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Cathepsin J, a novel murine cysteine protease of the papain family with a placenta‐restricted expression
Author(s) -
Tisljar Kai,
Deussing Jan,
Peters Christoph
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01263-6
Subject(s) - cathepsin o , cathepsin h , cathepsin e , cathepsin a , cathepsin c , microbiology and biotechnology , cathepsin b , proteases , cathepsin l1 , cathepsin , biology , cathepsin l , complementary dna , cysteine protease , biochemistry , cathepsin s , cysteine , cathepsin d , gene , enzyme
A novel mouse cysteine protease of the papain family was identified by searching the dbEST database. A 1.28 kb full‐length cDNA was obtained which contains an open reading frame of 999 nucleotides and encodes a predicted polypeptide of 333 amino acids. The deduced polypeptide exhibits features characteristic of cysteine proteases of the papain type including the highly conserved residues of the catalytic triad, and was hence named cathepsin J. Cathepsin J represents the murine homologue of a previously described rat cathepsin L‐related protein. Mature cathepsin J shows 59.3% identity to mouse cathepsin L and contains the characteristic ER(F/W)NIN motif within the propeptide indicating that this protease belongs to the subgroup of cathepsin L‐like cysteine proteases. Northern blot analysis of various tissues revealed a placenta‐restricted expression. This expression pattern may suggest a role of cathepsin J in embryo implantation and/or placental function. Ctsj was mapped to mouse chromosome 13 in the vicinity of cathepsin L suggesting that cathepsin J may have arisen by gene duplication from cathepsin L or a common ancestral gene.