title: Characterization of a new member of the fatty acid-binding protein family that binds all-trans-retinol.
abstract: Cellular retinol-binding protein, type I (CRBP-I) and type II (CRBP-II) are the only members of the fatty acid-binding protein (FABP) family that process intracellular retinol. Heart and skeletal muscle take up postprandial retinol but express little or no CRBP-I or CRBP-II. We have identified an intracellular retinol-binding protein in these tissues. The 134-amino acid protein is encoded by a cDNA that is expressed primarily in heart, muscle and adipose tissue. It shares 57 and 56% sequence identity with CRBP-I and CRBP-II, respectively, but less than 40% with other members of the FABP family. In situ hybridization demonstrates that the protein is expressed at least as early as day 10 in developing heart and muscle tissue of the embryonic mouse. Fluorescence titrations of purified recombinant protein with retinol isomers indicates binding to all-trans-, 13-cis-, and 9-cis-retinol, with respective K(d) values of 109, 83, and 130 nm. Retinoic acids (all-trans-, 13-cis-, and 9-cis-), retinals (all-trans-, 13-cis-, and 9-cis-), fatty acids (laurate, myristate, palmitate, oleate, linoleate, arachidonate, and docosahexanoate), or fatty alcohols (palmityl, petrosenlinyl, and ricinolenyl) fail to bind. The distinct tissue expression pattern and binding specificity suggest that we have identified a novel FABP family member, cellular retinol-binding protein, type III.
authors.affiliation: Department of Medicine, Institute of Human Nutrition, College of Physicians & Surgeons of Columbia University, New York, New York, 10032, USA.
authors.forename: S
authors.initials: S
authors.lastname: Vogel
authors.forename: C L
authors.initials: CL
authors.lastname: Mendelsohn
authors.forename: J R
authors.initials: JR
authors.lastname: Mertz
authors.forename: R
authors.initials: R
authors.lastname: Piantedosi
authors.forename: C
authors.initials: C
authors.lastname: Waldburger
authors.forename: M E
authors.initials: ME
authors.lastname: Gottesman
authors.forename: W S
authors.initials: WS
authors.lastname: Blaner
mesh_terms: D000273:Adipose Tissue / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D003001:Cloning, Molecular; D018076:DNA, Complementary; D004926:Escherichia coli; D018507:Gene Expression Regulation, Developmental; D006321:Heart / Q000196:embryology / Q000254:growth & development; D017403:In Situ Hybridization; D007700:Kinetics; D051379:Mice; D008969:Molecular Sequence Data; D024510:Muscle Development; D018482:Muscle, Skeletal / Q000196:embryology / Q000254:growth & development / Q000378:metabolism; D009206:Myocardium / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D012177:Retinol-Binding Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D054840:Retinol-Binding Proteins, Cellular; D020133:Reverse Transcriptase Polymerase Chain Reaction; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D018411:Spodoptera; D013379:Substrate Specificity; D014162:Transfection; D014801:Vitamin A / Q000378:metabolism*
chemical_list: D018076:DNA, Complementary; C518460:Rbp2 protein, mouse; C521400:Rbp7 protein, mouse; D011994:Recombinant Proteins; D012177:Retinol-Binding Proteins; D054840:Retinol-Binding Proteins, Cellular; D014801:Vitamin A