title: Molecular cloning and characterization of chick CD9.
abstract: CD9 is a tetra-membrane-spanning glycoprotein involved in cell adhesion, migration, growth signaling and tumor cell metastasis. In this study a CD9 cDNA clone has been isolated from chick cDNA library. The chick CD9 clone contains an open reading frame of 224 amino acids. The deduced amino acid sequence from chick CD9 shows 63.3% identity with the human counterpart. Human and monkey CD9 upregulate the diphtheria toxin (DT) binding activity of human heparin-binding EGF-like growth factor, while chick CD9 lacks the ability to upregulate the DT binding activity. Comparison of the amino acid sequence of chick CD9 with that of human CD9 gives a clue to understanding the upregulation mechanism.
authors.affiliation: Division of Cell Biology, Kurume University, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Kobayashi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015703:Antigens, CD / Q000235:genetics*; D001483:Base Sequence; D002460:Cell Line; D002642:Chick Embryo; D003001:Cloning, Molecular; D018076:DNA, Complementary; D006801:Humans; D008562:Membrane Glycoproteins / Q000235:genetics*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D060245:Tetraspanin 29
chemical_list: D015703:Antigens, CD; C554869:CD9 protein, human; D018076:DNA, Complementary; D008562:Membrane Glycoproteins; D060245:Tetraspanin 29