 on type I collagen expression during endothelial mesenchymal transformation. Invest Ophthalmol Vis Sci 46: 4495-4503.
41. Shi Y, Massagué J (2003) Mechanisms of TGF-β signaling from cell membrane to the nucleus. Cell 113: 685-700.
42. Itoh S, Thorikay M, Kowanetz M, Moustakas A, Itoh F, et al. (2003) Elucidation of Smad requirement in transforming growth factor-beta type I receptor-induced responses. J Biol Chem 278: 3751-3761.
43. Schiemann BJ, Neil JR, Schiemann WP (2003) SPARC inhibits epithelial cell proliferation in part through stimulation of the transforming growth factor-β-signaling system. Mol Biol Cell 14: 3977-3988.
44. Moretti FA, Chauhan AK, Iaconcig A, Porro F, Baralle FE, et al. (2007) A major fraction of fibronectin present in the extracellular matrix of tissues is plasma-derived. J Biol Chem 282: 28057-28062.
45. McClung HM, Thomas SL, Osenkowski P, Toth M, Menon P, et al. (2007) SPARC upregulates MT1-MMP expression, MMP-2 activation, and the secretion and cleavage of Galectin-3 in U87MG glioma cells. Neurosci Lett 419: 172-177.
46. Seltzer JL, Lee A-Y, Akers KT, Sudbeck B, Southon E, et al. (1994) Activation of 72-kDa type IV collagenase/gelatinase by normal fibroblasts in collagen lattices is mediated by integrin receptors but is not related to lattice contraction. Exp Cell Res 213: 365-374.
47. Deryugina EI, Bourdon MA, Reisfeld RA, Strongin A (1998) Remodeling of collagen matrix by human tumor cells requires activation and cell surface association of matrix metalloproteinase-2. Cancer Res 58: 3743-3750.
48. Wynn TA (2007) Common and unique mechanisms regulate fibrosis in various fibroproliferative diseases. J Clin Invest 117: 524-529.