cDNA cloning and the identification of an aggrecanase-like cleavage site in rat brevican

Hidekazu Yamada, Ken Watanabe, Motoyuki Shimonaka, Motoo Yamasaki, Yu Yamaguchi

    Research output: Contribution to journalArticle

    43 Citations (Scopus)

    Abstract

    Brevican is a member of the aggrecan family of chondroitin sulfate proteoglycans that is predominantly expressed in the nervous system. In the adult brain, the brevican core protein undergoes proteolytic cleavage and exists as a 145-kDa full-length form and an 80-kDa C-terminal fragment. We have determined the complete primary structure of rat brevican and the N-terminal amino acid sequence of the 80-kDa fragment. The results demonstrate that the cleavage of the brevican core protein occurs in a highly conserved region within a generally poorly conserved central domain, and that the sequence at the cleavage site shows intriguing similarities to the “aggrecanase” cleavage site in aggrecan. cDNA cloning of rat brevican has also revealed that the putative hyaluronic acid binding protein, BEHAB, is identical to the N-terminal half of brevican.

    Original languageEnglish
    Pages (from-to)957-963
    Number of pages7
    JournalBiochemical and biophysical research communications
    Volume216
    Issue number3
    DOIs
    Publication statusPublished - 1995 Nov 22

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

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