Expression of a novel cadherin (EP-cadherin) in unfertilized eggs and early Xenopus embryos.
Two distinct cadherin cDNA clones of Xenopus laevis were isolated from a stage 17 embryo cDNA library. Analysis of the complete deduced amino acid sequences indicated that one of these molecules is closely homologous to chicken and mouse N-cadherin, while the other displays comparable homology to both E- and P-cadherins and was thus denoted EP-cadherin. This molecule has an apparent relative molecular mass of 125 x 10(3) (compared to approx. 138 x 10(3) or approx. 140 x 10(3) of E-cadherin and N-cadherins, respectively). Northern and Western blot analyses indicated that N-cadherin is first expressed at the neurula stage while EP-cadherin is the only cadherin detected in unfertilized eggs and cleavage stage embryos. Immunolabeling of Xenopus eggs with antibodies prepared against a fusion protein, containing a segment of EP-cadherin, indicated that the protein is highly enriched at the periphery of the animal hemisphere. EP-cadherin was also found in A6 epithelial cells derived from Xenopus kidneys, and was apparently localized in the intercellular adherens junctions.
Ginsberg
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D
Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.
DeSimone
D
D
Geiger
B
B
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D001483:Base Sequence; D015152:Blotting, Northern; D015820:Cadherins / Q000235:genetics* / Q000276:immunology; D004270:DNA, Circular / Q000032:analysis*; D004625:Embryo, Nonmammalian / Q000502:physiology*; D005455:Fluorescent Antibody Technique; D015151:Immunoblotting; D007365:Intercellular Junctions / Q000737:chemistry; D007668:Kidney / Q000737:chemistry; D008969:Molecular Sequence Data; D010063:Ovum / Q000502:physiology*; D014981:Xenopus
D000911:Antibodies, Monoclonal; D015820:Cadherins; D004270:DNA, Circular