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A cytochemical assay for osteoclast cathepsin K activity
Author(s) -
Dodds Robert A.
Publication year - 2003
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.1078
Subject(s) - cathepsin k , osteoclast , cathepsin , bone resorption , proteases , chemistry , biochemistry , cysteine proteinase inhibitors , enzyme , microbiology and biotechnology , biology , in vitro , endocrinology , programmed cell death , apoptosis , caspase
Abstract Cathepsin K is a member of the papain superfamily of cysteine proteases and plays a pivotal role in osteoclast‐mediated bone resorption. This enzyme is an excellent target for antiresorptive therapies for osteopenic disorders such as osteoporosis. 1 Although isolated inhibitor studies on purified enzymes is required to discover potent and selective inhibitors of cathepsin K, a quantitative cytochemical assay 2 for cathepsin K would allow inhibitors to be tested on actual osteoclasts within sections of bone. Furthermore cathepsin K activity could be used to identify and analyse osteoclasts at definitive stages of their lifespan. A cytochemical assay is described that localizes osteoclast cathepsin K activity in unfixed, undecalcified cryostat sections of animal and human bone. Copyright © 2003 John Wiley & Sons, Ltd.