title: Plasminogen interaction with Trypanosoma cruzi.
abstract: The ability of Trypanosoma cruzi to interact with plasminogen, the zimogenic form of the blood serin protease plasmin, was examined. Immunohistochemistry studies revealed that both forms, epimastigotes and metacyclic trypomastigotes, were able to fix plasminogen in a lysine dependant manner. This interaction was corroborated by plasminogen activation studies. Both forms of the parasite enhanced the plasminogen activation by tissue-type plasminogen activator. The maximal enhancements obtained were 15-fold and 3.4-fold with epimastigotes and metacyclic trypomastigotes, respectively, as compared to plasminogen activation in absence of cells. Ligand-blotting analysis of proteins extracted with Triton X-114 from a microsomal fraction of epimastigotes revealed at least five soluble proteins and one hydrophobic protein able to bind plasminogen.
authors.affiliation: Departamento de Biología, Facultad de Ciencias, Universidad de Los Andes, Mérida, Venezuela.
authors.forename: Laura
authors.initials: L
authors.lastname: Almeida
authors.forename: Gilmer
authors.initials: G
authors.lastname: Vanegas
authors.forename: Marina
authors.initials: M
authors.lastname: Calcagno
authors.forename: Juan Luis
authors.initials: JL
authors.lastname: Concepción
authors.forename: Luisana
authors.initials: L
authors.lastname: Avilan
mesh_terms: D000818:Animals; D004789:Enzyme Activation; D006801:Humans; D007150:Immunohistochemistry; D010958:Plasminogen / Q000378:metabolism*; D010959:Tissue Plasminogen Activator / Q000378:metabolism; D014349:Trypanosoma cruzi / Q000378:metabolism*
chemical_list: D010958:Plasminogen; D010959:Tissue Plasminogen Activator