Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2
Authors:
- Harold A. ChapmanHCHarold A. Chapman
- Srirama M. BhairiSBSrirama M. Bhairi
- Carrie DeLeeuwCDCarrie DeLeeuw
- Vivek Y. ReddyVRVivek Y. Reddy
- Stephen J. WeissSWStephen J. Weiss
- 3 January 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 357 (2) , 129-134
Abstract
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.Keywords
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