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J. Biol. Chem., Vol. 277, Issue 9, 7405-7411, March 1, 2002
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From the We have previously shown that
transgenic expression of catalytically inactive lipoprotein lipase
(LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as
whole particle lipoprotein and selective cholesterol ester uptake. In
the current study, we have examined whether these functions can be
performed by inactive LPL alone or require the presence of active LPL
expressed in the same tissue. To study inactive LPL in the presence of
active LPL in the same tissue, the Mck-N-LPL transgene was bred onto
the heterozygous LPL-deficient (LPL1) background. At 18 h
of age, Mck-N-LPL reduced triglycerides by 35% and markedly increased muscle lipid droplets. In adult mice, it reduced triglycerides by 40%
and increased lipoprotein particle uptake into muscle by 60% and
cholesterol ester uptake by 110%. To study inactive LPL alone, the
Mck-N-LPL transgene was bred onto the LPL-deficient (LPL0) background.
These mice die at ~24 h of age. At 18 h of age, in the absence
of active LPL, inactive LPL expression did not diminish triglycerides
nor did it result in the accumulation of muscle lipid droplets. To
study inactive LPL in the absence of active LPL in the same tissue in
adult animals, the Mck-N-LPL transgene was bred onto mice that only
expressed active LPL in the heart (LPL0/He-LPL). In this case,
Mck-N-LPL did not reduce triglycerides or increase the uptake of
lipoprotein particles but did increase muscle uptake of chylomicron and
very low density lipoprotein cholesterol ester by 40%. Thus, in
the presence of active LPL in the same tissue, inactive LPL augments
triglyceride hydrolysis and increases whole particle triglyceride-rich
lipoprotein and selective cholesterol ester uptake. In the absence of
active LPL in the same tissue, inactive LPL only mediates selective
cholesterol ester uptake.
Inactive Lipoprotein Lipase (LPL) Alone Increases
Selective Cholesterol Ester Uptake in Vivo, Whereas in the
Presence of Active LPL It Also Increases Triglyceride Hydrolysis and
Whole Particle Lipoprotein Uptake*
§,,,,
,, and
Department of Medicine, University Hospital
Eppendorf, 20246 Hamburg, Germany, the ¶ Department of
Neuropathology, University of Bonn, Medical Center, 53105 Bonn,
Germany, the Institute of Molecular
Biology, Biochemistry and Microbiology, Karl-Franzens University, 8010 Graz, Austria, the Laboratory of Biochemical Genetics and
Metabolism, Rockefeller University, New York, New York 10021, and the
** Department of Medicine, Columbia University College of
Physicians & Surgeons, New York, New York 10032
*
This work was supported by the German Research Foundation
(Deutsche Forschungsgemeinschaft) Grant Me-1507/2-1 (to M. M.). Histological preparations were supported by the Förderprogramm an
den Medizinischen Einrichtungen Bonn (BONFOR 154/41) (to H. R.).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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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