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Originally published In Press as doi:10.1074/jbc.M102791200 on July 12, 2001

J. Biol. Chem., Vol. 276, Issue 38, 35990-35994, September 21, 2001
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Lipoprotein Lipase and Leptin Are Accumulated in Different Secretory Compartments in Rat Adipocytes*

Cecilia RohDagger , Raphael Roduit§, Bernard Thorens§, Susan Fried, and Konstantin V. KandrorDagger ||

From the Dagger  Boston University School of Medicine, Boston, Massachusetts 02118, § University of Lausanne, Lausanne, Switzerland, CH 1005, and  Rutgers University, New Brunswick, New Jersey 08901

Adipose cells produce and secrete several physiologically important proteins, such as lipoprotein lipase (LPL), leptin, adipsin, Acrp30, etc. However, secretory pathways in adipocytes have not been characterized, and vesicular carriers responsible for the accumulation and transport of secreted proteins have not been identified. We have compared the intracellular localization of two proteins secreted from adipose cells: leptin and LPL. Adipocytes accumulate large amounts of both proteins, suggesting that neither of them is targeted to the constitutive secretory pathway. By means of velocity centrifugation in sucrose gradients, equilibrium density centrifugation in iodixanol gradients, and immunofluorescence confocal microscopy, we determined that LPL and leptin were localized in different membrane structures. LPL was found mainly in the endoplasmic reticulum with a small pool being present in low density membrane vesicles that may represent a secretory compartment in adipose cells. Virtually all intracellular leptin was localized in these low density secretory vesicles. Insulin-sensitive Glut4 vesicles did not contain either LPL or leptin. Thus, secretion from adipose cells is controlled both at the exit from the endoplasmic reticulum as well as at the level of "downstream" secretory vesicles.


* This work was supported by Research Grants DK52057 and DK56736 from the National Institutes of Health and by a research grant from the American Diabetes Association (to K. V. K.).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.

|| To whom correspondence should be sent: Boston University School of Medicine, Dept. of Biochemistry, K121, 715 Albany St., Boston, MA 02118. Tel.: 617-638-5049; Fax: 617-638-5339; E-mail: kandror@biochem.bumc.bu.edu.


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