Phosphocreatine resynthesis during recovery in different muscles of the exercising leg by31P-MRS

Author(s):  
T. Yoshida ◽  
D. Abe ◽  
Y. Fukuoka
1999 ◽  
Vol 31 (Supplement) ◽  
pp. S264
Author(s):  
D. L. Carl ◽  
N. Alperin ◽  
K. Kochendorfer ◽  
J. Stieger ◽  
F. Andres ◽  
...  

1999 ◽  
Vol 31 (2) ◽  
pp. 236-242 ◽  
Author(s):  
KATLEEN VANDENBERGHE ◽  
PAUL VAN HECKE ◽  
MARC VAN LEEMPUTTE ◽  
FLORENT VANSTAPEL ◽  
PETER HESPEL

1994 ◽  
Vol 17 (8) ◽  
pp. 835-841 ◽  
Author(s):  
Jane A. Kent-Braun ◽  
Khema R. Sharma ◽  
Robert G. Miller ◽  
Michael W. Weiner

2008 ◽  
Vol 40 (Supplement) ◽  
pp. S349 ◽  
Author(s):  
Ronald A. Meyer ◽  
Jill M. Slade ◽  
Theodore F. Towse ◽  
Jennifer L. Olive ◽  
Sean C. Forbes

2016 ◽  
Vol 120 (6) ◽  
pp. 649-656 ◽  
Author(s):  
Alison Sleigh ◽  
David B. Savage ◽  
Guy B. Williams ◽  
David Porter ◽  
T. Adrian Carpenter ◽  
...  

Fundamental criticisms have been made over the use of 31P magnetic resonance spectroscopy (MRS) magnetization transfer estimates of inorganic phosphate (Pi)→ATP flux (VPi-ATP) in human resting skeletal muscle for assessing mitochondrial function. Although the discrepancy in the magnitude of VPi-ATP is now acknowledged, little is known about its metabolic determinants. Here we use a novel protocol to measure VPi-ATP in human exercising muscle for the first time. Steady-state VPi-ATP was measured at rest and over a range of exercise intensities and compared with suprabasal oxidative ATP synthesis rates estimated from the initial rates of postexercise phosphocreatine resynthesis (VATP). We define a surplus Pi→ATP flux as the difference between VPi-ATP and VATP. The coupled reactions catalyzed by the glycolytic enzymes GAPDH and phosphoglycerate kinase (PGK) have been shown to catalyze measurable exchange between ATP and Pi in some systems and have been suggested to be responsible for this surplus flux. Surplus VPi-ATP did not change between rest and exercise, even though the concentrations of Pi and ADP, which are substrates for GAPDH and PGK, respectively, increased as expected. However, involvement of these enzymes is suggested by correlations between absolute and surplus Pi→ATP flux, both at rest and during exercise, and the intensity of the phosphomonoester peak in the 31P NMR spectrum. This peak includes contributions from sugar phosphates in the glycolytic pathway, and changes in its intensity may indicate changes in downstream glycolytic intermediates, including 3-phosphoglycerate, which has been shown to influence the exchange between ATP and Pi catalyzed by GAPDH and PGK.


2002 ◽  
Vol 1553 (3) ◽  
pp. 223-231 ◽  
Author(s):  
Benoit Giannesini ◽  
Marguerite Izquierdo ◽  
Patrick J Cozzone ◽  
David Bendahan

1997 ◽  
Vol 82 (1) ◽  
pp. 329-335 ◽  
Author(s):  
Alan M. Nevill ◽  
David A. Jones ◽  
David McIntyre ◽  
Gregory C. Bogdanis ◽  
Mary E. Nevill

Nevill, Alan M., David A. Jones, David McIntyre, Gregory C. Bogdanis, and Mary E. Nevill. A model for phosphocreatine resynthesis. J. Appl. Physiol. 82(1): 329–335, 1997.—A model for phosphocreatine (PCr) resynthesis is proposed based on a simple electric circuit, where the PCr store in muscle is likened to the stored charge on the capacitor. The solution to the second-order differential equation that describes the potential around the circuit suggests the model for PCr resynthesis is given by PCr( t) = R − [ d 1 ⋅ exp(− k 1 ⋅ t) ± d 2 ⋅ exp(− k 2 ⋅ t)], where R is PCr concentration at rest, d 1, d 2, k 1, and k 2 are constants, and t is time. By using nonlinear least squares regression, this double-exponential model was shown to fit the PCr recovery data taken from two studies involving maximal exercise accurately. In study 1, when the muscle was electrically stimulated while occluded, PCr concentrations rose during the recovery phase to a level above that observed at rest. In study 2, after intensive dynamic exercise, PCr recovered monotonically to resting concentrations. The second exponential term in the double-exponential model was found to make a significant additional contribution to the quality of fit in both study 1( P < 0.05) and study 2( P < 0.01).


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