Premium
Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2
Author(s) -
Shi Guo-Ping,
Chapman Harold A.,
Bhairi Srirama M.,
DeLeeuw Carrie,
Reddy Vivek Y.,
Weiss Stephen J.
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(94)01349-6
Subject(s) - cathepsin h , complementary dna , microbiology and biotechnology , cathepsin e , cathepsin , cathepsin o , cathepsin l1 , cathepsin s , cdna library , cathepsin l , biology , cathepsin a , biochemistry , monocyte , molecular cloning , amino acid , enzyme , gene , immunology
A 1670‐bp cDNA coding for a novel human cysteine protease has been isolated from a monocyte‐derived macrophage cDNA library. This cDNA predicts a 329‐amino acid preprocathepsin with more than 50% identity to both human cathepsin S and cathepsin L and 94% identity to a rabbit cDNA, termed OC2, recently isolated from osteoclasts. Based on its high homology to OC2, we have named the human enzyme cathepsin O. Cathepsin O mRNA was identified as a single ∼1.7 kb transcript in cultures of 15‐day‐old monocyte‐derived macrophages, but was not expressed in human monocytes or alveolar macrophages. When transfected into COS‐7 cells, cathepsin O displayed potent endoprotease activity against fibrinogen at acid pH. This novel endoprotease may play an important role in extracellular matrix degradation.