Hostname: page-component-8448b6f56d-tj2md Total loading time: 0 Render date: 2024-04-23T22:12:56.015Z Has data issue: false hasContentIssue false
  • English
  • Français

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.
Get access Rights & Permissions [Opens in a new window]

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

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)