1055
Braz J Med Biol Res 36(8) 2003
GAGs affect human plasma kallikrein activity and inhibition
Brazilian Journal of Medical and Biological Research (2003) 36: 1055-1059
ISSN 0100-879X
Glycosaminoglycans affect the
interaction of human plasma
kallikrein with plasminogen,
factor XII and inhibitors
Departamentos de 1Bioquimica and 2Biofisica,
Escola Paulista de Medicina, Universidade Federal de Sao Paulo,
Sao Paulo, SP, Brasil
A.J. Gozzo1, V.A. Nunes1,
H.B. Nader1, C.P. Dietrich1,
A.K. Carmona2,
M.U. Sampaio1,
C.A.M. Sampaio1
and M.S. Araujo1
Abstract
Human plasma kallikrein, a serine proteinase, plays a key role in
intrinsic blood clotting, in the kallikrein-kinin system, and in fibrin-
olysis. The proteolytic enzymes involved in these processes are usu-
ally 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 plas-
minogen 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 der-
matan 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

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