Disassembly from both ends of thick filaments in rabbit skeletal muscle fibers. An optical diffraction study
- PMID: 2983791
- PMCID: PMC1435202
- DOI: 10.1016/S0006-3495(85)83915-1
Disassembly from both ends of thick filaments in rabbit skeletal muscle fibers. An optical diffraction study
Abstract
We show in this paper that the change of the internal structure of a sarcomere in a rabbit glycerinated psoas muscle fiber can be examined by analyzing the intensity change of the first- and the second-order optical diffraction lines. A unit-cell (sarcomere)-structure model has been applied to the estimation of the length of thick filaments in a muscle fiber while they undergo dissociation. The optical factors, except for the unit-cell-structure factor, hardly changed during the dissociation of the filaments. Our results show that thick filaments dissociate from both ends on increasing the KCl concentration in the presence of 10 mM pyrophosphate and 5 mM MgCl2. Micromolar concentrations of Ca2+ suppressed to some extent the dissociation of thick filaments. The disassembly of thick filaments occurred at higher KCl concentrations in the absence of pyrophosphate. There was a correlation between the stability of the thick filament structure and cross-bridge formation, which was induced either by the addition of micromolar concentrations of Ca2+ in the presence of Mg-pyrophosphate or by removal of Mg-pyrophosphate.
Similar articles
-
Diffraction rings obtained from a suspension of skeletal myofibrils by laser light illumination. Study of internal structure of sarcomeres.Biophys J. 1989 Dec;56(6):1113-20. doi: 10.1016/S0006-3495(89)82759-6. Biophys J. 1989. PMID: 2692720 Free PMC article.
-
Disassembly kinetics of thick filaments in rabbit skeletal muscle fibers. Effects of ionic strength, Ca2+ concentration, pH, temperature, and cross-bridges on the stability of thick filament structure.Biophys J. 1985 Mar;47(3):267-75. doi: 10.1016/S0006-3495(85)83916-3. Biophys J. 1985. PMID: 2983792 Free PMC article.
-
Accumulated strain mechanism for length determination of thick filaments in skeletal muscle. I. Experimental bases.J Muscle Res Cell Motil. 1986 Dec;7(6):491-500. doi: 10.1007/BF01753565. J Muscle Res Cell Motil. 1986. PMID: 3805256
-
A periodic cytoskeletal lattice in striated muscle.Cell Muscle Motil. 1985;6:287-313. doi: 10.1007/978-1-4757-4723-2_9. Cell Muscle Motil. 1985. PMID: 3888376 Review.
-
Ultrastructure of invertebrate muscle cell types.Histol Histopathol. 1996 Jan;11(1):181-201. Histol Histopathol. 1996. PMID: 8720463 Review.
Cited by
-
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. doi: 10.1016/S0006-3495(85)83767-X. Biophys J. 1985. PMID: 3874654 Free PMC article.
-
Incorporation of nascent myosin heavy chains into thick filaments of cardiac myocytes in thyroid-treated rabbits.J Cell Biol. 1987 Dec;105(6 Pt 1):2771-80. doi: 10.1083/jcb.105.6.2771. J Cell Biol. 1987. PMID: 3320054 Free PMC article.
-
Diffraction rings obtained from a suspension of skeletal myofibrils by laser light illumination. Study of internal structure of sarcomeres.Biophys J. 1989 Dec;56(6):1113-20. doi: 10.1016/S0006-3495(89)82759-6. Biophys J. 1989. PMID: 2692720 Free PMC article.
-
Extraction of Thick Filaments in Individual Sarcomeres Affects Force Production by Single Myofibrils.Biophys J. 2020 Apr 21;118(8):1921-1929. doi: 10.1016/j.bpj.2020.03.007. Epub 2020 Mar 19. Biophys J. 2020. PMID: 32251620 Free PMC article.
-
Elastic filaments in situ in cardiac muscle: deep-etch replica analysis in combination with selective removal of actin and myosin filaments.J Cell Biol. 1993 Feb;120(3):711-24. doi: 10.1083/jcb.120.3.711. J Cell Biol. 1993. PMID: 8425898 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Miscellaneous