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Título
T‐Cadherin 2: Molecular characterization, function in cell adhesion, and coexpression with T‐cadherin and N‐cadherin
Autor(es)
Assunto
Cell adhesion molecule
Calcium dependence
Homophilic binding
T-cadherin isoforms
Clasificación UNESCO
2302 Bioquímica
2407 Biología Celular
2415 Biología Molecular
Fecha de publicación
1993
Editor
Wiley Online Library
Citación
Sacristan, 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.
Resumen
[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.
URI
ISSN
0360-4012
DOI
10.1002/jnr.490340610
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