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  • Title: Molecular cloning of a novel brain-specific serine protease with a kringle-like structure and three scavenger receptor cysteine-rich motifs.
    Author: Yamamura Y, Yamashiro K, Tsuruoka N, Nakazato H, Tsujimura A, Yamaguchi N.
    Journal: Biochem Biophys Res Commun; 1997 Oct 20; 239(2):386-92. PubMed ID: 9344839.
    Abstract:
    In order to find serine proteases specifically expressed in brain, we designed degenerate mixed primers for consensus sequences of serine protease domains. By PCR utilizing the primers, we have cloned a novel sequence from reverse transcripts of total RNA of mouse brain and used it as a probe to screen a mouse brain cDNA library. Overlapping cDNAs encoding a precursor of a novel brain specific serine protease (BSSP-3) were cloned. DNA insert of the longest clone consisted of 2614-bp with an entire open reading frame encoding a secretory/membrane-anchored precursor protein consisting of 761 amino acids (AA) which may be processed to yield an active enzyme of 245 AA. As found in known serine proteases, BSSP-3 enzyme domain contained a catalytic triad which consists of AA residues essential for the enzyme activity. In the upstream region of the enzyme domain that resides at C-terminus of the precursor protein, there are, from N-terminus to downstream, a sequence similar to a kringle structure and three repetitive ones highly similar to the scavenger receptor cysteine-rich (SRCR) motifs. Northern blot analysis demonstrated that mBSSP-3 mRNA was specifically expressed in the mouse brain, lung and kidney. We concluded that a novel brain serine protease, BSSP-3, is a new member of kringle and SRCR superfamilies.
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