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ADAM-TS5, ADAM-TS6, and ADAM-TS7, Novel Members of a New Family of Zinc Metalloproteases

Open access
Hurskainen, Tiina L., Hirohata, Satoshi, Seldin, Michael F., Apte, Suneel S.·1999·Journal of Biological Chemistry

Abstract

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.

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Metadata

Authors
Hurskainen, T. L., Hirohata, S., Seldin, M. F., & Apte, S. S.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1999-09
Volume
274
Issue
36
Pages
25555-25563
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2128487191
Cited by
200
References
2
FWCI
5.24
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: ADAM-TS5, ADAM-TS6, and ADAM-TS7, Novel Members of a New Family of Zinc Metalloproteases. https://app.cochat.ai/papers/10.1074/jbc.274.36.25555
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Hurskainen, T. L., Hirohata, S., Seldin, M. F., & Apte, S. S. (1999). ADAM-TS5, ADAM-TS6, and ADAM-TS7, Novel Members of a New Family of Zinc Metalloproteases. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.274.36.25555

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