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. 1995 Dec 1;312(Pt 2):377–384. doi: 10.1042/bj3120377

Glial hyaluronate-binding protein: a product of metalloproteinase digestion of versican?

G Perides 1, R A Asher 1, M W Lark 1, W S Lane 1, R A Robinson 1, A Bignami 1
PMCID: PMC1136273  PMID: 8526845

Abstract

Glial hyaluronate-binding protein (GHAP) is a 60 kDa glycoprotein with an amino acid sequence identical to that of the hyaluronate-binding region of versican, a large fibroblast aggregating proteoglycan found in the brain. Both GHAP and versican were identified by immunoblot in bovine brain extracts prepared only minutes after death. Human recombinant collagenase, stromelysin, mouse gelatinase and gelatinases isolated from human brain by affinity chromatography digest versican and give rise to a polypeptide with electrophoretic mobility identical to GHAP. Immunoblot analysis, peptide mapping and C-terminal amino acid sequencing indicate that the polypeptide generated by digestion with human brain gelatinases is identical to GHAP. We suggest that GHAP is a naturally occurring versican degradation product.

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