Cellular prion protein binds laminin and mediates neuritogenesis

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dc.contributor.authorGraner, E.
dc.contributor.authorMercadante, A. F.
dc.contributor.authorZanata, S. M.
dc.contributor.authorForlenza, O. V.
dc.contributor.authorCabral, ALB
dc.contributor.authorVeiga, S. S.
dc.contributor.authorJuliano, M. A.
dc.contributor.authorRoesler, R.
dc.contributor.authorWalz, R.
dc.contributor.authorMinetti, A.
dc.contributor.authorIzquierdo, I
dc.contributor.authorMartins, V. R.
dc.contributor.authorBrentani, R. R.
dc.contributor.institutionLudwig Inst Canc Res
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUFRGS
dc.contributor.institutionCtr Tratamento
dc.contributor.institutionPesquisa Hosp Canc
dc.date.accessioned2016-01-24T12:31:02Z
dc.date.available2016-01-24T12:31:02Z
dc.date.issued2000-03-10
dc.description.abstractLaminin (LN) plays a major role in neuronal differentiation, migration and survival. Here, we show that the cellular prion protein (PrPc) is a saturable, specific, high-affinity receptor for LN. the PrPc-LN interaction is involved in the neuritogenesis induced by NGF plus LN in the PC-12 cell line and the binding site resides in a carboxy-terminal decapeptide from the gamma-1 LN chain. Neuritogenesis induced by LN or its gamma-1-derived peptide in primary cultures from rat or either wild type or PrP null mice hippocampal neurons, indicated that PrPc is the main cellular receptor for that particular LN domain. These results point out to the importance of the PrPc-LN interaction for the neuronal plasticity mechanism. (C) 2000 Elsevier Science B.V. All rights reserved.en
dc.description.affiliationLudwig Inst Canc Res, São Paulo Branch, BR-01509010 São Paulo, Brazil
dc.description.affiliationUSP, Fac Med, Inst Psiquiatria, Lab Invest Med LIM 27, BR-09500900 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, INFAR, São Paulo, Brazil
dc.description.affiliationUFRGS, Inst Ciencias Basicas Saude, Dept Bioquim, BR-90035003 Porto Alegre, RS, Brazil
dc.description.affiliationCtr Tratamento, BR-01509010 São Paulo, Brazil
dc.description.affiliationPesquisa Hosp Canc, BR-01509010 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, INFAR, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent85-92
dc.identifierhttp://dx.doi.org/10.1016/S0169-328X(99)00334-4
dc.identifier.citationMolecular Brain Research. Amsterdam: Elsevier B.V., v. 76, n. 1, p. 85-92, 2000.
dc.identifier.doi10.1016/S0169-328X(99)00334-4
dc.identifier.issn0169-328X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/26270
dc.identifier.wosWOS:000085921300010
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofMolecular Brain Research
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectcellular prion proteinen
dc.subjectextracellular matrixen
dc.subjecthippocampal neuronen
dc.subjectlamininen
dc.subjectneurite outgrowthen
dc.subjectPC-12 cell lineen
dc.titleCellular prion protein binds laminin and mediates neuritogenesisen
dc.typeinfo:eu-repo/semantics/article
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