Please use this identifier to cite or link to this item:
http://sgc.anlis.gob.ar/handle/123456789/2105
DC Field | Value | Language |
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dc.contributor.author | Joensen, Lilian G | es |
dc.contributor.author | Borda, Enri | es |
dc.contributor.author | Kohout, Trudy | es |
dc.contributor.author | Perry, Stephen J | es |
dc.contributor.author | Garcia, Gabriela | es |
dc.contributor.author | Sterin-Borda, Leonor | es |
dc.date.accessioned | 2021-01-12T19:44:02Z | - |
dc.date.available | 2021-01-12T19:44:02Z | - |
dc.date.issued | 2003-04-03 | - |
dc.identifier.issn | 0166-6851 | - |
dc.identifier.uri | http://sgc.anlis.gob.ar/handle/123456789/2105 | - |
dc.description | Fil: Joensen, Lilian. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina. | es |
dc.description | Fil: Borda, Enri. Pharmacology Unit, School of Dentistry, Argentine National Research Council (CONICET), University of Buenos Aires, Buenos Aires; Argentina. | es |
dc.description | Fil: Kohout, Trudy. Department of Medicine, Duke University Medical Center, Durham, NC; Estados Unidos. | es |
dc.description | Fil: Perry, Stephen. Pharmacology Unit, School of Dentistry, Argentine National Research Council (CONICET), University of Buenos Aires, Buenos Aires; Argentina. | es |
dc.description | Fil: García, Gabriela. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina. | es |
dc.description | Fil: Sterin-Borda, Leonor. Pharmacology Unit, School of Dentistry, Argentine National Research Council (CONICET), University of Buenos Aires, Buenos Aires; Argentina. | es |
dc.description.abstract | Previously, we have demonstrated that plasma membranes from the parasite Trypanosoma cruzi (T. cruzi) recognize and adhere to host cells through parasite surface attachment molecules that have affinity for beta(1)-adrenergic receptors (beta(1)-ARs) on target organs. In this report we identify a parasite protein that not only interacts with beta(1)-ARs, but also displays beta-agonist-like activity. We demonstrate that a recombinant maltose binding protein fusion of Tc13 Tul (MBP-Tc13 Tul), a member of the T. cruzi antigen 13 family of surface antigen proteins, competes for binding sites with the beta-adrenergic receptor antagonist [125I]-CYP on membranes purified both from CHO cells expressing human beta(1)-ARs and from rat atria. The competition is prevented by pre-treating MBP-Tc13 Tul with antibodies directed against the EPKSA repeat domain of Tc13 Tul, implicating this portion of the molecule in binding to the beta(1)-AR. Furthermore, MBP-Tc13 Tul activates rat myocardial beta(1)-ARs, resulting in synthesis of cyclic adenosine monophosphate (cAMP) and an increase in cardiac contractility. These biological effects are selectively suppressed by the beta(1)-AR antagonist atenolol, by a synthetic peptide corresponding to the second extracellular loop of the human beta(1)-AR, and by the anti-EPKSA repeat antibodies. These results imply that the Tc13 Tul cell-surface antigen of T. cruzi plays a central role in misregulating the beta(1)-AR following parasite infection, and may be a causative factor of dysautonomic syndrome described in Chagas' disease. | es |
dc.language.iso | en | es |
dc.publisher | Elsevier | es |
dc.relation.ispartof | Molecular and biochemical parasitology | es |
dc.rights | Closed Access | - |
dc.source | Molecular and Biochemical Parasitology 2003; 127(2):169-77. | - |
dc.subject | Trypanosoma cruzi | es |
dc.subject | Enfermedad de Chagas | es |
dc.title | Trypanosoma cruzi antigen that interacts with the beta1-adrenergic receptor and modifies myocardial contractile activity | es |
dc.type | Artículo | es |
dc.identifier.doi | 10.1016/s0166-6851(03)00003-3 | - |
anlis.essnrd | 1 | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.grantfulltext | none | - |
item.openairetype | Artículo | - |
item.fulltext | No Fulltext | - |
item.languageiso639-1 | en | - |
Appears in Collections: | Publicaciones INP |
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