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pubmed-article:8631380pubmed:abstractTextTc-85, an 85-kDa surface glycoprotein specific for the trypomastigote stage of Trypanosoma cruzi, has been implicated in the invasion of host cells by the parasite. Radioactive palmitic acid was incorporated into Tc-85 immunoprecipitated from the culture medium with the H1A10 monoclonal antibody, suggesting that shedding occurs with Tc-85 bearing its GPI anchor. In contrast to the glycoprotein remaining in the parasites, the glycosylphosphatidylinositol moiety in shed Tc-85 is resistant to phosphatidylinositol phospholipase C and becomes susceptible to the enzyme following alkali treatment. An alkylglycerol was identified by thin layer chromatography of an ether extract after the enzymatic reaction. Resistance to cleavage by phospholipase C is due to fatty acid esterification of the inositol residue in shed Tc-85. This is the first example of inositol modification in anchors from a glycoprotein of Trypanosoma cruzi.lld:pubmed
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pubmed-article:8631380pubmed:articleTitleTrypanosoma cruzi: the Tc-85 surface glycoprotein shed by trypomastigotes bears a modified glycosylphosphatidylinositol anchor.lld:pubmed
pubmed-article:8631380pubmed:affiliationDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Brazil.lld:pubmed
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