We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Vanadyl acetylacetonate upregulates PPARγ and adiponectin expression in differentiated rat adipocytes.
- Authors
Wu, Yaling; Huang, Meiling; Zhao, Pan; Yang, Xiaoda
- Abstract
Vanadium compounds are promising agents in the therapeutic treatment of diabetes mellitus, but their mechanism of action has not been fully elucidated. The current work investigated the effects of vanadyl acetylacetonate, VO(acac), on peroxisome-proliferator-activated receptor γ (PPARγ) and adiponectin, which are important targets of antidiabetic drugs. The experimental results revealed that vanadyl complexes increased the expression and multimerization of adiponectin in differentiated rat adipocytes. VO(acac) caused activation of p38 mitogen-activated protein kinase (MAPK) and AMP-activated protein kinase (AMPK) and elevation of PPARγ levels. The specific inhibitors SB203580 (p38 MAPK inhibitor) and T0070907 (PPARγ inhibitor) decreased the expression of adiponectin; however, compound C (AMPK inhibitor) did not significantly reduce the expression of adiponectin. In addition, vanadyl complexes induced protein-protein interaction between PPARγ and a vanadium-binding chaperone, heat shock protein 60 kDa. Overall, our results suggest that vanadyl complexes may upregulate PPARγ by suppressing PPARγ degradation, and thus stimulate adiponectin expression and multimerization. The present work has provided new insights into the mechanism of the antidiabetic actions of vanadium compounds.
- Subjects
PEROXISOME proliferator-activated receptors; VANADIUM compounds; ADIPONECTIN; GENETIC regulation; FAT cells; CELL differentiation
- Publication
Journal of Biological Inorganic Chemistry (JBIC), 2013, Vol 18, Issue 6, p623
- ISSN
0949-8257
- Publication type
Academic Journal
- DOI
10.1007/s00775-013-1007-3