Mechanisms of serpin dysfunction in disease
D Kaiserman, JC Whisstock, PI Bird - Expert reviews in molecular …, 2006 - cambridge.org
D Kaiserman, JC Whisstock, PI Bird
Expert reviews in molecular medicine, 2006•cambridge.orgThe 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.
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.
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.
Cambridge University Press