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Opticin is an anti‐angiogenic component of the vitreous humour of the eye
Author(s) -
Slevin Mark,
Le Goff Magali,
Sutton Matthew,
West David,
Bishop Paul
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.a980-a
Subject(s) - angiogenesis , extracellular matrix , fibroblast growth factor , microbiology and biotechnology , neovascularization , matrigel , chemistry , medicine , biology , cancer research , receptor
Angiogenesis plays a key role in ocular development and disease. Normally following regression of the hyaloid vascular system the vitreous humour is avascular and anti‐angiogenic. However, in diseases such as proliferative diabetic retinopathy, new blood vessels grow from the retina into the vitreous humour potentially leading to blindness. Opticin is a glycoprotein that was first isolated from vitreous humour of the eye and is a member of the extracellular matrix small leucine‐rich repeat proteoglycan/protein family. As it is highly expressed in the eye throughout life we hypothesised that it contributes towards the anti‐angiogenic properties of the vitreous humour. Purified recombinant opticin was generated as previously described (Le Goff et al. JBC 2003, 278:45280). Using the recombinant opticin we show that opticin potently inhibits VEGF and FGF‐2‐induced human retinal endothelial cell and bovine aortic endothelial cell proliferation, migration, formation of tube‐like structures in matrigel and collagen, and invasion. In vivo studies showed that opticin significantly decreased FGF‐2 and VEGF induced angiogenesis in chick chorioallantoic membrane assays. We also demonstrate that opticin decreases signalling through ERK1/2. These observations suggest that opticin is a key regulator of angiogenesis in the eye and further studies will elucidate its mechanisms of action.