Literature DB >> 318072

Stretch and radial compression studies on relaxed skinned muscle fibers of the frog.

D W Maughan, R E Godt.   

Abstract

The influence of stretch and radial compression on the width of mechanically skinned fibers from the semitendinosus muscle of the frog (R. pipiens) was examined in relaxing solutions with high-power light microscopy. Fibers were skinned under mineral oil. We find that, after correcting for water uptake in the oil, fiber width increased by an average of 28% upon transfer from oil to relaxing medium, with some tendency for greater swelling at longer sarcomere lengths. Subsequently, fibers were compressed by addition of the long-chain polymer polyvinylpyrrolidone (PVP-40, number average molecular weight 40,000) to relaxing solutions. Sarcomere length does not appear to be affected by addition of PVP. At any PVP concentration, the inverse square of the fiber width increased smoothly and linearly with increasing stretch for sarcomere lengths between 2.10 and 4.60 micrometer. At any fixed sarcomere length, fiber width decreased linearly with the logarithm of the osmotic compressive pressure exerted by PVP (2-10% concentration). From this logarithmic relation we estimate that the swelling pressure of the intact fiber is 3.40 x 10(3) N/m2, between that of a 2 and a 3% PVP solution. The pressure giving rise to fiber swelling is not due to dilation of the sarcoplasmic reticulum (SR), since the experimental results above were not significantly different after treatment with 0.5% BRIJ-58, a nonionic detergent that disrupts the SR. Swelling may be due simply to elastic structures within the fiber that are constrained in the intact cell. Values of bulk moduli of fibers, calculated from the compression experiments, and preliminary measurements of Young's modulus from stretch experiments, are quantitatively consistent with the idea that skinned fibers behave as nonisotropic elastic bodies.

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Year:  1979        PMID: 318072      PMCID: PMC1328645          DOI: 10.1016/S0006-3495(79)85188-7

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


  15 in total

1.  Connectin, an elastic protein of muscle. Characterization and Function.

Authors:  K Maruyama; S Matsubara; R Natori; Y Nonomura; S Kimura
Journal:  J Biochem       Date:  1977-08       Impact factor: 3.387

2.  Measurement and modification of forces between lecithin bilayers.

Authors:  D M LeNeveu; R P Rand
Journal:  Biophys J       Date:  1977-05       Impact factor: 4.033

3.  The myofilament lattice: studies on isolated fibers. IV. Lattice equilibria in striated muscle.

Authors:  E W April
Journal:  J Mechanochem Cell Motil       Date:  1975

4.  X-ray diffraction studies on skinned single fibres of frog skeletal muscle.

Authors:  I Matsubara; G F Elliott
Journal:  J Mol Biol       Date:  1972-12-30       Impact factor: 5.469

5.  Three-dimensional structure of the vertebrate muscle M-region.

Authors:  P Luther; J Squire
Journal:  J Mol Biol       Date:  1978-11-05       Impact factor: 5.469

6.  Swelling of skinned muscle fibers of the frog. Experimental observations.

Authors:  R E Godt; D W Maughan
Journal:  Biophys J       Date:  1977-08       Impact factor: 4.033

7.  Connectin, an elastic protein of muscle. Comparative Biochemistry.

Authors:  K Maruyama; F Murakami; K Ohashi
Journal:  J Biochem       Date:  1977-08       Impact factor: 3.387

8.  Intracellular calcium movements in skinned muscle fibres.

Authors:  L E Ford; R J Podolsky
Journal:  J Physiol       Date:  1972-05       Impact factor: 5.182

9.  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

10.  Calcium-activated tension of skinned muscle fibers of the frog. Dependence on magnesium adenosine triphosphate concentration.

Authors:  R E Godt
Journal:  J Gen Physiol       Date:  1974-06       Impact factor: 4.086

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  37 in total

1.  Parvalbumin concentration and diffusion coefficient in frog myoplasm.

Authors:  D W Maughan; R E Godt
Journal:  J Muscle Res Cell Motil       Date:  1999-02       Impact factor: 2.698

2.  Tetragonal deformation of the hexagonal myofilament matrix in single skinned skeletal muscle fibres owing to change in sarcomere length.

Authors:  P Schiereck; E L de Beer; R L Grundeman; T Manussen; N Kylstra; W Bras
Journal:  J Muscle Res Cell Motil       Date:  1992-10       Impact factor: 2.698

3.  Diffraction ellipsometry studies of osmotically compressed muscle fibers.

Authors:  W L Kerr; R J Baskin; Y Yeh
Journal:  Pflugers Arch       Date:  1990-08       Impact factor: 3.657

4.  Nonuniform volume changes during muscle contraction.

Authors:  I R Neering; L A Quesenberry; V A Morris; S R Taylor
Journal:  Biophys J       Date:  1991-04       Impact factor: 4.033

5.  Radial stability of the actomyosin filament lattice in isolated skeletal myofibrils studied using atomic force microscopy.

Authors:  Daisuke Miyashiro; Jun'ichi Wakayama; Nao Akiyama; Yuki Kunioka; Takenori Yamada
Journal:  J Physiol Sci       Date:  2013-05-21       Impact factor: 2.781

6.  The force bearing capacity of frog muscle fibres during stretch: its relation to sarcomere length and fibre width.

Authors:  K A Edman
Journal:  J Physiol       Date:  1999-09-01       Impact factor: 5.182

7.  An electrostatic model with weak actin-myosin attachment resolves problems with the lattice stability of skeletal muscle.

Authors:  D A Smith; D G Stephenson
Journal:  Biophys J       Date:  2011-06-08       Impact factor: 4.033

8.  Force response to rapid and slow small amplitude length releases in isometrically contracting normal width and radially compressed trabeculae from rat heart.

Authors:  M R Berman
Journal:  Pflugers Arch       Date:  1985-02       Impact factor: 3.657

9.  A quantitative analysis of elastic, entropic, electrostatic, and osmotic forces within relaxed skinned muscle fibers.

Authors:  D W Maughan; R E Godt
Journal:  Biophys Struct Mech       Date:  1980

10.  Actomyosin energy turnover declines while force remains constant during isometric muscle contraction.

Authors:  Timothy G West; N A Curtin; Michael A Ferenczi; Zhen-He He; Yin-Biao Sun; Malcolm Irving; Roger C Woledge
Journal:  J Physiol       Date:  2003-10-17       Impact factor: 5.182

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