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Mechanisms of serpin dysfunction in disease

Published online by Cambridge University Press:  11 December 2006

Dion Kaiserman ,
James C. Whisstock  and
Phillip I. Bird
Dion Kaiserman
Affiliation:
Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia.
James C. Whisstock
Affiliation:
Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia.
Phillip I. Bird
Affiliation:
Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia.
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Abstract

The serpin superfamily encompasses hundreds of proteins, spread across all kingdoms of life, linked by a common tertiary fold. This review focuses on five diseases caused by serpin dysfunction: variants of antithrombin III lose their ability to interact with heparin; the α1-antitrypsin Pittsburgh mutation causes a change in target proteinase; the α1-antitrypsin Z mutation and neuroserpin, polymerisation of which lead to cellular cytotoxicity; and a loss of maspin expression resulting in cancer.

Type
Review Article
Information
Expert Reviews in Molecular Medicine , Volume 8 , Issue 31 , December 2006 , pp. 1 - 19
Copyright
© 2006 Cambridge University Press

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