Related Articles13C/31P NMR assessment of mitochondrial energy coupling in skeletal muscle of awake fed and fasted rats. Relationship with uncoupling protein 3 expression.
J Biol Chem. 2000 Dec 15;275(50):39279-86
Authors: Jucker BM, Ren J, Dufour S, Cao X, Previs SF, Cadman KS, Shulman GI
To examine the relationship between mitochondrial energy coupling in skeletal muscle and change in uncoupling protein 3 (UCP3) expression during the transition from the fed to fasted state, we used a novel noninvasive (31)P/(13)C NMR spectroscopic approach to measure the degree of mitochondrial energy coupling in the hind limb muscles of awake rats before and after a 48-h fast. Compared with fed levels, UCP3 mRNA and protein levels in the gastrocnemius increased 1.7- (p < 0.01) and 2.9-fold (p < 0.001), respectively, following a 48-h fast. Tricarboxylic acid cycle flux measured using (13)C NMR as an index of mitochondrial substrate oxidation was 212 +/- 23 and 173 +/- 25 nmol/g/min (p not significant) in the fed and 48-h fasted groups, respectively. Unidirectional ATP synthesis flux measured using (31)P NMR was 79 +/- 15 and 57 +/- 9 nmol/g/s (p not significant) in the fed and 48-h fasted groups, respectively. Mitochondrial energy coupling as expressed by the ratio of ATP synthesis to tricarboxylic acid cycle flux was not different between the fed and fasted states. To test the hypothesis that UCP3 may be involved in the translocation of long chain free fatty acids (FFA) into the mitochondrial matrix under conditions of elevated FFA availability, [U-(13)C]palmitate/albumin was administered in a separate group of rats with (+) or without (-) etomoxir (an inhibitor of carnitine palmitoyltransferase I). The ratio of glutamate enrichment ((+) etomoxir/(-) etomoxir) in the hind limb muscles was the same between groups, indicating that UCP3 does not appear to function as a translocator for long chain FFA in skeletal muscle following a 48-h fast. In summary, these data demonstrate that despite a 2-3-fold increase in UCP3 mRNA and protein expression in skeletal muscle during the transition from the fed to fasted state, mitochondrial energy coupling does not change. Furthermore, UCP3 does not appear to have a major role in FFA translocation into the mitochondria. The physiological role of UCP3 following a 48-h fast in skeletal muscle remains to be elucidated.
Skeletal muscle lipid metabolism studied by advanced magnetic resonance spectroscopy
Skeletal muscle lipid metabolism studied by advanced magnetic resonance spectroscopy
Publication year: 2012
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, Available online 23 February 2012</br>
Arunima*Pola, Suresh Anand*Sadananthan, Jadegoud*Yaligar, Vijayasarathi*Nagarajan, Weiping*Han, ...</br>
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02-26-2012 05:01 AM
Effect of ischemic preconditioning in skeletal muscle measured by functional ... - 7thSpace Interactive (press release)
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Effect of ischemic preconditioning in skeletal muscle measured by functional ...
7thSpace Interactive (press release)
Nuclear magnetic resonance (NMR) imaging and spectroscopy have been applied to assess skeletal muscle oxidative metabolism. Therefore, in-vivo NMR may enable the characterization of ischemia-reperfusion injury. The goal of this study was to evaluate ...
Protein NMR Spectroscopy: Practical Techniques and ApplicationsspectroscopyNOW.com
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Effect of ischemic preconditioning in skeletal muscle measured by...
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07-26-2011 11:22 PM
A NMR-based metabolomic approach for differentiation of hagfish dental and somatic skeletal muscles.
A NMR-based metabolomic approach for differentiation of hagfish dental and somatic skeletal muscles.
A NMR-based metabolomic approach for differentiation of hagfish dental and somatic skeletal muscles.
Fish Physiol Biochem. 2011 Feb 15;
Authors: Chiu KH, Ding S, Chen YW, Lee CH, Mok HK
The hagfish dental muscle is a large and specialized element of the feeding apparatus that helps ingest food. This muscle has enzymatic activities and contractile properties different from the hagfish somatic skeletal muscle. To verify the functional relevance of...
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02-18-2011 08:07 PM
[NMR paper] Proton NMR spectroscopy shows lipids accumulate in skeletal muscle in response to burn trauma-induced apoptosis.
Proton NMR spectroscopy shows lipids accumulate in skeletal muscle in response to burn trauma-induced apoptosis.
Related Articles Proton NMR spectroscopy shows lipids accumulate in skeletal muscle in response to burn trauma-induced apoptosis.
FASEB J. 2005 Sep;19(11):1431-40
Authors: Astrakas LG, Goljer I, Yasuhara S, Padfield KE, Zhang Q, Gopalan S, Mindrinos MN, Dai G, Yu YM, Martyn JA, Tompkins RG, Rahme LG, Tzika AA
Burn trauma triggers hypermetabolism and muscle wasting via increased cellular protein degradation and apoptosis. Proton...
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[NMR paper] Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alp
Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein.
Related Articles Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein.
J Mol Biol. 2001 Sep 28;312(4):833-47
Authors: Greenfield NJ, Huang YJ, Palm T, Swapna GV, Monleon D, Montelione GT, Hitchcock-DeGregori SE
Tropomyosin is an alpha-helical coiled-coil protein that aligns head-to-tail along the length of the actin filament and...
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11-19-2010 08:44 PM
[NMR paper] Assessment of mitochondrial energy coupling in vivo by 13C/31P NMR.
Assessment of mitochondrial energy coupling in vivo by 13C/31P NMR.
Related Articles Assessment of mitochondrial energy coupling in vivo by 13C/31P NMR.
Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6880-4
Authors: Jucker BM, Dufour S, Ren J, Cao X, Previs SF, Underhill B, Cadman KS, Shulman GI
The recently cloned uncoupling protein homolog UCP3 is expressed primarily in muscle and therefore may play a significant role in the regulation of energy expenditure and body weight. However, investigation into the regulation of uncoupling protein has...
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11-18-2010 09:15 PM
[NMR paper] NMR solution structure of calcium-saturated skeletal muscle troponin C.
NMR solution structure of calcium-saturated skeletal muscle troponin C.
Related Articles NMR solution structure of calcium-saturated skeletal muscle troponin C.
Biochemistry. 1995 Dec 12;34(49):15953-64
Authors: Slupsky CM, Sykes BD
Troponin C (TnC) is an 18 kDa (162-residue) thin-filament calcium-binding protein responsible for triggering muscle contraction upon the release of calcium from the sarcoplasmic reticulum. The structure of TnC with two calcium ions bound has previously been solved by X-ray methods. Shown here is the solution...