title: Characterization of the bovine tenascin-X.
abstract: The primary structure of flexilin, an extracellular matrix glycoprotein previously identified in bovine tissues (Lethias, C., Descollonges, Y., Boutillon, M.-M., and Garrone, R. (1996) Matrix Biol. 15, 11-19) was determined by cDNA cloning. The deduced amino acid sequence (4135 residues) reveals that this protein is composed of a succession of peptide motifs characteristic of the tenascin family: an amino-terminal domain containing cysteine residues and heptads of hydrophobic amino acids, 18.5 epidermal growth factor-like repeats, 30 fibronectin type III-like (FNIII) domains, and a carboxyl-terminal fibrinogen-like motif. Sequence analysis indicated that this protein is the bovine orthologue of human tenascin-X. By rotary shadowing, bovine tenascin-X was identified as monomers with a flexible aspect, which are ended by a globule. More FNIII motifs were characterized in the bovine protein than in human tenascin-X. The main difference between the human and bovine tenascin-X is found in the arrangement of the three classes of highly similar FNIII repeat types in the central region of tenascin-X. The bovine FNIII motif b10 exhibits an RGD putative cell attachment site. The functional role of this sequence is corroborated by cell adhesion on purified tenascin-X, which is inhibited by RGD peptides. Moreover, we demonstrate that this RGD site is conserved at the same location in the human molecule.
authors.affiliation: Institut de Biologie et Chimie des Protéines, CNRS, Unité Propre de Recherche 412, Université Claude Bernard, 7 passage du Vercors, 69367 Lyon cedex 07, France.
authors.forename: F
authors.initials: F
authors.lastname: Elefteriou
authors.forename: J Y
authors.initials: JY
authors.lastname: Exposito
authors.forename: R
authors.initials: R
authors.lastname: Garrone
authors.forename: C
authors.initials: C
authors.lastname: Lethias
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D003001:Cloning, Molecular; D018076:DNA, Complementary; D006801:Humans; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid; D019063:Tenascin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D018076:DNA, Complementary; D009842:Oligopeptides; D019063:Tenascin; C081865:tenascin X; C047981:arginyl-glycyl-aspartic acid