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Originally published In Press as doi:10.1074/jbc.M005118200 on October 5, 2000

J. Biol. Chem., Vol. 276, Issue 2, 1353-1360, January 12, 2001
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Characterization of a New Member of the Fatty Acid-binding Protein Family That Binds All-trans-retinol*

Silke VogelDagger , Cathy L. Mendelsohn§, James R. Mertz, Roseann PiantedosiDagger , Carey Waldburger||, Max E. Gottesman||, and William S. BlanerDagger **Dagger Dagger

From the Departments of Dagger  Medicine, § Urology, and || Microbiology and ** Institute of Human Nutrition, College of Physicians & Surgeons of Columbia University, New York, New York, 10032 and  Department of Biological Sciences, New England College of Optometry, Boston, Massachusetts 02115

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 Kd 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.

* This work was supported by National Institutes of Health Grant R01 DK52444.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Dagger To whom correspondence should be addressed: Dept. of Medicine, Columbia University, 701 W 168th St., New York, NY 10032. Tel.: 212-305-5429; Fax: 212-305-5384; E-mail: WSB2@columbia.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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