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• W4253301546 abstract "C1 inhibitor, although frequently considered primarily a complement protein, is able to inactivate proteinases that participate in several different proteolytic cascades, and is essential in the regulation of activation of both the complement system and the contact system of kinin formation. It also may serve a backup function in regulation of coagulation and of fibrinolysis. C1 inhibitor, therefore, is most important in host defense and in the mediation of vascular permeability. Its name is derived from its discovery as the inactivator of the first complement component. This came about as a result of the studies of Lepow and his colleagues in the late 1950s and early 1960s; these were directed toward the isolation of C1 and its constituent subunits: C1q, C1r and C1s1–5. C1 inhibitor was characterized as a heat labile serum protein that inhibited the esterolytic activity of C1 and its proteolytic activity against C4 and C2. It subsequently was shown to inactivate several other plasma proteases, including kallikrein, plasmin, tissue plasminogen activator, and coagulation factors XIa and XIIa (Hageman factor)5–10. The fact that C1 inhibitor inactivated proteases by formation of denaturant stable equimolar complexes was first clearly shown by Harpel and Cooper with both C1s and plasmin6. Cl inhibitor does not appear to differ in any significant way from other serpins in its mechanism of action. The P1 and P1’ residues are arginine and threonine, respectively11." @default.
• W4253301546 created "2022-05-12" @default.
• W4253301546 creator A5017017765 @default.
• W4253301546 date "1997-01-01" @default.
• W4253301546 modified "2023-10-17" @default.
• W4253301546 title "C1 Inhibitor" @default.
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• W4253301546 doi "https://doi.org/10.1007/978-1-4615-5391-5_18" @default.
• W4253301546 hasPublicationYear "1997" @default.
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