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J. Biol. Chem., Vol. 277, Issue 8, 5875-5881, February 22, 2002
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From the Trypanosoma cruzi activates the kinin
pathway through the activity of its major cysteine proteinase,
cruzipain. Because kininogen molecules may be displayed on cell
surfaces by binding to glycosaminoglycans, we examined whether 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
(Ki app) 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.
Heparan Sulfate Modulates Kinin Release by Trypanosoma
cruzi through the Activity of Cruzipain*
,,
,,
Instituto de Biofísica Carlos Chagas
Filho, Universidade do Brasil, CCS, Bloco G, Cidade
Universitária, CEP 21944-900, Rio de Janeiro, Brazil, the
§ Centro Interdisciplinar de Investigação
Bioquímica, Universidade Mogi das Cruzes, CEP 08780-911, Mogi das Cruzes, São Paulo, Brazil, the Departmento de
Biofísica, Universidade Federal do Estado de São
Paulo, Escola Paulista de Medicina, CEP04044-20 São Paulo,
Brazil, the ¶ Department of Internal Medicine, University of
Michigan, Ann Arbor, Michigan 48109-5669, and the
** Institute for Biochemistry II, University of Frankfurt
Medical School, Frankfurt D-60590, Germany
*
This work was supported in part by a grant from
Fundação de Amparo à Pesquisa do Estado do Rio de
Janeiro, Ministério de Ciência e Tecnologia (Pronex),
Fundação de Amparo à Pesquisa do Estado de São
Paulo (Grant 97/13133-4), funds from the Deutsche Forschungsgemeinschaft, a grant from Fonds der Chemischen Industrie (to
W. M. E.), and by National Institutes of Health Grant 4252779 (to A. H. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
55-21-2-280-2718; Fax: 55-21-2-280-8193;
E-mail:scharf@biof.ufrj.br.
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