title: Molecular cloning of human epimorphin: identification of isoforms and their unique properties.
abstract: Epithelial-mesenchymal interactions are crucial for various epithelial tissue organizations and epimorphin is one of the important signaling molecules from the mesenchyme. The sequence analysis of a human homologue revealed that both of primary and predicted secondary structures of epimorphin are highly conserved among species and this molecule has some isoforms including a putative soluble type. I found that human epimorphins also have a large discrepancy in molecular masses as the case of mouse (around 33kD are predicted by the sequences whereas two protein bands of 60-70kD and 150kD are detected in the cells), and it can be explained, at least in part, by the SDS-resistant complexes formed in the microsomal membranes.
authors: Biomaterial Res. Inst., Yokohama, Japan.
authors: Y
authors: Y
authors: Hirai
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015153:Blotting, Western; D003001:Cloning, Molecular; D005796:Genes; D006801:Humans; D008562:Membrane Glycoproteins / Q000235:genetics* / Q000276:immunology; D051379:Mice; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D014176:Protein Biosynthesis; D016415:Sequence Alignment; D050827:Syntaxin 1
chemical_list: C504582:Epim protein, mouse; D008562:Membrane Glycoproteins; D009838:Oligodeoxyribonucleotides; C074558:STX2 protein, human; D050827:Syntaxin 1