|
|
||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
1 Department of Radiology, University of Washington, Seattle, WA, USA
2 Department of Pediatrics, University of Washington, Seattle, WA, USA; Department of Anesthesiology, University of Washington, Seattle, WA, USA; Department of Bioengineering, University of Washington, Seattle, WA, USA
3 Children's Hospital and Regional Medical Center, Seattle, WA, USA
4 Department of Radiology, University of Washington, Seattle, WA, USA; Department of Physiology and Biophysics, University of Washington, Seatle, WA, USA; Department of Bioengineering, University of Washington, Seattle, WA, USA
* To whom correspondence should be addressed. E-mail: dmarc{at}u.washington.edu.
The coupling of mitochondrial ATP synthesis and oxygen consumption (P/O) plays a central role in cellular bioenergetics. Reduced P/O values are associated with mitochondrial pathologies that can lead to reduced capacity for ATP synthesis and tissue degeneration. Previous work has found a wide range of values for the P/O in normal mitochondria. To measure mitochondrial coupling under physiological conditions, we have developed a procedure for determining the P/O of skeletal muscle in vivo. This technique measures ATPase and oxygen consumption rates during ischemia, using 31P magnetic resonance and optical spectroscopies, respectively. This novel approach allows the independent quantitative measurement of ATPase and oxygen flux rates in intact tissue. The quantitative measure of oxygen consumption is made possible by our ability to independently measure the saturations of Hb and Mb from optical spectra. Our results indicate that the in vivo P/O in skeletal muscle of the mouse hindlimb is 2.16 ± 0.24. The theoretical P/O ratio for resting muscle is 2.33. Systemic treatment with 2,4-dinitrophenol to partially uncouple mitochondria does not affect the ATPase rate in the mouse hindlimb, but nearly doubles the rate of oxygen consumption, reducing the in vivo P/O to 1.37 ± 0.22. These results indicate that only a small fraction of the oxygen consumption in resting mouse skeletal muscle is non-phosphorylating under physiological conditions, suggesting that mitochondria are more tightly coupled than previously thought.
This article has been cited by other articles:
![]() |
A. Besserer, G. Becard, A. Jauneau, C. Roux, and N. Sejalon-Delmas GR24, a Synthetic Analog of Strigolactones, Stimulates the Mitosis and Growth of the Arbuscular Mycorrhizal Fungus Gigaspora rosea by Boosting Its Energy Metabolism Plant Physiology, September 1, 2008; 148(1): 402 - 413. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. J. Kemp The interpretation of abnormal 31P magnetic resonance saturation transfer measurements of Pi/ATP exchange in insulin-resistant skeletal muscle Am J Physiol Endocrinol Metab, March 1, 2008; 294(3): E640 - E642. [Full Text] [PDF] |
||||
![]() |
K. E. Conley, C. E. Amara, S. A. Jubrias, and D. J. Marcinek Muscle-energetic and cardio-pulmonary determinants of exercise tolerance in humans: Mitochondrial function, fibre types and ageing: new insights from human muscle in vivo Exp Physiol, March 1, 2007; 92(2): 333 - 339. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. W. Cline Tough love: left out in the cold, but not abandoned, by UCP3 J Appl Physiol, July 1, 2006; 101(1): 12 - 13. [Full Text] [PDF] |
||||
![]() |
G. Kemp, L. F. Ferreira, and T. J. Barstow Kinetics of muscle oxygen use, oxygen content, and blood flow during exercise J Appl Physiol, December 1, 2005; 99(6): 2463 - 2469. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. Bevilacqua, J. J. Ramsey, K. Hagopian, R. Weindruch, and M.-E. Harper Long-term caloric restriction increases UCP3 content but decreases proton leak and reactive oxygen species production in rat skeletal muscle mitochondria Am J Physiol Endocrinol Metab, September 1, 2005; 289(3): E429 - E438. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. E Kan, W. K. J. Renema, D. Isbrandt, and A. Heerschap Phosphorylated guanidinoacetate partly compensates for the lack of phosphocreatine in skeletal muscle of mice lacking guanidinoacetate methyltransferase J. Physiol., October 1, 2004; 560(1): 219 - 229. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| Visit Other APS Journals Online |