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M108518200v1
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Papers In Press, published online ahead of print November 28, 2001
J. Biol. Chem, 10.1074/jbc.M108518200
Submitted on September 5, 2001
Revised on November 19, 2001
Accepted on November 28, 2001

Heparan sulfate modulates kinin release by Trypanosoma cruzi through the activity of cruzipain

Ana Paula C.A. Lima, Paulo C. Almeida, Ivarne L.S. Tersariol, Veronica Schmitz, Alvin H. Schmaier, Luiz Juliano, Isaura Y. Hirata, Werner Müller-Esterl, Jair R. Chagas, and Julio Scharfstein

Instituto de Biofisica Carlos Chagas F., Federal University of Rio de Janeiro, Rio de Janeiro 21949-900

Corresponding Author: anapaula{at}biof.ufrj.br

Trypanosoma cruzi activates the kinin pathway through the activity of its major cysteine proteinase, cruzipain. Since kininogen molecules may be expressed on cell surfaces by binding to glycosaminoglycans, we examined if the ability of cruzipain to release kinins from high molecular weight kininogen (HK) is modulated by heparan sulfate (HS). Kinetic assays show that HS reduces the cysteine proteinase inhibitory activity (Kiapp) of HK about 10 fold. Conversely, the catalytic efficiency of cruzipain on kinin-related synthetic fluorogenic substrates is enhanced up to 6-fold in the presence of HS. Analysis of the HK breakdown products generated by cruzipain indicated that HS changes the pattern of HK cleavage products. Direct measurements of bradykinin demonstrated an up to 35-fold increase in cruzipain-mediated kinin liberation in the presence of HS. Similarly, kinin release by living trypomastigotes increased up to 10-fold in the presence of HS. These studies suggest that the efficiency of T. cruzi to initiate kinin release is potently enhanced by the mutual interactions between cruzipain, HK and heparan sulfate proteoglycans.


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