Mechanisms of serpin dysfunction in disease

Expert Rev Mol Med. 2006 Dec 11;8(31):1-19. doi: 10.1017/S1462399406000184.

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 alpha1-antitrypsin Pittsburgh mutation causes a change in target proteinase; the alpha1-antitrypsin Z mutation and neuroserpin, polymerisation of which lead to cellular cytotoxicity; and a loss of maspin expression resulting in cancer.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Antithrombins / chemistry
  • Disease*
  • Humans
  • Mutation / genetics
  • Protein Conformation
  • Serpins / chemistry
  • Serpins / genetics
  • Serpins / metabolism*
  • alpha 1-Antitrypsin / chemistry

Substances

  • Antithrombins
  • Serpins
  • alpha 1-Antitrypsin