title: [A new family of proteins with high activity for heparin and regulated by retinoic acid].
abstract: An heparin binding protein (RIHB) was purified from chick embryos. Essentially expressed during early embryogenesis it is mainly localized within basement membranes. Its synthesis and that of the RIHB mRNA are induced by retinoic acid in chicken myoblasts cell culture. This protein belongs to the same family that HBGAM or Pleiotropin and MK protein two other heparin binding proteins exhibiting growth and/or neurotrophic activities.
authors.affiliation: INSERM U 118 affiliée CNRS, Paris.
authors.forename: D
authors.initials: D
authors.lastname: Duprez
authors.forename: C
authors.initials: C
authors.lastname: Guettet
authors.forename: P
authors.initials: P
authors.lastname: Urios
authors.forename: D
authors.initials: D
authors.lastname: Raulais
authors.forename: M
authors.initials: M
authors.lastname: Vigny
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis / Q000145:classification* / Q000235:genetics / Q000302:isolation & purification; D002642:Chick Embryo; D005786:Gene Expression Regulation; D006493:Heparin / Q000378:metabolism*; D014212:Tretinoin / Q000494:pharmacology*
chemical_list: D002352:Carrier Proteins; D014212:Tretinoin; D006493:Heparin
vernacular_title: Une nouvelle famille de protéines présentant une forte affinité pour l'héparine et régulées par l'acide rétinoïque.