4.5 Article

Novel mechanism that Trypanosoma cruzi uses to adhere to the extracellular matrix mediated by human galectin-3

Journal

FEBS LETTERS
Volume 470, Issue 3, Pages 305-308

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(00)01347-8

Keywords

human galectin-3; extracellular matrix; laminin; mucin; adhesion; Trypanosoma cruzi surface protein

Funding

  1. NCRR NIH HHS [RR 03032] Funding Source: Medline
  2. NHLBI NIH HHS [HL 03149] Funding Source: Medline
  3. NIGMS NIH HHS [GM 08037] Funding Source: Medline

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Binding of Trypanosoma cruzi trypomastigotes to laminin is enhanced by galectin-3, a beta-galactoside binding lectin. The galectin-3 enhanced binding of trypanosomes to laminin is inhibited by lactose, Co-immunoprecipitations indicate that galectin-3 binds to the 45, 32 and 30 kDa trypanosome surface proteins. Binding of galectin-3 to the 45, 32 and 30 kDa surface proteins is inhibited by lactose, Polyclonal and a monoclonal antibodies to galectin-3 immnnoprecipitated a major 64 kDa trypanosome surface protein, T. cruzi monoclonal antibody to mucin recognized the 45 kDa surface protein. The 45, 32 and 30 kDa surface proteins interact with galectin-3 in order to enhance trypanosome adhesion to laminin, (C) 2000 Federation of European Biochemical Societies.

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