J. Lipid Res.
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A more recent version of this article appeared on November 1, 2004

Papers In Press, published online ahead of print August 16, 2004
J. Lipid Res., doi:10.1194/jlr.M400137-JLR200
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Submitted on April 12, 2004
Revised on July 19, 2004
Accepted on August 12, 2004

The role of extrahepatic retinol-binding protein (RBP) in the mobilization of retinoid stores

Loredana Quadro, William S. Blaner, Leora Hamberger, Phyllis M. Novikoff, Silke Vogel, Roseann Piantedosi, M. E. Gottesman, and Vittorio Colantuoni

Department of Medicine, Columbia University, New York, NY 10032

Corresponding Author: wsb2{at}columbia.edu

Although the major tissue site of retinol binding protein (RBP) synthesis in the body is liver, other sites of synthesis have been reported. The physiologic role(s) of circulating RBP that is produced and secreted extrahepatically has not been systematically investigated. To address this question, we used as a model a mouse strain (hRBP-/-) that expresses human RBP (hRBP) cDNA under the control of the mouse muscle creatine kinase (MCK) promoter in an rbp null background (RBP-/-). By comparing hRBP-/-, RBP-/- and wild type mice, we asked whether extrahepatic RBP can perform all of the physiologic functions of RBP synthesized in the liver. We demonstrate that extrahepatically synthesized hRBP, unlike RBP expressed in liver, cannot mobilize liver retinoid stores. Consistent with this conclusion, we find that circulating hRBP is not taken up by hepatocytes. RBP has been proposed to play an essential role in distributing hepatic retinoids between hepatocytes and hepatic stellate cells. We find, however, that the distribution of retinoid in the livers of the three mouse strains described above is identical. Thus, RBP is not required for intrahepatic transport and storage of retinoid. These and other observations are discussed.


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