| First Author | Yamamura Y | Year | 1997 |
| Journal | Biochem Biophys Res Commun | Volume | 239 |
| Issue | 2 | Pages | 386-92 |
| PubMed ID | 9344839 | Mgi Jnum | J:43684 |
| Mgi Id | MGI:1098345 | Doi | 10.1006/bbrc.1997.7417 |
| Citation | Yamamura Y, et al. (1997) Molecular cloning of a novel brain-specific serine protease with a kringle-like structure and three scavenger receptor cysteine-rich motifs. Biochem Biophys Res Commun 239(2):386-92 |
| abstractText | 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. Copyright 1997 Academic Press. |
