MMP7 cleaves OPTC

Stable Identifier
R-HSA-8940561
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Opticin (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). OPTC 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). MMP7 cleaves recombinant human OPTN at four positions, A20/S21LP (removing the signal peptide), E32/Q33, T87/S88, and G114/L115.

Literature References
PubMed ID Title Journal Year
23845380 Characterization of opticin digestion by proteases involved in osteoarthritis development

Tío, L, Martel-Pelletier, J, Pelletier, JP, Bishop, PN, Roughley, P, Farran, A, Benito, P, Monfort, J

Joint Bone Spine 2014
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
metalloendopeptidase activity of MMP7(95-267) [extracellular region]
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Activity
Orthologous Events
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