Skip to main content
PMC home page
Biophysical Journal logoLink to Biophysical Journal
. 1988 Dec;54(6):1169–1173. doi: 10.1016/S0006-3495(88)83052-2

Depression of Ca2+ insensitive tension due to reduced pH in partially troponin-extracted skinned skeletal muscle fibers.

J M Metzger 1, R L Moss 1
PMCID: PMC1330427  PMID: 3233271

Abstract

Previous studies on skinned muscle fibers have demonstrated a direct effect of elevated levels of H+ ion to depress force production; however, the molecular basis for this effect is presently unknown. Here, whole troponin complexes were removed from skinned single fiber preparations of rat slow-twitch and fast-twitch muscles, and the effect of H+ ions on the resultant Ca2+-insensitive force was examined. The effect of H+ ions to depress force was found to be virtually identical in untreated control fibers activated in the presence of Ca2+ and in fibers activated in the absence of Ca2+ by troponin removal. Thus, the effect of H+ ions to depress force occurs at a step in activation beyond the disinhibition of the thin filament by Ca2+, probably involving reductions in the number of attached cross-bridges or in the force per attachment.

Full text

PDF

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Allen J. D., Moss R. L. Factors influencing the ascending limb of the sarcomere length-tension relationship in rabbit skinned muscle fibres. J Physiol. 1987 Sep;390:119–136. doi: 10.1113/jphysiol.1987.sp016689. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Baldwin K. M., Klinkerfuss G. H., Terjung R. L., Molé P. A., Holloszy J. O. Respiratory capacity of white, red, and intermediate muscle: adaptative response to exercise. Am J Physiol. 1972 Feb;222(2):373–378. doi: 10.1152/ajplegacy.1972.222.2.373. [DOI] [PubMed] [Google Scholar]
  3. Blanchard E. M., Pan B. S., Solaro R. J. The effect of acidic pH on the ATPase activity and troponin Ca2+ binding of rabbit skeletal myofilaments. J Biol Chem. 1984 Mar 10;259(5):3181–3186. [PubMed] [Google Scholar]
  4. Bremel R. D., Weber A. Cooperation within actin filament in vertebrate skeletal muscle. Nat New Biol. 1972 Jul 26;238(82):97–101. doi: 10.1038/newbio238097a0. [DOI] [PubMed] [Google Scholar]
  5. Dawson M. J., Gadian D. G., Wilkie D. R. Muscular fatigue investigated by phosphorus nuclear magnetic resonance. Nature. 1978 Aug 31;274(5674):861–866. doi: 10.1038/274861a0. [DOI] [PubMed] [Google Scholar]
  6. Donaldson S. K. Ca2+-activated force-generating properties of mammalian skeletal muscle fibres: histochemically identified single peeled rabbit fibres. J Muscle Res Cell Motil. 1984 Dec;5(6):593–612. doi: 10.1007/BF00713922. [DOI] [PubMed] [Google Scholar]
  7. Donaldson S. K., Hermansen L., Bolles L. Differential, direct effects of H+ on Ca2+ -activated force of skinned fibers from the soleus, cardiac and adductor magnus muscles of rabbits. Pflugers Arch. 1978 Aug 25;376(1):55–65. doi: 10.1007/BF00585248. [DOI] [PubMed] [Google Scholar]
  8. Edman K. A., Mattiazzi A. R. Effects of fatigue and altered pH on isometric force and velocity of shortening at zero load in frog muscle fibres. J Muscle Res Cell Motil. 1981 Sep;2(3):321–334. doi: 10.1007/BF00713270. [DOI] [PubMed] [Google Scholar]
  9. Fabiato A., Fabiato F. Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J Physiol (Paris) 1979;75(5):463–505. [PubMed] [Google Scholar]
  10. Fabiato A., Fabiato F. Effects of pH on the myofilaments and the sarcoplasmic reticulum of skinned cells from cardiace and skeletal muscles. J Physiol. 1978 Mar;276:233–255. doi: 10.1113/jphysiol.1978.sp012231. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Fitts R. H., Courtright J. B., Kim D. H., Witzmann F. A. Muscle fatigue with prolonged exercise: contractile and biochemical alterations. Am J Physiol. 1982 Jan;242(1):C65–C73. doi: 10.1152/ajpcell.1982.242.1.C65. [DOI] [PubMed] [Google Scholar]
  12. Giulian G. G., Moss R. L., Greaser M. Improved methodology for analysis and quantitation of proteins on one-dimensional silver-stained slab gels. Anal Biochem. 1983 Mar;129(2):277–287. doi: 10.1016/0003-2697(83)90551-1. [DOI] [PubMed] [Google Scholar]
  13. Godt R. E. A simple electrostatic model can explain the effect of pH upon the force-pCa relation of skinned frog skeletal muscle fibers. Biophys J. 1981 Aug;35(2):385–392. doi: 10.1016/S0006-3495(81)84797-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Godt R. E., Lindley B. D. Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog. J Gen Physiol. 1982 Aug;80(2):279–297. doi: 10.1085/jgp.80.2.279. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Gordon A. M., Ridgway E. B. Extra calcium on shortening in barnacle muscle. Is the decrease in calcium binding related to decreased cross-bridge attachment, force, or length? J Gen Physiol. 1987 Sep;90(3):321–340. doi: 10.1085/jgp.90.3.321. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Güth K., Potter J. D. Effect of rigor and cycling cross-bridges on the structure of troponin C and on the Ca2+ affinity of the Ca2+-specific regulatory sites in skinned rabbit psoas fibers. J Biol Chem. 1987 Oct 5;262(28):13627–13635. [PubMed] [Google Scholar]
  17. Hermansen L., Osnes J. B. Blood and muscle pH after maximal exercise in man. J Appl Physiol. 1972 Mar;32(3):304–308. doi: 10.1152/jappl.1972.32.3.304. [DOI] [PubMed] [Google Scholar]
  18. Mainwood G. W., Renaud J. M. The effect of acid-base balance on fatigue of skeletal muscle. Can J Physiol Pharmacol. 1985 May;63(5):403–416. doi: 10.1139/y85-072. [DOI] [PubMed] [Google Scholar]
  19. Metzger J. M., Fitts R. H. Fatigue from high- and low-frequency muscle stimulation: contractile and biochemical alterations. J Appl Physiol (1985) 1987 May;62(5):2075–2082. doi: 10.1152/jappl.1987.62.5.2075. [DOI] [PubMed] [Google Scholar]
  20. Metzger J. M., Fitts R. H. Role of intracellular pH in muscle fatigue. J Appl Physiol (1985) 1987 Apr;62(4):1392–1397. doi: 10.1152/jappl.1987.62.4.1392. [DOI] [PubMed] [Google Scholar]
  21. Metzger J. M., Moss R. L. Greater hydrogen ion-induced depression of tension and velocity in skinned single fibres of rat fast than slow muscles. J Physiol. 1987 Dec;393:727–742. doi: 10.1113/jphysiol.1987.sp016850. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Moss R. L., Allen J. D., Greaser M. L. Effects of partial extraction of troponin complex upon the tension-pCa relation in rabbit skeletal muscle. Further evidence that tension development involves cooperative effects within the thin filament. J Gen Physiol. 1986 May;87(5):761–774. doi: 10.1085/jgp.87.5.761. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Moss R. L. Effects on shortening velocity of rabbit skeletal muscle due to variations in the level of thin-filament activation. J Physiol. 1986 Aug;377:487–505. doi: 10.1113/jphysiol.1986.sp016199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Moss R. L., Giulian G. G., Greaser M. L. The effects of partial extraction of TnC upon the tension-pCa relationship in rabbit skinned skeletal muscle fibers. J Gen Physiol. 1985 Oct;86(4):585–600. doi: 10.1085/jgp.86.4.585. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Moss R. L. Sarcomere length-tension relations of frog skinned muscle fibres during calcium activation at short lengths. J Physiol. 1979 Jul;292:177–192. doi: 10.1113/jphysiol.1979.sp012845. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Robertson S. P., Kerrick W. G. The effects of pH on Ca2+-activated force in frog skeletal muscle fibers. Pflugers Arch. 1979 May 15;380(1):41–45. doi: 10.1007/BF00582610. [DOI] [PubMed] [Google Scholar]
  27. Sahlin K., Edström L., Sjöholm H. Fatigue and phosphocreatine depletion during carbon dioxide-induced acidosis in rat muscle. Am J Physiol. 1983 Jul;245(1):C15–C20. doi: 10.1152/ajpcell.1983.245.1.C15. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES