May 2004
Volume 45, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2004
The anti–angiogenic effects of opticin, a glycoprotein in the vitreous humour of the eye.
Author Affiliations & Notes
  • M.M. Le Goff
    Research Group in Eye & Vision Sciences and Wellcome Trust Centre for Cell–Matrix Biology, University of Manchester, Manchester, United Kingdom
  • M.A. Slevin
    Manchester Metropolitan University, Manchester, United Kingdom
  • P.N. Bishop
    Research Group in Eye & Vision Sciences and Wellcome Trust Centre for Cell–Matrix Biology, University of Manchester, Manchester, United Kingdom
  • Footnotes
    Commercial Relationships  M.M. Le Goff, None; M.A. Slevin, None; P.N. Bishop, None.
  • Footnotes
    Support  The Wellcome Trust
Investigative Ophthalmology & Visual Science May 2004, Vol.45, 1915. doi:
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      M.M. Le Goff, M.A. Slevin, P.N. Bishop; The anti–angiogenic effects of opticin, a glycoprotein in the vitreous humour of the eye. . Invest. Ophthalmol. Vis. Sci. 2004;45(13):1915.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Abstract: : Purpose: Opticin is an extracellular matrix glycoprotein and a member of the small leucine–rich repeat protein/proteoglycan family (JBC, 2000, 275: 2123–2129). Opticin is highly expressed in the eye throughout life and localises to the vitreous humour. The vitreous humour is an avascular extracellular matrix that normally possesses anti–angiogenic properties and the purpose of this study was to determine whether opticin contributes to these properties. Methods: Recombinant bovine opticin was generated in 293–EBNA cells and purified from the conditioned media. Bovine aortic endothelial cells (BAEC) were used in in–vitro VEGF and FGF–2 stimulated proliferation and sprouting assays. The interactions between opticin and VEGF or FGF–2 were studied using solid phase assays. Results: With increasing concentrations of opticin there was a progressive reduction in both VEGF– and FGF–2–induced BAEC proliferation and sprouting, with almost complete inhibition being attained at between 10–25 µg/ml of opticin. Opticin bound directly to both VEGF (apparent Kd=38 nM) and FGF–2 (apparent Kd=34 nM). Conclusions: These results demonstrate that opticin has anti–angiogenic properties and inhibits the actions of both VEGF and FGF–2. A potential mechanism of action is direct binding to these growth factors to inhibit their actions. Opticin may play a key role in both the development of the eye (i.e. regression of the primary hyaloid vascular system) and in protection against vitreoretinal diseases such as proliferative diabetic retinopathy.

Keywords: vitreous • extracellular matrix 
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