Premium
Differential effects of chronic, in vivo, PPAR's stimulation on the myocardial subcellular redistribution of FAT/CD36 and FABPpm
Author(s) -
Kalinowska Agnieszka,
Górski Jan,
Harasim Ewa,
Harasiuk Dorota,
Bonen Arend,
Chabowski Adrian
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.07.008
Subject(s) - cd36 , peroxisome proliferator activated receptor , stimulation , downregulation and upregulation , ampk , peroxisome , fatty acid , chemistry , beta oxidation , medicine , endocrinology , subcellular localization , intracellular , in vivo , ppar agonist , rosiglitazone , microbiology and biotechnology , receptor , biology , biochemistry , protein kinase a , enzyme , cytoplasm , gene
This study reveals that the activation of either PPARα (WY 14 643) or PPARβ (GW0742) each induce the translocation of FAT/CD36 from an intracellular pool(s) to the plasma membrane, while PPARβ also induces the subcellular redistribution of FABPpm(Got2) to the plasma membrane. In contrast, activation of PPARγ failed to induce the subcellular redistribution of FAT/CD36 and FABPpm. These PPARα‐, and PPARβ‐induced changes in the plasmalemmal content of these fatty acid transporters were associated with the concurrent upregulation of fatty acid triacylglycerol esterification (PPARβ) and oxidation (PPARα and PPARβ). Observed effects of chronic PPAR stimulation were not related to either AMPK or ERK1/2 activation.