Artigo Revisado por pares

Cathepsin G, a regulator of human vitamin K, dependent clotting factors and inhibitors

1992; Elsevier BV; Volume: 67; Issue: 2 Linguagem: Inglês

10.1016/0049-3848(92)90134-v

ISSN

1879-2472

Autores

Philip T. Turkington,

Tópico(s)

Coagulation, Bradykinin, Polyphosphates, and Angioedema

Resumo

Cathepsin G was used in vitro to digest human factor VII and factor IX. Clotting assays indicated that the proteinase affected a rapid loss in coagulant activity while in the presence of calcium ions the activity was almost totally protected. SDS-polyacrylamide gel electrophoresis indicated the removal of a peptide from each zymogen, VII-L from factor VII and IX-L from factor IX. This lead to the formation of VII-H and IX-H respectively. N-terminal analysis of the VII-H and IX-H products and COOH-terminal analysis of the VII-L and IX-L products confirmed that cathepsin G had cleaved position Phe40:Trp41 in factor VII and factor IX. The cleavage site is the same as that when cathepsin G is reacted with factor II, factor X and protein C. The unique action of cathepsin G may be part of a regulatory system for controlling the coagulant activity of vitamin K dependent clotting in vivo.

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