Host cell invasion by Trypanosoma cruzi is potentiated by activation of bradykinin B-2 receptors

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dc.contributor.author Scharfstein, J.
dc.contributor.author Schmitz, V
dc.contributor.author Morandi, V
dc.contributor.author Capella, MMA
dc.contributor.author Lima, APCA
dc.contributor.author Morrot, A.
dc.contributor.author Juliano, Luiz [UNIFESP]
dc.contributor.author Muller-Esterl, W.
dc.date.accessioned 2016-01-24T12:31:12Z
dc.date.available 2016-01-24T12:31:12Z
dc.date.issued 2000-11-06
dc.identifier http://dx.doi.org/10.1084/jem.192.9.1289
dc.identifier.citation Journal of Experimental Medicine. New York: Rockefeller Univ Press, v. 192, n. 9, p. 1289-1299, 2000.
dc.identifier.issn 0022-1007
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/26412
dc.description.abstract The parasitic protozoan Trypanosoma cruzi employs multiple molecular strategies to invade a broad range of nonphagocytic cells. Here we demonstrate that the invasion of human primary umbilical vein endothelial cells (HUVECs) or Chinese hamster ovary (CHO) cells overexpressing the B-2 type of bradykinin receptor (CHO-B2R) by tissue culture trypomastigotes is subtly modulated by the combined activities of kininogens, kininogenases, and kinin-degrading peptidases. the presence of captopril, an inhibitor of bradykinin degradation by kininase II, drastically potentiated parasitic invasion of HUVECs and CHO-B2R, but not of mock-transfected CHO cells, whereas the B2R antagonist HOE 140 or monoclonal antibody MBK3 to bradykinin blocked these effects. Invasion competence correlated with the parasites' ability to Liberate the short-lived kinins from cell-bound kininogen and to elicit vigorous intracellular free calcium ([Ca2+](i)) transients through B2R. Invasion was impaired by membrane-permeable cysteine proteinase inhibitors such as Z-(SBz)Cys-Phe-CHN2 but not by the hydrophilic inhibitor 1-trans-epoxysuccinyl-L-leucyl-amido-(4-guanidino) butane or cystatin C, suggesting that kinin release is confined to secluded spaces formed by juxtaposition of host cell and parasite plasma membranes. Analysis of trypomastigote transfectants expressing various cysteine proteinase isoforms showed that invasion competence is linked to the kinin releasing activity of cruzipain, herein proposed as a factor of virulence in Chagas' disease. en
dc.format.extent 1289-1299
dc.language.iso eng
dc.publisher Rockefeller Univ Press
dc.relation.ispartof Journal of Experimental Medicine
dc.rights Acesso aberto
dc.subject Trypanosoma cruzi en
dc.subject bradykinin en
dc.subject cruzipain en
dc.subject cysteine proteinases en
dc.subject kinin receptors en
dc.title Host cell invasion by Trypanosoma cruzi is potentiated by activation of bradykinin B-2 receptors en
dc.type Artigo
dc.contributor.institution Universidade Federal do Rio de Janeiro (UFRJ)
dc.contributor.institution Universidade do Estado do Rio de Janeiro (UERJ)
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.contributor.institution Univ Frankfurt
dc.description.affiliation Univ Fed Rio de Janeiro, Ctr Ciencias Saude, Inst Biofis Carlos Chagas Filho, BR-21990400 Rio de Janeiro, Brazil
dc.description.affiliation Univ Estado Rio de Janeiro, Dept Genet & Cell Biol, BR-20550013 Rio de Janeiro, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-04044000 São Paulo, Brazil
dc.description.affiliation Univ Frankfurt, Sch Med, Inst Biochem 2, D-60590 Frankfurt, Germany
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-04044000 São Paulo, Brazil
dc.identifier.file WOS000165471100008.pdf
dc.identifier.doi 10.1084/jem.192.9.1289
dc.description.source Web of Science
dc.identifier.wos WOS:000165471100008



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