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J. Biol. Chem., Vol. 275, Issue 42, 32523-32529, October 20, 2000
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From the The transmembrane protein CD36 has been
identified in isolated cell studies as a putative transporter of long
chain fatty acids. In humans, an association between CD36 deficiency
and defective myocardial uptake of the fatty acid analog
15-(p-iodophenyl)-3-(R,S)-methyl pentadecanoic
acid (BMIPP) has been reported. To determine whether this association
represents a causal link and to assess the physiological role of CD36,
we compared tissue uptake and metabolism of two iodinated fatty acid
analogs BMIPP and 15-(p-iodophenyl) pentadecanoic acid
(IPPA) in CD36 null and wild type mice. We also investigated the uptake
and lipid incorporation of palmitate by adipocytes isolated from both
groups. Compared with wild type, uptake of BMIPP and IPPA was reduced
in heart (50-80%), skeletal muscle (40-75%), and adipose tissues
(60-70%) of null mice. The reduction was associated with a 50-68%
decrease in label incorporation into triglycerides and in 2-3-fold
accumulation of label in diglycerides. Identical results were obtained
from studies of [3H]palmitate uptake in isolated
adipocytes. The block in diglyceride to triglyceride conversion could
not be explained by changes in specific activities of the key enzymes
long chain acyl-CoA synthetase and diacylglycerol acyltransferase,
which were similar in tissues from wild type and null mice. It is
concluded that CD36 facilitates a large fraction of fatty acid uptake
by heart, skeletal muscle, and adipose tissues and that CD36 deficiency
in humans is the cause of the reported defect in myocardial BMIPP
uptake. In CD36-expressing tissues, uptake regulates fatty acid
esterification at the level of diacylglycerol acyltransferase by
determining fatty acyl-CoA supply. The membrane transport step may
represent an important control site for fatty acid metabolism in
vivo.
Defective Uptake and Utilization of Long Chain Fatty Acids in
Muscle and Adipose Tissues of CD36 Knockout Mice*
,
Department of Physiology and Biophysics,
State University of New York, Stony Brook, New York 11794-8661, the
§ Nuclear Medicine Program, Oak Ridge National Laboratory,
Oak Ridge, Tennessee 37831, and the ¶ Department of
Medicine, Division of Hematology and Medical Oncology, Weill
Medical College of Cornell University, New York, New York 10021
*
This work was supported by National Institutes of Health
Grants DK33301 (to N. A. A.), 1R29 HL58559 (to M. F.), and HL42540 (to R. L. S.), United States Department of Energy Contract
DE-AC05-96OR22464 (to F. F. K.), and by a gift from Sumitomo Chemical
Co., Japan (to N. A. A.).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 addressed. Tel.:
631-444-3489; Fax: 631-444-3432; E-mail: NadaA@
Physiology.pnb.sunysb.edu.
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