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    FEBS Lett. 1995 Jan 3;357(2):129-34.

    Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2.

    Shi GP, Chapman HA, Bhairi SM, DeLeeuw C, Reddy VY, Weiss SJ.

    Physiology Program, Harvard School of Public Health, Boston, MA 02115.

    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 approximately 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.

    PMID: 7805878 [PubMed - indexed for MEDLINE]

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