Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors

Brazilian Journal of Medical and Biological Research

A.j. Gozzo²  V.a. Nunes²  H.b. Nader²  C.p. Dietrich²  A.k. Carmona¹  M.u. Sampaio²  C.a.m. Sampaio²  M.s. Araújo² 

[1] ,Universidade Federal de São Paulo Escola Paulista de Medicina Departamento de Bioquímica

关键词: Glycosaminoglycans;    Human plasma kallikrein;    Plasminogen;    Factor XII;    C1-inhibitor;    Antithrombin;   

DOI  :  10.1590/S0100-879X2003000800011

来源: SciELO

【 摘 要 】

Human plasma kallikrein, a serine proteinase, plays a key role in intrinsic blood clotting, in the kallikrein-kinin system, and in fibrinolysis. The proteolytic enzymes involved in these processes are usually controlled by specific inhibitors and may be influenced by several factors including glycosaminoglycans, as recently demonstrated by our group. The aim of the present study was to investigate the effect of glycosaminoglycans (30 to 250 µg/ml) on kallikrein activity on plasminogen and factor XII and on the inhibition of kallikrein by the plasma proteins C1-inhibitor and antithrombin. Almost all available glycosaminoglycans (heparin, heparan sulfate, bovine and tuna dermatan sulfate, chondroitin 4- and 6-sulfates) reduced (1.2 to 3.0 times) the catalytic efficiency of kallikrein (in a nanomolar range) on the hydrolysis of plasminogen (0.3 to 1.8 µM) and increased (1.9 to 7.7 times) the enzyme efficiency in factor XII (0.1 to 10 µM) activation. On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 µM), while chondroitin 4- and 6-sulfates reduced it (1.3 times). Heparin and heparan sulfate increased (1.4 times) the enzyme inhibition by the C1-inhibitor (150 nM).

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