Skip to main content
NCBI home page
Biophysical Journal logoLink to Biophysical Journal
. 1983 Jul;43(1):115–119. doi: 10.1016/S0006-3495(83)84329-X

Alterations in the Ca2+ sensitivity of tension development by single skeletal muscle fibers at stretched lengths.

R L Moss, A E Swinford, M L Greaser
PMCID: PMC1329274  PMID: 6882858

Abstract

The apparent length dependence in the calcium sensitivity of tension development in skeletal muscle has been investigated in the present study. At sarcomere lengths of 2.46-2.62 micron, the Hill plot of tension-pCa data is well fit by not one but two straight lines, suggesting the possible involvement of more than a single class of Ca2+-binding site in tension development. On the other hand, increasing the sarcomere length to 3.00-3.25 micron yielded Hill plots that were described by a single straight line, which indicates that at long lengths tension might be regulated by the binding of Ca2+ to a single class of Ca2+-binding sites, presumably the low affinity sites of TnC. This length-dependent transformation of the tension pCa relation occurred at free Mg2+ concentrations of both 0.05 and 3.2 mM. Although the mechanism of this effect is uncertain, plausible explanations for the biphasic Hill plot at the shorter lengths include the possible involvement of Ca2+ activation of the thick filaments and/or myosin LC2 phosphorylation in the process of tension development.

Full text

PDF
115

Images in this article

118FIGURE 6
on p.118

Selected References

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

  1. Bagshaw C. R. Divalent metal ion binding and subunit interactions in myosins: a critical review. J Muscle Res Cell Motil. 1980 Sep;1(3):255–277. doi: 10.1007/BF00711931. [DOI] [PubMed] [Google Scholar]
  2. 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]
  3. Cornish-Bowden A., Koshland D. E., Jr Diagnostic uses of the Hill (Logit and Nernst) plots. J Mol Biol. 1975 Jun 25;95(2):201–212. doi: 10.1016/0022-2836(75)90390-3. [DOI] [PubMed] [Google Scholar]
  4. Donaldson S. K., Kerrick W. G. Characterization of the effects of Mg2+ on Ca2+- and Sr2+-activated tension generation of skinned skeletal muscle fibers. J Gen Physiol. 1975 Oct;66(4):427–444. doi: 10.1085/jgp.66.4.427. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ebashi S., Endo M. Calcium ion and muscle contraction. Prog Biophys Mol Biol. 1968;18:123–183. doi: 10.1016/0079-6107(68)90023-0. [DOI] [PubMed] [Google Scholar]
  6. Endo M. Stretch-induced increase in activation of skinned muscle fibres by calcium. Nat New Biol. 1972 Jun 14;237(76):211–213. doi: 10.1038/newbio237211a0. [DOI] [PubMed] [Google Scholar]
  7. Fuchs F., Fox C. Parallel measurements of bound calcium and force in glycerinated rabbit psoas muscle fibers. Biochim Biophys Acta. 1982 Jan 20;679(1):110–115. doi: 10.1016/0005-2728(82)90261-4. [DOI] [PubMed] [Google Scholar]
  8. Godt R. E., Maughan D. W. Influence of osmotic compression on calcium activation and tension in skinned muscle fibers of the rabbit. Pflugers Arch. 1981 Oct;391(4):334–337. doi: 10.1007/BF00581519. [DOI] [PubMed] [Google Scholar]
  9. Gordon A. M., Huxley A. F., Julian F. J. Tension development in highly stretched vertebrate muscle fibres. J Physiol. 1966 May;184(1):143–169. doi: 10.1113/jphysiol.1966.sp007908. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Haselgrove J. C., Huxley H. E. X-ray evidence for radial cross-bridge movement and for the sliding filament model in actively contracting skeletal muscle. J Mol Biol. 1973 Jul 15;77(4):549–568. doi: 10.1016/0022-2836(73)90222-2. [DOI] [PubMed] [Google Scholar]
  11. Hellam D. C., Podolsky R. J. Force measurements in skinned muscle fibres. J Physiol. 1969 Feb;200(3):807–819. doi: 10.1113/jphysiol.1969.sp008723. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hibberd M. G., Jewell B. R. Calcium- and length-dependent force production in rat ventricular muscle. J Physiol. 1982 Aug;329:527–540. doi: 10.1113/jphysiol.1982.sp014317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hill A. V. The Combinations of Haemoglobin with Oxygen and with Carbon Monoxide. I. Biochem J. 1913 Oct;7(5):471–480. doi: 10.1042/bj0070471. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Huxley A. F. Muscular contraction. J Physiol. 1974 Nov;243(1):1–43. [PMC free article] [PubMed] [Google Scholar]
  15. Huxley H. E., Faruqi A. R., Bordas J., Koch M. H., Milch J. R. The use of synchrotron radiation in time-resolved X-ray diffraction studies of myosin layer-line reflections during muscle contraction. Nature. 1980 Mar 13;284(5752):140–143. doi: 10.1038/284140a0. [DOI] [PubMed] [Google Scholar]
  16. Julian F. J., Moss R. L. Sarcomere length-tension relations of frog skinned muscle fibres at lengths above the optimum. J Physiol. 1980 Jul;304:529–539. doi: 10.1113/jphysiol.1980.sp013341. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Julian F. J., Moss R. L., Waller G. S. Mechanical properties and myosin light chain composition of skinned muscle fibres from adult and new-born rabbits. J Physiol. 1981 Feb;311:201–218. doi: 10.1113/jphysiol.1981.sp013581. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Maughan D. W., Godt R. E. Inhibition of force production in compressed skinned muscle fibers of the frog. Pflugers Arch. 1981 May;390(2):161–163. doi: 10.1007/BF00590200. [DOI] [PubMed] [Google Scholar]
  19. Moisescu D. G., Thieleczek R. Sarcomere length effects on the Sr2+- and Ca2+-activation curves in skinned frog muscle fibres. Biochim Biophys Acta. 1979 Apr 11;546(1):64–76. doi: 10.1016/0005-2728(79)90170-1. [DOI] [PubMed] [Google Scholar]
  20. Morgan M., Perry S. V., Ottaway J. Myosin light-chain phosphatase. Biochem J. 1976 Sep 1;157(3):687–697. doi: 10.1042/bj1570687. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. 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]
  22. PORTZEHL H., CALDWELL P. C., RUEEGG J. C. THE DEPENDENCE OF CONTRACTION AND RELAXATION OF MUSCLE FIBRES FROM THE CRAB MAIA SQUINADO ON THE INTERNAL CONCENTRATION OF FREE CALCIUM IONS. Biochim Biophys Acta. 1964 May 25;79:581–591. doi: 10.1016/0926-6577(64)90224-4. [DOI] [PubMed] [Google Scholar]
  23. Pemrick S. M. Comparison of the calcium sensitivity of actomyosin from native and L-2-deficient myosin. Biochemistry. 1977 Sep 6;16(18):4047–4054. doi: 10.1021/bi00637a017. [DOI] [PubMed] [Google Scholar]
  24. Potter J. D., Gergely J. The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J Biol Chem. 1975 Jun 25;250(12):4628–4633. [PubMed] [Google Scholar]
  25. Robertson S. P., Johnson J. D., Potter J. D. The time-course of Ca2+ exchange with calmodulin, troponin, parvalbumin, and myosin in response to transient increases in Ca2+. Biophys J. 1981 Jun;34(3):559–569. doi: 10.1016/S0006-3495(81)84868-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Stull J. T., High C. W. Phosphorylation of skeletal muscle contractile proteins in vivo. Biochem Biophys Res Commun. 1977 Aug 8;77(3):1078–1083. doi: 10.1016/s0006-291x(77)80088-0. [DOI] [PubMed] [Google Scholar]
  27. Yagi N., Matsubara I. Myosin heads do not move on activation in highly stretched vertebrate striated muscle. Science. 1980 Jan 18;207(4428):307–308. doi: 10.1126/science.6444254. [DOI] [PubMed] [Google Scholar]

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

RESOURCES