Show simple item record

dc.contributor.authorAcosta-Serrano, A.
dc.contributor.authorAlmeida, I. C.
dc.contributor.authorFreitas, L. H.
dc.contributor.authorYoshida, N.
dc.contributor.authorSchenkman, S.
dc.date.accessioned2016-01-24T12:31:22Z
dc.date.available2016-01-24T12:31:22Z
dc.date.issued2001-05-01
dc.identifierhttp://dx.doi.org/10.1016/S0166-6851(01)00245-6
dc.identifier.citationMolecular and Biochemical Parasitology. Amsterdam: Elsevier B.V., v. 114, n. 2, p. 143-150, 2001.
dc.identifier.issn0166-6851
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/26542
dc.description.abstractTrypanosoma cruzi expresses at its surface large amounts of mucin-like glycoproteins. the T. cruzi mucins (TcMUC), a group of highly glycosylated GPI-anchored proteins rich in Thr, Ser, and Pro residues, are expressed in high copy numbers in both insect and mammalian stages of the parasite. These molecules are encoded by a multigene family and contain a unique type of glycosylation consisting of several sialylated O-glycans linked to the protein backbone via Nw-acetylglucosamine residues. the TcMUC are important because of their role in host cell invasion and the ability to induce secretion of proinflammatory cytokines and nitric oxide in activated macrophages. the TcMUC are also significant in being the major substrate for the cell surface trans-sialidase. in this review, we summarize the recent knowledge on the molecular structure and function of this family of T. cruzi glycoproteins. (C) 2001 Elsevier Science B.V. All rights reserved.en
dc.format.extent143-150
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofMolecular and Biochemical Parasitology
dc.rightsAcesso restrito
dc.subjectTrypanosoma cruzien
dc.subjectmucinsen
dc.subjectsialic aciden
dc.subjecttrans-sialidaseen
dc.subjectGPIen
dc.subjectglycosylationen
dc.titleThe mucin-like glycoprotein super-family of Trypanosoma cruzi: structure and biological rolesen
dc.typeResenha
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institutionJohns Hopkins Univ
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.description.affiliationJohns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA
dc.description.affiliationUniv São Paulo, ICB2, Dept Parasitol, BR-05508900 São Paulo, Brazil
dc.description.affiliationUNIFESP, Escola Paulista Med, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifespUNIFESP, Escola Paulista Med, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.identifier.doi10.1016/S0166-6851(01)00245-6
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000168924900002


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record