Acute Phase Proteins in the Acute Phase Response

Part of the series Argenteuil Symposia pp 107-122

The Plasma Serine Protease Inhibitors (Serpins): Structural Modifications in Inflammation

  • P. E. Stein
  • , R. W. Carrell

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The serine protease inhibitor (serpin) superfamily comprises more than 20 glycoproteins that show primary sequence homology at protein or cDNA level with the archetype of the family, α1-antitrypsin (abbreviated hereafter to antitrypsin). Members of the family are presumed to be derived by divergent evolution from a common ancestral protein over a period of more than 500 million years (Hunt and Dayhoff 1980; Carrell and Boswell 1986). Although the serpins are widely distributed in nature, and have been identified in viruses and plants, the best studied members of the family are the human plasma serpins (Table 9.1). Most plasma serpins function as inhibitors of serine proteases and are principally involved in inflammation, controlling the activities of enzymes that trigger the inflammatory cascades including coagulation, fibrinolysis, complement activation and kinin release. However some serpins have apparently lost their antiprotease activity and have evolved other functions, such as hormone binding in the case of thyroxine binding globulin (TBG) and cortisol binding globulin (CBG).