Mechanisms of serpin dysfunction in disease.
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.
Kaiserman
Dion
D
Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia. dion.kaiserman@med.monash.edu.au
Whisstock
James C
JC
Bird
Phillip I
PI
D000818:Animals; D000991:Antithrombins / Q000737:chemistry; D004194:Disease; D006801:Humans; D009154:Mutation / Q000235:genetics; D011487:Protein Conformation; D015843:Serpins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000515:alpha 1-Antitrypsin / Q000737:chemistry
D000991:Antithrombins; D015843:Serpins; D000515:alpha 1-Antitrypsin