Abstract
Inhibition of serine proteases by serpins (serpin: serine protease inhibitor) is a key mechanism for the control of proteolysis in thrombosis, shock, and inflammation. The various members of the serpin gene superfamily ( α 1-antitrypsin, ovalbumin, C1-inhibitor, antithrombin III, α 2-antiplasmin, type-1 plasminogen-activator inhibitor, and so forth) have many characteristics in common. In this article, we review the biochemistry and cell biology of serpins, and we discuss their clinical importance and therapeutic potential.
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