Home LiteratureArticle Details
PMID: 2351746 Published · ppublish English Journal Article

Deterioration induced by physiological concentration of calcium ions in skinned muscle fibres.

Journal of muscle research and cell motility ·Vol. 11 ·No. 1 ·1990-02-00 ·Pages 41-7

Kasuga N, Umazume Y

Abstract

The deteriorating effect of microM order of Ca2+ on skinned frog skeletal muscle fibres was studied from the view point of the digestion of proteins by calcium-activated neutral protease (CANP). Tension developed in solutions containing no MgATP (rigor solution) decreased irreversibly with the addition of Ca2+ in quantities of more than 0.1 microM. Low temperature was seen to suppress (Q10 greater than 4), and neutral pH to maximize, this decrease in tension. In rigor solution containing Ca2+, SDS electrophoresis indicated that a 95 k dalton component (alpha-actinin) was released from the fibre; electron micrography showed the disappearance of Z-lines. These results suggest that one of the causes for decrease in rigor tension is the proteolytic activity of CANP, and its inhibitors were shown to be quite useful in experiments on skinned fibre.

MeSH Terms
Animals Antipain/pharmacology Calcium/pharmacology Cysteine Proteinase Inhibitors/pharmacology Dose-Response Relationship, Drug Electrophoresis, Polyacrylamide Gel Hydrogen-Ion Concentration Iodoacetates/pharmacology Iodoacetic Acid Leucine/analogs & derivatives,pharmacology Leupeptins/pharmacology Microscopy, Electron Muscle Contraction/drug effects,physiology Muscles/drug effects,physiopathology,ultrastructure Rana catesbeiana Temperature
Chemicals
Cysteine Proteinase Inhibitors Iodoacetates Leupeptins Antipain Leucine E 64 Calcium Iodoacetic Acid
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kasuga N
Department of Physiology, Jikei University School of Medicine, Tokyo, Japan.
Umazume Y
References (21)
21 references, click to expand
  1. Width and lattice spacing in radially compressed frog skinned muscle fibres at various pH values, magnesium ion concentrations and ionic strengths.
    J Muscle Res Cell Motil. 1986 Jun;7(3):251-8 PMID: 3488330
  2. The effects of a calcium dependent protease on the ultrastructure and contractile mechanics of skinned uterine smooth muscle.
    J Muscle Res Cell Motil. 1985 Jun;6(3):347-63 PMID: 2999192
  3. The use of A23187 to demonstrate the role of intracellular calcium in causing ultrastructural damage in mammalian muscle.
    J Neuropathol Exp Neurol. 1978 Sep;37(5):554-7 PMID: 357685
  4. Localization of the parallel elastic components in frog skinned muscle fibers studied by the dissociation of the A- and I-bands.
    Biophys J. 1985 Jul;48(1):137-47 PMID: 3874654
  5. The protein inhibitor of calcium-dependent proteases: purification from bovine heart and possible mechanisms of regulation.
    Arch Biochem Biophys. 1983 Sep;225(2):779-86 PMID: 6312892
  6. Removal of Z-lines and alpha-actinin from isolated myofibrils by a calcium-activated neutral protease.
    J Biol Chem. 1975 Jun 10;250(11):4278-84 PMID: 805138
  7. Delayed degeneration of dystrophic and normal muscle cell cultures treated with pepstatin, leupeptin, and antipain.
    Exp Neurol. 1976 Mar;50(3):649-57 PMID: 1253868
  8. Sarcomere-associated cytoskeletal lattices in striated muscle. Review and hypothesis.
    Cell Muscle Motil. 1985;6:315-69 PMID: 3888377
  9. Stages in fibre breakdown in Duchenne muscular dystrophy. An electron-microscopic study.
    J Neurol Sci. 1975 Feb;24(2):179-200 PMID: 163299
  10. Canine cardiac calcium-dependent proteases: Resolution of two forms with different requirements for calcium.
    FEBS Lett. 1980 Jan 1;109(1):129-33 PMID: 6766404
  11. Connectin filaments in stretched skinned fibers of frog skeletal muscle.
    J Cell Biol. 1984 Oct;99(4 Pt 1):1391-7 PMID: 6384237
  12. Calcium-induced weakening of skeletal muscle Z-disks.
    J Biochem. 1982 Aug;92(2):381-90 PMID: 6290462
  13. Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization.
    J Biochem. 1978 Jul;84(1):225-30 PMID: 29038
  14. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.
    J Biol Chem. 1969 Aug 25;244(16):4406-12 PMID: 5806584
  15. Re-examination of the apparent binding constant of ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid with calcium around neutral pH.
    J Biochem. 1980 May;87(5):1305-12 PMID: 6771253
  16. Intracellular calcium accumulation in Duchenne dystrophy and other myopathies: a study of 567,000 muscle fibers in 114 biopsies.
    Neurology. 1978 May;28(5):439-46 PMID: 76996
  17. Comparison of calcium-activated neutral proteases from skeletal muscle of rabbit and chicken.
    J Biochem. 1984 Jan;95(1):95-101 PMID: 6323396
  18. Extensibility of the myofilaments in vertebrate skeletal muscle as revealed by stretching rigor muscle fibers.
    J Gen Physiol. 1983 Apr;81(4):531-46 PMID: 6682885
  19. Electron microscopy in the study of muscular dystrophy.
    Ann N Y Acad Sci. 1966 Sep 9;138(1):138-50 PMID: 5339356
  20. Calcium ion and muscle contraction.
    Prog Biophys Mol Biol. 1968;18:123-83 PMID: 4894870
  21. Ca 2+ -specific removal of Z lines from rabbit skeletal muscle.
    J Cell Biol. 1972 Feb;52(2):367-81 PMID: 4621650
Article Info
Journal
Journal of muscle research and cell motility
Abbr.
J Muscle Res Cell Motil
ISSN
0142-4319
Published
1990-02-00
Pages
41-7
Language
English
Region
Netherlands
NLM ID
8006298
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com