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[Untitled]
- Source :
- Molecular and Cellular Biochemistry. 166:153-158
- Publication Year :
- 1997
- Publisher :
- Springer Science and Business Media LLC, 1997.
-
Abstract
- The present study was designed to investigate the presence of the fatty acid-binding protein (FABP(PM)) in the plasma membranes of skeletal muscles with different oxidative capacities for free fatty acid (FFA) oxidation during conditions of normal (fed) or increased (fasted) FFA utilization in the rat. Female Sprague-Dawley rats were either fed or fasted for 12, 24, or 48 h and, plasma membranes (PM) fractions from red and white skeletal muscles were isolated. Short-term fasting significantly decreased body weight by 11% and blood glucose concentration by 42% (6.6+/-0.2-3.8+/-0.4 mmol/l) and increased plasma FFA concentration by 5-fold (133+/-14-793+/-81 micromol/l). Immunoblotting of PM fractions showed that FABP(PM) protein content was 83+/-18% higher in red than in white skeletal muscle and correlated with oxidative capacity as measured by succinate dehydrogenase activity (r = 0.78, p < 0.05). Short-term fasting significantly increased FABP(PM) protein content by 60+/-8% in red skeletal muscle but no change was measured in white skeletal muscle. These results show that FABP(PM) protein content in skeletal muscle is related to oxidative potential and can be increased during a physiological condition known to be associated with an increase in FFA utilization, suggesting that cellular expression of FABP(PM) may play a role in the regulation of FFA metabolism in skeletal muscle.
- Subjects :
- chemistry.chemical_classification
medicine.medical_specialty
biology
Clinical chemistry
Physiological condition
Succinate dehydrogenase
Clinical Biochemistry
Fatty acid
Skeletal muscle
Cell Biology
General Medicine
Metabolism
Oxidative phosphorylation
Fatty acid-binding protein
Endocrinology
medicine.anatomical_structure
chemistry
Internal medicine
biology.protein
medicine
lipids (amino acids, peptides, and proteins)
Molecular Biology
Subjects
Details
- ISSN :
- 03008177
- Volume :
- 166
- Database :
- OpenAIRE
- Journal :
- Molecular and Cellular Biochemistry
- Accession number :
- edsair.doi...........9dc5760d0aa87b0cdfb20c582203435f
- Full Text :
- https://doi.org/10.1023/a:1006846907394