Abstract
This study reveals that the activation of either PPARalpha (WY 14643) or PPARbeta (GW0742) each induce the translocation of FAT/CD36 from an intracellular pool(s) to the plasma membrane, while PPARbeta also induces the subcellular redistribution of FABPpm(Got2) to the plasma membrane. In contrast, activation of PPARgamma failed to induce the subcellular redistribution of FAT/CD36 and FABPpm. These PPARalpha-, and PPARbeta-induced changes in the plasmalemmal content of these fatty acid transporters were associated with the concurrent upregulation of fatty acid triacylglycerol esterification (PPARbeta) and oxidation (PPARalpha and PPARbeta). Observed effects of chronic PPAR stimulation were not related to either AMPK or ERK1/2 activation.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
AMP-Activated Protein Kinases / genetics
-
AMP-Activated Protein Kinases / metabolism
-
Animals
-
CD36 Antigens / genetics
-
CD36 Antigens / metabolism*
-
Cell Membrane / metabolism
-
Extracellular Signal-Regulated MAP Kinases / genetics
-
Extracellular Signal-Regulated MAP Kinases / metabolism
-
Fatty Acid-Binding Proteins / genetics
-
Fatty Acid-Binding Proteins / metabolism*
-
Fatty Acids / chemistry
-
Fatty Acids / metabolism
-
Lipid Peroxidation
-
Male
-
Myocardium / cytology
-
Myocardium / metabolism*
-
PPAR alpha / metabolism*
-
PPAR gamma / metabolism*
-
PPAR-beta / metabolism*
-
Palmitates / chemistry
-
Palmitates / metabolism
-
Rats
-
Rats, Wistar
Substances
-
CD36 Antigens
-
Fatty Acid-Binding Proteins
-
Fatty Acids
-
Got2 protein, rat
-
PPAR alpha
-
PPAR gamma
-
PPAR-beta
-
Palmitates
-
Extracellular Signal-Regulated MAP Kinases
-
AMP-Activated Protein Kinases