Review demonstrates how distinct mutations cause serpin dysfunction across clinical disorders, highlighting pathways ranging from altered protease targeting to toxic protein polymerization.
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.
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Kaiserman et al. (2006) studied this question.
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