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Cloning of cDNA for human granzyme 3
Author(s) -
Przetak Melinda M.,
Yoast Sienna,
Schmidt Brian F.
Publication year - 1995
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 - 10.1016/0014-5793(95)00407-z
Subject(s) - granzyme , granzyme a , complementary dna , microbiology and biotechnology , granzyme b , proteases , serine , biology , tmprss6 , serine protease , masp1 , peptide sequence , amino acid , molecular cloning , biochemistry , northern blot , gene , protease , perforin , cytotoxic t cell , phosphorylation , enzyme , in vitro
A serine protease gene was cloned from cDNA prepared from tissue isolated from human ascites. The gene codes for a protein of 264 amino acids, identified as human granzyme 3 by the N‐terminal amino acid sequence. Granzyme 3 has the expected features of the chymotrypsin family of serine proteases, and is closely related to other human granzymes (40–45% identity). However, the closest granzyme 3 homologue is the recently characterized rat tryptase, RNK‐Tryp‐2 (75% identity). From Northern blots, granzyme 3 appears to be highly expressed in peripheral blood leukocytes, spleen, thymus, and lung tissues.