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J Biol Chem, Vol. 273, Issue 51, 34406-34412, December 18, 1998
From the Arthritis Biology Unit, Novartis Pharmaceuticals, Summit,
New Jersey 07901
The human homologue of the Escherichia coli
htrA gene product was identified by the differential display
analysis of transcripts expressed in osteoarthritic cartilage. This
transcript was identified previously as being repressed in
SV40-transformed fibroblasts (Zumbrunn, J., and Trueb, B. (1996)
FEBS Lett. 398, 187-192). Levels of HtrA mRNA were
elevated ~7-fold in cartilage from individuals with osteoarthritis
compared with nonarthritic controls. Differential expression of human
HtrA protein was confirmed by an immunoblot analysis of cartilage
extracts. Human HtrA protein expressed in heterologous systems was
secreted and exhibited endoproteolytic activity, including
autocatalytic cleavage. Conversion by mutagenesis of the putative
active site serine 328 to alanine eliminated the enzymatic activity.
Serine 328 was also found to be required for the formation of a stable
complex with
Human HtrA, an Evolutionarily Conserved Serine Protease
Identified as a Differentially Expressed Gene Product in Osteoarthritic
Cartilage
1-antitrypsin. We have determined that the
HtrA gene is highly conserved among mammalian species: the amino acid
sequences encoded by HtrA cDNA clones from cow, rabbit, and guinea
pig are 98% identical to human. In E. coli, a functional
htrA gene product is required for cell survival after heat
shock or oxidative stress; its role appears to be the degradation of
denatured proteins. We propose that mammalian HtrA, with the addition
of a new functionality during evolution, i.e. a mac25
homology domain, plays an important role in cell growth regulation.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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