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Glycosyl phosphatidylinositol--anchored T-cadherin mediates calcium- dependent, homophilic cell adhesion

Cadherins are a family of cell adhesion molecules that exhibit calcium- dependent, homophilic binding. Their function depends on both an HisAlaVal sequence in the first extracellular domain, EC1, and the interaction of a conserved cytoplasmic region with intracellular proteins. T-cadherin is an unus...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1992
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289661/
https://www.ncbi.nlm.nih.gov/pubmed/1400585
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collection PubMed
description Cadherins are a family of cell adhesion molecules that exhibit calcium- dependent, homophilic binding. Their function depends on both an HisAlaVal sequence in the first extracellular domain, EC1, and the interaction of a conserved cytoplasmic region with intracellular proteins. T-cadherin is an unusual member of the cadherin family that lacks the HisAlaVal motif and is anchored to the membrane through a glycosyl phosphatidylinositol moiety (Ranscht, B., and M. T. Dours- Zimmermann. 1991. Neuron. 7:391-402). To assay the function of T- cadherin in cell adhesion, we have transfected T-cadherin cDNA into CHO cells. Two proteins, mature T-cadherin and the uncleaved T-cadherin precursor, were produced from T-cadherin cDNA. The T-cadherin proteins differed from classical cadherins in several aspects. First, the uncleaved T-cadherin precursor was expressed, together with mature T- cadherin, on the surface of the transfected cells. Second, in the absence of calcium, T-cadherin was more resistant to proteolytic cleavage than other cadherins. Lastly, in contrast to classical cadherins, T-cadherin was not concentrated into cell-cell contacts between transfected cells in monolayer cultures. In cellular aggregation assays, T-cadherin induced calcium-dependent, homophilic adhesion which was abolished by treatment of T-cadherin-transfected cells with phosphatidylinositol-specific phospholipase C. These results demonstrate that T-cadherin is a functional cadherin that differs in several properties from classical cadherins. The function of T-cadherin in homophilic cell recognition implies that the mechanism of T-cadherin- induced adhesion is distinct from that of classical cadherins.
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spelling pubmed-22896612008-05-01 Glycosyl phosphatidylinositol--anchored T-cadherin mediates calcium- dependent, homophilic cell adhesion J Cell Biol Articles Cadherins are a family of cell adhesion molecules that exhibit calcium- dependent, homophilic binding. Their function depends on both an HisAlaVal sequence in the first extracellular domain, EC1, and the interaction of a conserved cytoplasmic region with intracellular proteins. T-cadherin is an unusual member of the cadherin family that lacks the HisAlaVal motif and is anchored to the membrane through a glycosyl phosphatidylinositol moiety (Ranscht, B., and M. T. Dours- Zimmermann. 1991. Neuron. 7:391-402). To assay the function of T- cadherin in cell adhesion, we have transfected T-cadherin cDNA into CHO cells. Two proteins, mature T-cadherin and the uncleaved T-cadherin precursor, were produced from T-cadherin cDNA. The T-cadherin proteins differed from classical cadherins in several aspects. First, the uncleaved T-cadherin precursor was expressed, together with mature T- cadherin, on the surface of the transfected cells. Second, in the absence of calcium, T-cadherin was more resistant to proteolytic cleavage than other cadherins. Lastly, in contrast to classical cadherins, T-cadherin was not concentrated into cell-cell contacts between transfected cells in monolayer cultures. In cellular aggregation assays, T-cadherin induced calcium-dependent, homophilic adhesion which was abolished by treatment of T-cadherin-transfected cells with phosphatidylinositol-specific phospholipase C. These results demonstrate that T-cadherin is a functional cadherin that differs in several properties from classical cadherins. The function of T-cadherin in homophilic cell recognition implies that the mechanism of T-cadherin- induced adhesion is distinct from that of classical cadherins. The Rockefeller University Press 1992-10-02 /pmc/articles/PMC2289661/ /pubmed/1400585 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Glycosyl phosphatidylinositol--anchored T-cadherin mediates calcium- dependent, homophilic cell adhesion
title Glycosyl phosphatidylinositol--anchored T-cadherin mediates calcium- dependent, homophilic cell adhesion
title_full Glycosyl phosphatidylinositol--anchored T-cadherin mediates calcium- dependent, homophilic cell adhesion
title_fullStr Glycosyl phosphatidylinositol--anchored T-cadherin mediates calcium- dependent, homophilic cell adhesion
title_full_unstemmed Glycosyl phosphatidylinositol--anchored T-cadherin mediates calcium- dependent, homophilic cell adhesion
title_short Glycosyl phosphatidylinositol--anchored T-cadherin mediates calcium- dependent, homophilic cell adhesion
title_sort glycosyl phosphatidylinositol--anchored t-cadherin mediates calcium- dependent, homophilic cell adhesion
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289661/
https://www.ncbi.nlm.nih.gov/pubmed/1400585