MUCIN-LIKE GLYCOPROTEINS LINKED TO the MEMBRANE BY GLYCOSYLPHOSPHATIDYLINOSITOL ANCHOR ARE the MAJOR ACCEPTORS of SIALIC-ACID in A REACTION CATALYZED BY TRANS-SIALIDASE in METACYCLIC FORMS of TRYPANOSOMA-CRUZI

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dc.contributor.author Schenkman, S.
dc.contributor.author Ferguson, MAJ
dc.contributor.author Heise, N.
dc.contributor.author Dealmeida, MLC
dc.contributor.author Mortara, R. A.
dc.contributor.author Yoshida, N.
dc.date.accessioned 2016-01-24T11:40:13Z
dc.date.available 2016-01-24T11:40:13Z
dc.date.issued 1993-06-01
dc.identifier http://dx.doi.org/10.1016/0166-6851(93)90227-O
dc.identifier.citation Molecular and Biochemical Parasitology. Amsterdam: Elsevier B.V., v. 59, n. 2, p. 293-303, 1993.
dc.identifier.issn 0166-6851
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/25331
dc.description.abstract We have previously shown that 35- and 50-kDa glycoconjugates of cultured metacyclic trypomastigotes participate in the attachment of parasites to mammalian cells. Here we show that when metacyclic trypomastigotes are incubated with [H-3]sialyllactose, most of the sialic acid is transferred to these 35/50-kDa molecules in a reaction catalyzed by a parasite transsialidase. the sialic acid is incorporated in oligosaccharides of about 10 glucose units in size that are released from the glycoconjugate by mild alkaline hydrolysis. Compositional analysis reveals that the 35/50-kDa molecules are highly glycosylated proteins rich in threonine, galactose, N-acetyl-glucosamine and sialic acid. These glycoproteins can be labeled in vivo with [H-3]palmitate, and the labeled fatty acid is released by glycosylphosphatidylinositol specific phospholipases C. This result, associated with the fact that they contain mannose, ethanolamine, myo-inositol, and lipid, indicate that these glycoproteins are anchored to the membrane by glycosylphosphatidylinositol. During cell invasion, these molecules appear to be capped and locally released by the parasite. en
dc.format.extent 293-303
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Molecular and Biochemical Parasitology
dc.rights Acesso restrito
dc.subject TRYPANOSOMA-CRUZI en
dc.subject SIALIC ACID en
dc.subject TRANS-SIALIDASE en
dc.subject CELL INVASION en
dc.subject GLYCOSYLPHOSPHATIDYLINOSITOL en
dc.title MUCIN-LIKE GLYCOPROTEINS LINKED TO the MEMBRANE BY GLYCOSYLPHOSPHATIDYLINOSITOL ANCHOR ARE the MAJOR ACCEPTORS of SIALIC-ACID in A REACTION CATALYZED BY TRANS-SIALIDASE in METACYCLIC FORMS of TRYPANOSOMA-CRUZI en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution UNIV DUNDEE
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation UNIV DUNDEE,DEPT BIOCHEM,DUNDEE DD1 4HN,SCOTLAND
dc.identifier.doi 10.1016/0166-6851(93)90227-O
dc.description.source Web of Science
dc.identifier.wos WOS:A1993LE84900012



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