Energy changes and muscular contraction.

Curtin, N. A.; Woledge, Roger C.

doi:10.1152/physrev.1978.58.3.690

Cited by 177 publications

(130 citation statements)

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“…The effects of the breakdown of creatine phosphate to creatine and the effluxes of H+ ion of lactate to extracellular space must be taken into consideration but they remain to be elucidated. However, the estimated value agreed in general with the values of 23-27 mEq/(pH • kg muscle) which were calculated from the reports of CURTIN and WOLEDGE (1978), indicating that these effects would be negligible, as assumed by DAwsoN et al (1978DAwsoN et al ( , 1980 for their analysis of metabolic aspects of muscular fatigue.…”

Section: Discussionsupporting

confidence: 79%

A 1H-nuclear magnetic resonance study on lactate and intracellular pH in frog muscle.

1983

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High resolution proton magnetic resonance spectra of intact frog muscle, obtained by the selective saturation of water signal with 15 min accumulation, showed well-resolved signals from lactate, carnosine, and other compounds. This technique was used to monitor the changes in lactate content and in intracellular pH which was estimated from the chemical shift of carnosine in muscle. The intracellular pH was estimated to be 7.1 in fresh muscles. Under an anaerobic condition, resting muscle showed a gradual increase in lactate content with intracellular acidification. When the anaerobic muscle was electrically stimulated for 5 sec, a transient acceleration of the lactate production and the intracellular acidification was observed. The intracellular buffer value was estimated to be 27 mEq/(pH kg muscle), based on the pH change due to the increase in lactate content.

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Section: Discussionsupporting

confidence: 79%

A 1H-nuclear magnetic resonance study on lactate and intracellular pH in frog muscle.

1983

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“…The third possible mechanism is the involvement of myosin ATPase and actomyosin ATPase reactions. This type of mechanism has been proposed (WoLEDGE, 1977;CURTIN and WoLEDGE, 1978) to explain the course of the energy balance discrepancy and has been used by KODAMA and YAMADA (1979) to explain the energy balance discrepancy during active shortening of muscle. It is most likely that the distribution of myosin and actomyosin intermediates during maintained contraction is very different from that before contraction, and that it takes a long time for these intermediate species to become redistributed to their pre-contractile level after the muscle has relaxed.…”

Section: Discussionmentioning

confidence: 99%

“…These changes recover after relaxation, if oxygenation is adequate. This has been revealed by chemical analysis (LUNDSGAARD, 1934;CARLSON and SIGER, 1960;MOMMAERTS, 1969;CURTIN and WOLEDGE, 1978;HOMSHER and KEAN, 1978) and by phosphorus nuclear magnetic resonance (31P NMR) of living muscle (DAWSON et al, 1977). Improved time-resolution of 31P NMR has allowed us to follow the course of changes of the levels of PCr and P; associated with contraction of living muscles in more detail and without the confusing intervention of semi-specific metabolic inhibitors such as iodoacetate (IAA) or fluorodinitrobenzene (FDNB).…”

mentioning

confidence: 99%

Post-contractile phosphocreatine splitting in muscle as revealed by time-resolved 31P nuclear magnetic resonance.

Yamada

Tanokura

1983

Jpn.J.Physiol

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We have designed and constructed a 25 mm diameter chamber in order to study the phosphorus nuclear magnetic resonance (31P NMR) spectra from a considerable mass of toad and frog muscles (16 sartorii weighing 5-10 g) which were maintained in a well-oxygenated condition at 4°C. We have thus been able to measure the biochemical changes that accompany contraction and recovery with improved time-resolution. Using this apparatus it is shown that splitting of phosphocreatine (PCr) continues for a few minutes after relaxation. Subsequently the PCr is rebuilt by oxidative processes in the familiar way, with a timeconstant~ 10 min. By studying tetanic contractions of various durations we have shown that the time-course of the post-contractile PCr splitting is similar to that of the heat production that cannot yet be accounted for by known chemical changes. Myosin and actomyosin ATPase reactions most likely underlie the post-contractile ATP utilization. The results suggest that the post-contractile ATP utilization is responsible for the unexplained enthalpy mentioned above.Key Words: muscle, phosphocreatine, nuclear magnetic resonance.When muscle contracts, phosphocreatine (PCr) is split, and inorganic phosphate (Pi) is released. These changes recover after relaxation, if oxygenation is adequate. This has been revealed by chemical analysis (LUNDSGAARD, 1934;CARLSON and SIGER, 1960;MOMMAERTS, 1969;CURTIN and WOLEDGE, 1978;HOMSHER and KEAN, 1978) and by phosphorus nuclear magnetic resonance (31P NMR) of living muscle (DAWSON et al., 1977). Improved time-resolution of 31P NMR has allowed us to follow the course of changes of the levels of PCr and P; associated with contraction of living muscles in more detail and without the confusing intervention of semi-specific metabolic inhibitors such as iodoacetate (IAA) or fluorodinitrobenzene (FDNB). We show here that the level of PCr continues to decrease considerably for 2 to 3 min after the muscle has relaxed from a brief tetanus and then starts to increase, whereas the level of Pi attains its maximum at

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“…The enthalpy changes associated with Ca2+ binding to (or Mg2+-Ca2+ exchange on) parvalbumins have been measured only for &par-valbumins other than bullfrog PA1 @type) and PA2 (a-type); (i) carp ~14.25 [34], (ii) whiting pI 4.4 [37], and (iii) frog pI 4.75 (I?. temporaria) [38].…”

Section: Febs Letters December 1986mentioning

confidence: 99%

“…In the early stage of contraction, muscles are known to produce 'labile' maintenance heat, which could be related to the heat produced by Mg'+-Ca2+ exchange on parvalbumin [36,37]. The value of the enthalpy change associated with Mg2+-Ca2+ exchange on the 'ideal' amphibian parvalbumin proposed here is just the same as that used to estimate the amount of heat (-AH) expected for Mg2+-Ca2+ exchange of parvalbumins in intact frog skeletal muscles in a previous paper [14].…”

Section: Febs Letters December 1986mentioning

confidence: 99%

A calorimetric study of Ca²⁺ binding by the parvalbumin of the toad (Bufo): distinguishable binding sites in the molecule

1986

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Microcalorimetric titrations of the major isotype of parvalbumin (tPA) from toad (Bufo) skeletal muscle, with Ca*+ in the presence and absence of Mg+ and with M$+ in the absence of Ca2+, have been carried out at 25°C and pH 7.0. The results indicate that the two binding sites in each molecule are distinguishable from each other for both Ca2+ binding and Mg 2+ binding. Such a characteristic is distinctly different from those of other parvalbumins. The enthalpy changes determined are distinctly different from those of bullfrog parvalbumins on Ca2+ or Mg2+ binding, but are similar to those on Mg 2+-Ca2+ exchange. The results indicate that the reaction of Mg2+-Ca*+ exchange is driven almost entirely by the large favorable enthalpy change.

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Energy changes and muscular contraction.

Cited by 177 publications

References 0 publications

A 1H-nuclear magnetic resonance study on lactate and intracellular pH in frog muscle.

A 1H-nuclear magnetic resonance study on lactate and intracellular pH in frog muscle.

Post-contractile phosphocreatine splitting in muscle as revealed by time-resolved 31P nuclear magnetic resonance.

A calorimetric study of Ca²⁺ binding by the parvalbumin of the toad (Bufo): distinguishable binding sites in the molecule

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Energy changes and muscular contraction.

Cited by 177 publications

References 0 publications

A 1H-nuclear magnetic resonance study on lactate and intracellular pH in frog muscle.

A 1H-nuclear magnetic resonance study on lactate and intracellular pH in frog muscle.

Post-contractile phosphocreatine splitting in muscle as revealed by time-resolved 31P nuclear magnetic resonance.

A calorimetric study of Ca2+ binding by the parvalbumin of the toad (Bufo): distinguishable binding sites in the molecule

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A calorimetric study of Ca²⁺ binding by the parvalbumin of the toad (Bufo): distinguishable binding sites in the molecule