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Mechanisms of serpin dysfunction in disease

  • Dion Kaiserman (a1), James C. Whisstock (a1) and Phillip I. Bird (a1)
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.

Copyright
© 2006 Cambridge University Press
Corresponding author
Corresponding author: Dion Kaiserman, Building 13B, Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia. Tel: +61 03 99055214; Fax: +61 03 99053726; E-mail: dion.kaiserman@med.monash.edu.au
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Expert Reviews in Molecular Medicine
  • ISSN: -
  • EISSN: 1462-3994
  • URL: /core/journals/expert-reviews-in-molecular-medicine
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