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Details on Person Opticin (OPTC) is a a member of the small leucine-rich repea...

Class:IdSummation:8942312
_displayNameOpticin (OPTC) is a a member of the small leucine-rich repea...
_timestamp2016-10-12 13:25:28
created[InstanceEdit:8942313] Jupe, Steve, 2016-10-12
literatureReference[LiteratureReference:8940527] Characterization of opticin digestion by proteases involved in osteoarthritis development
[LiteratureReference:8940555] Opticin exerts its anti-angiogenic activity by regulating extracellular matrix adhesiveness
[LiteratureReference:8940558] Characterization of opticin and evidence of stable dimerization in solution
[LiteratureReference:8940528] Identification of opticin, a member of the small leucine-rich repeat proteoglycan family, in human articular tissues: a novel target for MMP-13 in osteoarthritis
[LiteratureReference:8940545] Identification in vitreous and molecular cloning of opticin, a novel member of the family of leucine-rich repeat proteins of the extracellular matrix
[LiteratureReference:8940519] Structural macromolecules and supramolecular organisation of the vitreous gel
[LiteratureReference:8940557] Opticin production is reduced by hypoxia and VEGF in human retinal pigment epithelium via MMP-2 activation
[LiteratureReference:8942316] Opticin, a small leucine-rich proteoglycan, is uniquely expressed and translocated to the nucleus of chronic lymphocytic leukemia cells
modified[InstanceEdit:8942323] Jupe, Steve, 2016-10-12
textOpticin (OPTC) is a a member of the small leucine-rich repeat proteoglycan family (Reardon et al. 2000). It is found in the vitreous cavity of the eye where it co-localizes with the fine network of collagen fibrils that maintains the gel state of the vitreous and the inner-limiting lamina, and in other tissues, including the brain, heart, and cartilage (Le Goff et al. 2012). It forms a homodimer in solution through its leucine-rich repeats (Le Goff et al. 2003). Opticin has anti-angiogenic activity which is mediated by binding to vitreous collagen fibrils, which are composed of collagens II, IX, and V/XI (Bishop 2000). This binding competitively inhibits endothelial cell interactions with collagen I via Alpha-1Beta-1and Alpha-2Beta-1 integrins, preventing proangiogenic signaling via these integrins (Le Goff et al. 2012). OPTC is expressed and translocated to the nucleus of chronic lymphocytic leukemia cells (Mikaelsson et al.2013).

OPTC can be degraded by Matrix metalloprotease (MMP) -1, -2, -3, -7, -8, -9, -13 and by ADAMTS-4 and ADAMTS-5, with MMP2 and MMP7 having highest activity towards the recombinant protein (Montfort et al. 2008, Ma et al. 2012, Tio et al. 2014). MMP13 cleaves recombinant bovine OPTC at G104/L105 (major product), and P109/A110 (minor product) (Montfort et al. 2008).The major cleavage site corresponds to G114/L115 in human opticin.
(summation)[Reaction:8942302] MMP13 cleaves OPTC [Homo sapiens]
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