Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems

Gary A. Silverman, James C. Whisstock, Stephen P. Bottomley, James A. Huntington, Dion Kaiserman, Cliff J. Luke, Stephen C. Pak, Jean Marc Reichhart, Phillip I. Bird

Research output: Contribution to journalShort surveypeer-review

100 Scopus citations

Abstract

Serpins compose the largest superfamily of peptidase inhibitors and are well known as regulators of hemostasis and thrombolysis. Studies using model organisms, from plants to vertebrates, now show that serpins and their unique inhibitory mechanism and conformational flexibility are exploited to control proteolysis in molecular pathways associated with cell survival, development, and host defense. In addition, an increasing number of non-inhibitory serpins are emerging as important elements within a diversity of biological systems by serving as chaperones, hormone transporters, or anti-angiogenic factors.

Original languageEnglish
Pages (from-to)24299-24305
Number of pages7
JournalJournal of Biological Chemistry
Volume285
Issue number32
DOIs
StatePublished - Aug 6 2010
Externally publishedYes

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