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J Biol Chem, Vol. 274, Issue 36, 25555-25563, September 3, 1999
, and
From the Department of Biomedical Engineering, Lerner Research
Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195 and the
We report the primary structure of three novel,
putative zinc metalloproteases designated ADAM-TS5, ADAM-TS6, and
ADAM-TS7. All have a similar domain organization, comprising a
preproregion, a reprolysin-type catalytic domain, a disintegrin-like
domain, a thrombospondin type-1 (TS) module, a cysteine-rich domain, a spacer domain without cysteine residues, and a COOH-terminal TS module.
These genes are differentially regulated during mouse embryogenesis and
in adult tissues, with Adamts5 highly expressed in the
peri-implantation period in embryo and trophoblast. These proteins are
similar to four other cognate gene products, defining a distinct family
of human reprolysin-like metalloproteases, the ADAM-TS family. The
other members of the family are ADAM-TS1, an inflammation-induced gene,
the procollagen I/II amino-propeptide processing enzyme (PCINP,
ADAM-TS2), and proteins predicted by the KIAA0366 and
KIAA0688 genes (ADAM-TS3 and ADAM-TS4). Individual ADAM-TS
members differ in the number of COOH-terminal TS modules, and some have
unique COOH-terminal domains. The ADAM-TS genes are dispersed in human
and mouse genomes.
Rowe Program in Genetics, Departments of Biological
Chemistry and Medicine, University of California,
Davis, California 956161
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