Literature DB >> 6201824

The relationship between ATP hydrolysis and active force in compressed and swollen skinned muscle fibers of the rabbit.

B Krasner, D Maughan.   

Abstract

We investigated whether the inhibition of force generation observed in compressed muscle fibers is accompanied by a coupled reduction in hydrolytic activity. Isometric force and rates of ATP hydrolysis (ATPase) were measured as functions of the relative width of chemically skinned skeletal muscle fiber segments immersed in relaxing (pCa greater than 8) and activating (pCa 4.9) salt solutions. Osmotic radial compression of the fiber segment was produced (with little or no affect on striation spacing) by adding Dextran T500 to the bathing media. ADP as a product of ATP hydrolysis in fibers undergoing 10-15 min contractions was measured using high pressure liquid chromatography. Compression of the (initially swollen) fiber segment with dextran produced a slight (4%) increase in average active force and then, with further compression, a sharp decrease (with maximum around in situ width). With compression, the average ATPase of the fiber decreased monotonically, and with extreme compression (with 0.22 g dextran per ml), ATPase fell to a fifth of its level determined in dextran-free solution while force was abolished. The time course of active force development was described by the sum of two exponential functions, the faster of which characterized the rate of rise. Fiber compression (0.14 g dextran per ml) reduced the rate of rise of force ten-fold compared to that in dextran-free solution. Hindrance of cross movement is proposed to account for the inhibition of active force generation and (coupled) ATPase in compressed fibers.

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Year:  1984        PMID: 6201824     DOI: 10.1007/bf00585033

Source DB:  PubMed          Journal:  Pflugers Arch        ISSN: 0031-6768            Impact factor:   3.657


  12 in total

1.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

2.  Relaxation of glycerinated muscle: low-angle x-ray diffraction studies.

Authors:  E Rome
Journal:  J Mol Biol       Date:  1972-03-28       Impact factor: 5.469

3.  Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells.

Authors:  A Fabiato; F Fabiato
Journal:  J Physiol (Paris)       Date:  1979

4.  Axial elastic modulus as a function of relative fiber width in relaxed skinned skeletal muscle fibers.

Authors:  M R Berman; D W Maughan
Journal:  Pflugers Arch       Date:  1982-03       Impact factor: 3.657

5.  Force and ATPase rate in skinned skeletal muscle fibers.

Authors:  M J Kushmerick; B Krasner
Journal:  Fed Proc       Date:  1982-05

6.  Activation of fast skeletal muscle: contributions of studies on skinned fibers.

Authors:  E W Stephenson
Journal:  Am J Physiol       Date:  1981-01

7.  Inhibition of force production in compressed skinned muscle fibers of the frog.

Authors:  D W Maughan; R E Godt
Journal:  Pflugers Arch       Date:  1981-05       Impact factor: 3.657

8.  Geometrical factors influencing muscle force development. I. The effect of filament spacing upon axial forces.

Authors:  M Schoenberg
Journal:  Biophys J       Date:  1980-04       Impact factor: 4.033

9.  Influence of osmotic compression on calcium activation and tension in skinned muscle fibers of the rabbit.

Authors:  R E Godt; D W Maughan
Journal:  Pflugers Arch       Date:  1981-10       Impact factor: 3.657

10.  Nonparallel isometric tension response of rabbit soleus skinned muscle fibers to magnesium adenosine triphosphate and magnesium inosine triphosphate.

Authors:  B Krasner
Journal:  J Gen Physiol       Date:  1979-08       Impact factor: 4.086

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  24 in total

1.  Length-dependent effects of osmotic compression on skinned rabbit psoas muscle fibers.

Authors:  Y P Wang; F Fuchs
Journal:  J Muscle Res Cell Motil       Date:  2000-05       Impact factor: 2.698

2.  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

3.  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

4.  Active tension generation in isolated skeletal myofibrils.

Authors:  M L Bartoo; V I Popov; L A Fearn; G H Pollack
Journal:  J Muscle Res Cell Motil       Date:  1993-10       Impact factor: 2.698

5.  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

6.  Active force as a function of filament spacing in crayfish skinned muscle fibers.

Authors:  E W April; D W Maughan
Journal:  Pflugers Arch       Date:  1986-10       Impact factor: 3.657

7.  Shortening velocity in skinned single muscle fibers. Influence of filament lattice spacing.

Authors:  J M Metzger; R L Moss
Journal:  Biophys J       Date:  1987-07       Impact factor: 4.033

8.  Length and myofilament spacing-dependent changes in calcium sensitivity of skeletal fibres: effects of pH and ionic strength.

Authors:  D A Martyn; A M Gordon
Journal:  J Muscle Res Cell Motil       Date:  1988-10       Impact factor: 2.698

9.  Z-line structural diversity in frog single muscle fiber in the passive state.

Authors:  M Yamaguchi; G A Fuller; W Klomkleaw; S Yamano; T Oba
Journal:  J Muscle Res Cell Motil       Date:  1999-05       Impact factor: 2.698

10.  Myosin heads contact with thin filaments in compressed relaxed skinned fibres of frog skeletal muscle.

Authors:  Y Umazume; H Higuchi; S Takemori
Journal:  J Muscle Res Cell Motil       Date:  1991-10       Impact factor: 2.698

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