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J. Biol. Chem., Vol. 278, Issue 10, 7988-7995, March 7, 2003
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From the Nonesterified long-chain fatty acids may enter
cells by free diffusion or by membrane protein transporters. A
requirement for proteins to transport fatty acids across the plasma
membrane would imply low partitioning of fatty acids into the membrane lipids, and/or a slower rate of diffusion (flip-flop) through the lipid
domains compared to the rates of intracellular metabolism of fatty
acids. We used both vesicles of the plasma membrane of adipocytes and
intact adipocytes to study transmembrane fluxes of externally added
oleic acid at concentrations below its solubility limit at pH 7.4. Binding of oleic acid to the plasma membrane was determined by
measuring the fluorescent fatty acid-binding protein ADIFAB added to
the external medium. Changes in internal pH caused by flip-flop and
metabolism were measured by trapping a fluorescent pH indicator in the
cells. The metabolic end products of oleic acid were evaluated over the
time interval required for the return of intracellular pH to its
initial value. The primary findings were that (i) oleic acid rapidly
binds with high avidity in the lipid domains of the plasma membrane
with an apparent partition coefficient similar to that of protein-free
phospholipid bilayers; (ii) oleic acid rapidly crosses the plasma
membrane by the flip-flop mechanism (both events occur within 5 s); and (iii) the kinetics of esterification of oleic acid closely
follow the time dependence of the recovery of intracellular pH. Any
postulated transport mechanism for facilitating translocation of fatty
acid across the plasma membrane of adipocytes, including a protein
transporter, would have to compete with the highly effective flip-flop mechanism.
Rapid Flip-flop of Oleic Acid across the Plasma Membrane of
Adipocytes*
§,¶
,**,**, and¶
Obesity Research Center, Boston Medical
Center, Boston, Massachusetts 02118 and the Departments of
¶ Physiology and Biophysics, Medicine and
** Biochemistry, Boston University School of Medicine,
Boston, Massachusetts 02118
*
This work was supported by National Institutes of Health
Grants HL26335 (to J. A. H.) and DK30425 and DK56935 (to
P. F. P.).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: Dept. of Physiology
and Biophysics, Boston University School of Medicine, 715 Albany St.,
Boston, MA 02118. Tel.: 617-638-5048; Fax: 617-638-4041; E-mail:
jhamilt@bu.edu.
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