Literature DB >> 3874654

Localization of the parallel elastic components in frog skinned muscle fibers studied by the dissociation of the A- and I-bands.

H Higuchi, Y Umazume.   

Abstract

Localization of the parallel elastic components (PECs) in skinned muscle fibers was investigated by analyzing the change of the resting tension, which accompanies the dissociation of the A- and I-bands. The A-band was dissociated from both ends by increasing the concentration of KCl under relaxing conditions (0.09-0.54 M KCl, 4.0 mM MgATP, 1.0 mM Mg2+, 4.0 mM EGTA, pH 6.0-9.0, 20 degrees C). At sarcomere lengths greater than or equal to 3.5 microns, the length of the A-band was estimated by comparing the intensity of the first-order optical diffraction line with the results of model calculations. These results were supported by differential-interference microscopy and sodium dodecyl sulfate gel electrophoresis. It was shown that the resting tension decreased nearly in proportion to the residual length of the A-band. At sarcomere lengths less than or equal to 4.0 microns, the resting tension after the dissociation of the A-band was lowered to less than 10% of the initial value. On the other hand, at sarcomere lengths greater than or equal to 5.0 microns the resting tension after the dissociation of the A-band still showed approximately 35% of the initial value and did not change even after the I-band was dissociated by a solution containing KI. From these results, we propose that most of the PECs contributing to resting tension bind almost uniformly to the A-band and there are also PECs connecting Z-lines.

Entities:  

Mesh:

Substances:

Year:  1985        PMID: 3874654      PMCID: PMC1356636          DOI: 10.1016/S0006-3495(85)83767-X

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  22 in total

1.  Sarcomere length dispersion in single skeletal muscle fibers and fiber bundles.

Authors:  P J Paolini; R Sabbadini; K P Roos; R J Baskin
Journal:  Biophys J       Date:  1976-08       Impact factor: 4.033

2.  Electro-optical property of extremely stretched skinned muscle fibers.

Authors:  Y Umazume; S Fujime
Journal:  Biophys J       Date:  1975-02       Impact factor: 4.033

3.  Optical diffraction study of muscle fibers.

Authors:  S Fujime
Journal:  Biochim Biophys Acta       Date:  1975-01-30

4.  New elastic protein from muscle.

Authors:  K Maruyama; R Natori; Y Nonomura
Journal:  Nature       Date:  1976-07-01       Impact factor: 49.962

5.  The effects of pH on Ca2+-activated force in frog skeletal muscle fibers.

Authors:  S P Robertson; W G Kerrick
Journal:  Pflugers Arch       Date:  1979-05-15       Impact factor: 3.657

6.  Optical diffraction study of muscle fibers. II. Electro-optical properties of muscle fibers.

Authors:  S Yoshino; Y Umazume; R Natori; S Fujime; S Chiba
Journal:  Biophys Chem       Date:  1978-09       Impact factor: 2.352

7.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

8.  Titin: major myofibrillar components of striated muscle.

Authors:  K Wang; J McClure; A Tu
Journal:  Proc Natl Acad Sci U S A       Date:  1979-08       Impact factor: 11.205

9.  Ionic strength and the contraction kinetics of skinned muscle fibers.

Authors:  M D Thames; L E Teichholz; R J Podolsky
Journal:  J Gen Physiol       Date:  1974-04       Impact factor: 4.086

10.  Tension in skinned frog muscle fibers in solutions of varying ionic strength and neutral salt composition.

Authors:  A M Gordon; R E Godt; S K Donaldson; C E Harris
Journal:  J Gen Physiol       Date:  1973-11       Impact factor: 4.086

View more
  15 in total

1.  Regulation of skeletal muscle stiffness and elasticity by titin isoforms: a test of the segmental extension model of resting tension.

Authors:  K Wang; R McCarter; J Wright; J Beverly; R Ramirez-Mitchell
Journal:  Proc Natl Acad Sci U S A       Date:  1991-08-15       Impact factor: 11.205

2.  Passive force enhancement in single myofibrils.

Authors:  V Joumaa; D E Rassier; T R Leonard; W Herzog
Journal:  Pflugers Arch       Date:  2007-06-06       Impact factor: 3.657

3.  The organization of titin (connectin) and nebulin in the sarcomeres: an immunocytolocalization study.

Authors:  S Pierobon-Bormioli; R Betto; G Salviati
Journal:  J Muscle Res Cell Motil       Date:  1989-12       Impact factor: 2.698

4.  Lattice shrinkage with increasing resting tension in stretched, single skinned fibers of frog muscle.

Authors:  H Higuchi; Y Umazume
Journal:  Biophys J       Date:  1986-09       Impact factor: 4.033

5.  Positioning of actin filaments and tension generation in skinned muscle fibres released after stretch beyond overlap of the actin and myosin filaments.

Authors:  H Higuchi; T Yoshioka; K Maruyama
Journal:  J Muscle Res Cell Motil       Date:  1988-12       Impact factor: 2.698

6.  Accumulated strain mechanism for length determination of thick filaments in skeletal muscle. I. Experimental bases.

Authors:  H Higuchi; T Funatsu; A Ishijima; N Okamura; S Ishiwata
Journal:  J Muscle Res Cell Motil       Date:  1986-12       Impact factor: 2.698

7.  Lattice swelling with the selective digestion of elastic components in single-skinned fibers of frog muscle.

Authors:  H Higuchi
Journal:  Biophys J       Date:  1987-07       Impact factor: 4.033

8.  Characterization of beta-connectin (titin 2) from striated muscle by dynamic light scattering.

Authors:  H Higuchi; Y Nakauchi; K Maruyama; S Fujime
Journal:  Biophys J       Date:  1993-11       Impact factor: 4.033

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

Authors:  N Kasuga; Y Umazume
Journal:  J Muscle Res Cell Motil       Date:  1990-02       Impact factor: 2.698

10.  Localization and elasticity of connectin (titin) filaments in skinned frog muscle fibres subjected to partial depolymerization of thick filaments.

Authors:  H Higuchi; T Suzuki; S Kimura; T Yoshioka; K Maruyama; Y Umazume
Journal:  J Muscle Res Cell Motil       Date:  1992-06       Impact factor: 2.698

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.