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dc.contributor.authorSacristán Martín, María Paz 
dc.contributor.authorVestal, D. J.
dc.contributor.authorDours‐Zimmermann, M. T.
dc.contributor.authorRanscht, B.
dc.date.accessioned2024-04-04T11:14:12Z
dc.date.available2024-04-04T11:14:12Z
dc.date.issued1993
dc.identifier.citationSacristan, M. P., Vestal, D. J., Dours‐Zimmermann, M. T., & Ranscht, B. (1993). T‐Cadherin 2: Molecular characterization, function in cell adhesion, and coexpression with T‐cadherin and N‐cadherin. Journal of neuroscience research, 34(6), 664-680.es_ES
dc.identifier.issn0360-4012
dc.identifier.urihttp://hdl.handle.net/10366/157116
dc.description.abstract[EN] Cadherins are integral membrane glycoproteins that mediate calcium-dependent, hornophilic cell-cell adhesion and are implicated in controlling tissue morphogenesis. T-cadherin is anchored to the membrane through a glycosyl phosphatidylinositol and expressed in a restricted pattern in developing embryos. We report here the molecular and functional characterization of the T-cadherin isoform, T-cadherin 2 (Tcad-2) and the expression of the corresponding mRNA. Tcad-2 cDNA differs in its 3’ nucleotide sequence from T-cadherin cDNA and encodes a protein in which the carboxy terminal Leu of T-cadherin is substituted by Lys and extended by the amino acids SerPheProTyrVal. By RNase protection, mRNAs encoding the T-cadherin isoforms are coexpressed in heart, muscle, liver, skin, somites, and in neural tissue. Many tissues contain both T-cadherin and Tcad-2 mRNAs in conjunction with N-cadherin transcripts, and T-cadherins and N-cadherin proteins are coexpressed on the surface of individual neurons in vitro. Expression in Chinese hamster ovary cells (CHO) revealed that Tcad-2 is a glycosyl phosphatidylinositol-anchored membrane protein that functions in calcium-dependent, homophilic cell adhesion. The identification of a functional T-cadherin isoform and the coexpression of T-cadherins and N-cadherin by individual cells suggest that specific adhesive interactions of embryonic cells may involve a complex interplay between multiple cadherins.es_ES
dc.language.isoenges_ES
dc.publisherWiley Online Libraryes_ES
dc.rightsCC0 1.0 Universal*
dc.rights.urihttp://creativecommons.org/publicdomain/zero/1.0/*
dc.subjectCell adhesion moleculees_ES
dc.subjectCalcium dependencees_ES
dc.subjectHomophilic bindinges_ES
dc.subjectT-cadherin isoformses_ES
dc.titleT‐Cadherin 2: Molecular characterization, function in cell adhesion, and coexpression with T‐cadherin and N‐cadherines_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publishversionhttps://doi.org/10.1002/jnr.490340610es_ES
dc.subject.unesco2302 Bioquímicaes_ES
dc.subject.unesco2407 Biología Celulares_ES
dc.subject.unesco2415 Biología Moleculares_ES
dc.identifier.doi10.1002/jnr.490340610
dc.relation.projectIDNational Institute of Health (HD25938)es_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES
dc.identifier.essn1097-4547
dc.journal.titleJournal of Neuroscience Researches_ES
dc.volume.number34es_ES
dc.issue.number6es_ES
dc.page.initial664es_ES
dc.page.final680es_ES
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersiones_ES


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