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• W2040657853 startingPage "511" @default.
• W2040657853 abstract "AbstractBy immunological methods, we show that the monoclonal antibody 6D5 which reacts specifically with Xenopus laevis XB/U-cadherin, also binds to mouse P-cadherin and to chicken B-cadherin but not to the respective E-cadherins (L-CAM) or other “classical” cadherins in these species. In the first extracellular domain, three amino acid residues are identified that are shared by frog XB/U-cadherin, chicken B-cadherin and mammalian P-cadherins but not by the other “classical” cadherins. With few exceptions, the other cadherins possess residues at these positions that are also characteristic of each type of cadherin. Moreover, the expression patterns of P-, B-, and XB/U-cadherin in mouse, chicken and frog are more similar to each other than they are to those of the E-cadherins, L-CAM or other classical cadherins. Taken together, our results suggest that mammalian P-cadherins, chicken B-cadherin and frog XB/U-cadherin are closely related, if not homologous, molecules. A number of differences in the expression patterns between P-, B-, and XB/U-cadherin indicate that these molecules assume differential morphogenetic roles in different species.Key Words: cell-cell adhesioncalcium-dependentcadherin superfamilyexpression analysiscross-species homologuesphylogenesis" @default.
• W2040657853 created "2016-06-24" @default.
• W2040657853 creator A5044566638 @default.
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• W2040657853 date "1994-01-01" @default.
• W2040657853 modified "2023-09-30" @default.
• W2040657853 title "Similarities in Structure and Expression between Mouse P-Cadherin, Chicken B-Cadherin and Frog XB/U-Cadherin" @default.
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• W2040657853 doi "https://doi.org/10.3109/15419069409014215" @default.
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