Plasminogen interaction with Trypanosoma cruzi

Laura Almeida, Gilmer Vanegas, Marina Calcagno, Juan Luis Concepción, Luisana Avilan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)63-7
Number of pages5
JournalMemorias do Instituto Oswaldo Cruz
Volume99
Issue number1
DOIs
Publication statusPublished - Feb 2004

Keywords

  • Animals
  • Enzyme Activation
  • Humans
  • Immunohistochemistry
  • Plasminogen/metabolism
  • Tissue Plasminogen Activator/metabolism
  • Trypanosoma cruzi/metabolism

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