Observation and quantitation of lactate in oxidative and glycolytic fibers of skeletal muscles

Magnetic Resonance in Medicine

Volumn 36, Issue 1, 1996, Pages 30-38

  Shen, Dee ^b   Gregory, Carl D ^b   Dawson, M Joan ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

fiber types; lactate; proton NMR; skeletal muscle

Indexed keywords

CHEMICAL BONDS; FIBERS; MAGNETIC SUSCEPTIBILITY; NUCLEAR MAGNETIC RESONANCE; SPECTROSCOPIC ANALYSIS;

BULK MAGNETIC SUSCEPTIBILITIES; CHEMICAL BONDINGS; FIBER TYPES; LACTATE; ORIENTATION DEPENDENCE; PROTON NMR; SKELETAL MUSCLE; SPECTROSCOPIC STUDIES;

MUSCLE;

CARBON 13; LACTIC ACID; MYOGLOBIN;

ANIMAL TISSUE; ARTICLE; FORCE; FROG; MUSCLE CELL; MUSCLE FATIGUE; NONHUMAN; PHANTOM; PROTON NUCLEAR MAGNETIC RESONANCE; RAT; SKELETAL MUSCLE;

EID: 0029886873     PISSN: 07403194     EISSN: None     Source Type: Journal    
DOI: 10.1002/mrm.1910360107     Document Type: Article

References (34)

1. 31P nuclear magnetic resonance. J. Physiol. 258, 82-83 (1976).
2. 1H magnetic resonance spectroscopic studies of skeletal muscle: an analytic reviow. Magn. Reson. Q. 10, 43-63 (1994).
3. R. A. Meyer, T. R. Brown, M. J. Kushmerick. Phosphorus nuclear magnetic resonance of fast- and slow-twitch muscle. Am. J. Physiol. 248, C279-C287 (1985).
4. 31P NMR spectroscopy and the metabolic properties of different muscle fibers. J. Appl. Physiol. 68, 644-649 (1990).
5. M. J. Dawson, D. G. Gadian, D. R. Wilkie, Muscular fatigue investigated by phosphorus nuclear magnetic resonance. Nature 274, 861-886 (1978).
6. G. J. Kemp, D. J. Taylor, P. Styles, G. K. Radda, The production, buffering and efflux of protons in human skeletal muscle during exercise and recovery. NMR Biomed. 6, 73-83 (1993).
7. F. A. Howe, R. J. Maxwell, D. E. Saunders, M. M. Brown, J. R. Griffiths, Proton spectroscopy in vivo. Magn. Reson. Q. 9, 31-59 (1993).
8. P. J. Hore, Solvent suppression in Fourier transform nuclear magnetic resonance. J. Magn. Reson. 55, 283-300 (1983).
9. D. L. Rothman, F. Arias-Mendoza, G. I. Shulman, R. G. Shulman, A pulse sequence for simplifying hydrogen NMR spectra of biological tissues. J. Magn. Reson. 60, 430-436 (1984).
10. V. Sklenar, A. D. Bax, Spin-echo water suppression for the generation of pure-phase two-dimensional NMR spectra. J. Magn. Reson. 74, 469-479 (1987).
11. S. D. Fenster, L. E. Ford, A threaded interpretative language inter-faced to BASIG for laboratory application. Byte 10, 147-148 (1985).
12. M. Bárány, T. Glonek, Phosphorus-31 nuclear magnetic resonance of contractile systems. Methods Enzymol. 85, 624-676 (1982).
13. G. Bodenhausen, R. Freeman, D. L. Turner, Suppression of artifacts in two-dimensional spectroscopy. J. Magn. Reson. 18, 401-405 (1977).
14. A. Kumar, R. V. Hosur, K. Chandrasekhar, A superior pulse scheme for homonuclear two-dimensional correlated spectroscopy. J. Magn. Reson. 66, 143-148 (1984).
15. R. Freeman, T. H. Mareci, G. A. Morris. Weak satellite signals in high-resolution NMR spectra: separating the wheat from the chaff. J. Magn. Reson. 42, 341-445 (1981).
16. S. R. Williams, D. G. Gadian, E. Proctor, A method for lactate detection in vivo by spectral editing without the need for double irradiation. J. Magn. Reson. 66, 562-567 (1986).
17. J. Frahm, K. D. Merboldt, W. Hanicke, Localized proton spectroscopy using stimulated echoes. J. Magn. Reson. 72, 502-508 (1987).
18. 1H NMR chemical shift selective (CHESS) imaging. Phys. Med. Biol. 30, 341-344 (1985).
19. M. J. Dawson, D. Grower, M. K. Kretzschmar, D. R. Wilkie, Heat production and chemical change in frog sartorius; a comparison of R. pipiens with R. temporaria. J. Physiol. 254, 41-42 (1975).
20. D. G. Gadian, G. K. Radda, T. R. Brown, E. M. Chance, M. J. Dawson, D. R. Wilkie, The activity of creatine kinase in frog skeletal muscle studied by saturation-transfer nuclear magnetic resonance. Biochem. J. 194, 215-228 (1981).
21. B. Saltin, P. D. Gollnick, Skeletal muscle adaptability: significance for metabolism and performance, in "Handbook of Physiology: Skeletal Muscle," (L. D. Peachey, Ed.), Sect, 10, pp. 555-831, American Physiology Society, Bethesda, MD, 1983.
22. C. H. Holten, A. Muller, D. Rehbinder, "Lactic Acid: Properties and Chemistry of Lactic Acid and Derivatives," pp. 517-519, Verlag Chemie, GmbH, Weinheim/Bergstrasse, 1971.
23. 1NMR observation of tissue myoglobin: an indicator of cellular oxygenation in vivo. Magn. Reson. Med. 13, 524-528 (1990).
24. D. P. Shoemaker, C. W. Garland, "Experiments in Physical Chemistry," 2nd ed., pp. 30-35, McGraw-Hill, New York, 1967.
25. 1H-NMR spectroscopy for the study of perifused amphibian and excised mammalian muscles. Biochim. Biophys. Acta 886, 411-424 (1986).
26. 1H MR spectroscopy in vivo. Magn. Reson. Med. 10, 210-226 (1989).
27. 1H homonuclear editing sequence to observe laclate in human skeletal muscle after exercise. J. Magn. Reson. 82, 86-96 (1989).
28. S. R. Williams, D. G. Gadian, E. Proctor, D. B. Sprague, D. F. Talbot, I. R. Young, F. F. Brown, Proton NMR studies of muscle metabolites in vivo. J. Magn. Reson. 63, 406-412 (1985).
29. C. S. Springer, Y. Xu, Aspects of bulk magnetic susceptibility in in vivo MRI and MRS, in "New Developments in Contrast Agent Research" (P. A. Rinck, R. N. Muller, Eds.), pp. 13-25, European Magnetic Resonance Forum, Blonay, Switzerland, 1991.
30. A. V. Hill, "Trails & Trials in Physiology," pp. 245-246, Edward Arnold, London, 1965.
31. L. V. Thompson, E. M. Balog, D. A. Riley, R. H. Fitts, Muscle fatigue in frog semitendinosus: alternations in contractile function. Am. J. Physiol. 262, C1500-C1506 (1992).
32. R. W. Tsika, R. E. Herrick, K. M. Baldwin, Subunit composition of rodent isomyosins and their distribution in hindlimb skeletal muscle. J. Appl. Physiol. 63, 2101-2110 (1987).
33. J. B. Wittenberg, Myoglobin-facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle. Physiol. Rev. 50, 559-636 (1970).
34. M. J. Kushmerick, T. S. Moerland, R. W. Wiseman, Mammalian skeletal muscle fibers distinguished by contents of phophocreatine, ATP, and P,. Proc. Natl Acad. Sci. USA 89, 7521-7524 (1992).