High impact information on CDH13

• We have characterized T-cadherin, a glycoprotein of 95 kd from chick embryo brain by expression cloning and sequencing of corresponding cDNAs [1].
• To assay the function of T-cadherin in cell adhesion, we have transfected T-cadherin cDNA into CHO cells [2].
• However, immunopurified caveolin-3-containing membranes contained no associated T-cadherin [3].
• T-cadherin could be ADP-ribosylated by a transferase that was also present in the caveolin-enriched Triton-insoluble fraction [3].
• These results suggest that T-cadherin is a major glycophosphoinositol-linked protein in cardiac myocytes and that it may be located in plasma membrane "rafts" distinct from but possibly adjacent to caveolae [3].

Biological context of CDH13

• Glycosyl phosphatidylinositol--anchored T-cadherin mediates calcium-dependent, homophilic cell adhesion [2].
• 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 [4].
• Microsequence analysis of peptides derived from the 100-kDa protein yielded amino acid sequences with high homology to T-cadherin, a truncated cadherin lacking a cytoplasmic domain [3].

Anatomical context of CDH13

• By RNase protection, mRNAs encoding the T-cadherin isoforms are coexpressed in heart, muscle, liver, skin, somites, and in neural tissue [4].
• To test whether glycosyl phosphatidylinositol-linked T-cadherin is a component of cell junctions like classical cadherins, we have examined its distribution and targeting in polarized epithelial cells [5].
• Immunocytochemical analysis of cultured rat atrial myocytes revealed that T-cadherin and caveolin have related but nonoverlapping staining patterns [3].
• In vivo, T-cadherin was detected on the apical cell surface of the chick intestinal epithelium [5].
• T-cadherin is a major glycophosphoinositol-anchored protein associated with noncaveolar detergent-insoluble domains of the cardiac sarcolemma [3].

Associations of CDH13 with chemical compounds

• T-cadherin-containing membrane fragments cofractionated on sucrose gradients with caveolin-3, a marker protein for myocyte caveolae [3].

Other interactions of CDH13

• Thus, GPI-linked T-cadherin is not a component of cell junctions, consistent with a function as a recognition rather than a cell adhesion molecule [5].
• In cultures of transfected Madin-Darby canine kidney cells, T-cadherin was also expressed apically, whereas classical N-cadherin resided basolaterally [5].
• Lastly, we deduce that the chicken ecto-ATPase is not identical to T-cadherin, as has been recently proposed [6].

References