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A novel transmembrane serine protease, BSSP-2, in mouse and human brain



A novel transmembrane serine protease, BSSP-2, in mouse and human brain



Society for Neuroscience Abstracts 26(1-2): Abstract No -33 2



The evidences showing that some serine proteases play significant roles in the mammalian central nervous system (CNS) are accumulating. We are proceeding to identify novel serine proteases expressed in the CNS to understand the interaction between ECM and neuronal cells. Here, we describe cDNA cloning encoding a novel transmembrane serine protease, BSSP-2. Mouse BSSP-2 was isolated from mouse brain DNA pool by PCR techniques. 5' rapid amplification of cDNA ends (RACE) revealed two types of BSSP-2 isoforms which appeared to be caused by alternative splicing. The longer type (455 amino acids) had transmembrane domain near the amino terminal and a scavenger receptor cysteine-rich domain. The shorter type (311 amino acids) was relatively simple form composed of leader peptide and a protease domain. The serine protease domain showed 42% identity to that TMPRSS2. Northern hybridization showed that the expression of BSSP-2 in the fetal brain (E15-E20) but not in the neonatal and adult brains. Furthermore, cDNA encoding human BSSP-2 was also isolated. Human BSSP-2 was 457 amino acids and showed 78 % identity to the longer type mouse BSSP-2. Northern hybridization showed a 2.4 kb transcript in the brain and 1.3 kb in the skeletal muscle. Our results suggest that a novel transemembrane serine protease, BSSP-2, may be involved in the CNS functions.

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Accession: 034312588

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