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J. Biol. Chem., Vol. 280, Issue 25, 24286-24292, June 24, 2005

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Cellular Retinol-binding Protein Type III Is Needed for Retinoid Incorporation into Milk^*

Roseann Piantedosi, Norbert Ghyselinck, William S. Blaner, and Silke Vogel¶

From the Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, New York 10032 and Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS/INSERM/Universite Louis Pasteur, College de France, BP 101042, 67404 Illkirch Cedex, France

The physiologic role(s) of cellular retinol-binding protein (CRBP)-III, an intracellular retinol-binding protein that is expressed solely in heart, muscle, adipose, and mammary tissue, remains to be elucidated. To address this, we have generated and characterized CRBP-III-deficient (CRBP-III^-/-) mice. Mice that lack CRBP-III were viable and healthy but displayed a marked impairment in retinoid incorporation into milk. Milk obtained from CRBP-III^-/- dams contains significantly less retinyl ester, especially retinyl palmitate, than milk obtained from wild type dams. We demonstrated that retinol bound to CRBP-III is an excellent substrate for lecithin-retinol acyltransferase, the enzyme responsible for catalyzing retinyl ester formation from retinol. Our data indicated that the diminished milk retinyl ester levels arise from impaired utilization of retinol by lecithin-retinol acyltransferase in CRBP-III^-/- mice. Interestingly, CRBP-I and CRBP-III each appeared to compensate for the absence of the other, specifically in mammary tissue, adipose tissue, muscle, and heart. For CRBP-III^-/- mice, CRBP-I protein levels were markedly elevated in adipose tissue and mammary gland. In addition, in CRBP-I^-/- mice, CRBP-III protein levels were elevated in tissues that normally express CRBP-III but were not elevated in other tissues that do not normally express CRBP-III. Our data suggested that CRBP-I and CRBP-III share some physiologic actions within tissues and that each can compensate for the absence of the other to help maintain normal retinoid homeostasis. However, under conditions of high demand for retinoid, such as those experienced during lactation, this compensation was incomplete.

Received for publication, April 11, 2005 , and in revised form, May 2, 2005.

^* This work was supported by National Institutes of Health Grants DK052444 (to W. S. B.), DK068437 (to W. S. B.), and DK067512 (to S. V.) and United States Department of Agriculture Grant 35208-11578 (to S. V.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed: Dept. of Medicine, Division of Preventive Medicine and Nutrition, Columbia University, 630 W. 168th St., P&S 9-510, New York, NY 10032. Tel.: 212-305-0062; Fax: 212-305-2801; E-mail: sv98{at}columbia.edu.

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