Standard magnetic resonance-based measurements of the Pi→ATP rate do not index the rate of oxidative phosphorylation in cardiac and skeletal muscles

被引:41
作者
From, Arthur H. L. [1 ,2 ]
Ugurbil, Kamil [1 ,2 ,3 ]
机构
[1] Univ Minnesota, Ctr Magnet Resonance Res, Sch Med, Minneapolis, MN 55455 USA
[2] Univ Minnesota, Dept Med, Sch Med, Div Cardiovasc, Minneapolis, MN 55455 USA
[3] Univ Minnesota, Sch Med, Dept Radiol, Minneapolis, MN 55455 USA
来源
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY | 2011年 / 301卷 / 01期
基金
美国国家卫生研究院;
关键词
magnetization transfer; oxidative ATP synthesis; striated muscle; SATURATION-TRANSFER MEASUREMENTS; P-31 NMR MEASUREMENT; ATP SYNTHESIS; IN-VIVO; INSULIN-RESISTANCE; SUBSTRATE OXIDATION; INTACT MYOCARDIUM; C-13/P-31; NMR; BLOOD-FLOW; P-I;
D O I
10.1152/ajpcell.00345.2010
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
From AH, Ugurbil K. Standard magnetic resonance-based measurements of the P-i -> ATP rate do not index the rate of oxidative phosphorylation in cardiac and skeletal muscles. Am J Physiol Cell Physiol 301: C1-C11, 2011. First published March 2, 2011; doi:10.1152/ajpcell.00345.2010.-Magnetic resonance spectroscopy-based magnetization transfer techniques (MT) are commonly used to assess the rate of oxidative (i.e., mitochondrial) ATP synthesis in intact tissues. Physiologically appropriate interpretation of MT rate data depends on accurate appraisal of the biochemical events that contribute to a specific MT rate measurement. The relative contributions of the specific enzymatic reactions that can contribute to a MT P-i -> ATP rate measurement are tissue dependent; nonrecognition of this fact can bias the interpretation of MT P-i -> ATP rate data. The complexities of MT-based measurements of mitochondrial ATP synthesis rates made in striated muscle and other tissues are reviewed, following which, the adverse impacts of erroneous P-i -> ATP rate data analyses on the physiological inferences presented in selected published studies of cardiac and skeletal muscle are considered.
引用
收藏
页码:C1 / C11
页数:11
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