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Induced adiposity and adipocyte hypertrophy in mice lacking the AMP-activated protein kinase-alpha2 subunit.
- Source :
-
Diabetes [Diabetes] 2004 Sep; Vol. 53 (9), pp. 2242-9. - Publication Year :
- 2004
-
Abstract
- AMP-activated protein kinase (AMPK) is considered as a cellular energy sensor that regulates glucose and lipid metabolism by phosphorylating key regulatory enzymes. Despite the major role of adipose tissue in regulating energy partitioning in the organism, the role of AMPK in this tissue has not been addressed. In the present study, we subjected AMPKalpha2 knockout (KO) mice to a high-fat diet to examine the effect of AMPK on adipose tissue formation. Compared with the wild type, AMPKalpha2 KO mice exhibited increased body weight and fat mass. The increase in adipose tissue mass was due to the enlargement of the preexisting adipocytes with increased lipid accumulation. However, we did not observe any changes in adipocyte marker expression, such as peroxisome proliferator-activated receptor-gamma, CCAAT/enhancer-binding protein alpha (C/EBPalpha) and adipocyte fatty acid-binding protein (aFABP/aP2), or total cell number. Unlike impaired glucose homeostasis observed on normal diet feeding, when fed a high-fat diet AMPKalpha2 KO mice did not show differences in glucose tolerance and insulin sensitivity compared with wild-type mice. Our results suggest that the increase in lipid storage in adipose tissue in AMPKalpha2 KO mice may have protected these mice from further impairment of glucose homeostasis that normally accompanies high-fat feeding. Our study also demonstrates that lack of AMPKalpha2 subunit may be a factor contributing to the development of obesity.
- Subjects :
- AMP-Activated Protein Kinases
Adipose Tissue metabolism
Adipose Tissue pathology
Animals
Body Weight
Cell Size
Dietary Fats pharmacology
Glucose Tolerance Test
Hypertrophy
Insulin Resistance
Mice
Mice, Inbred C57BL
Mice, Knockout
Obesity metabolism
Obesity pathology
Triglycerides metabolism
Adipocytes enzymology
Adipocytes pathology
Multienzyme Complexes genetics
Multienzyme Complexes metabolism
Obesity physiopathology
Protein Serine-Threonine Kinases genetics
Protein Serine-Threonine Kinases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0012-1797
- Volume :
- 53
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Diabetes
- Publication Type :
- Academic Journal
- Accession number :
- 15331533
- Full Text :
- https://doi.org/10.2337/diabetes.53.9.2242