Literature DB >> 10545136

Structural responses to the photolytic release of ATP in frog muscle fibres, observed by time-resolved X-ray diffraction.

A K Tsaturyan1, S Y Bershitsky, R Burns, Z H He, M A Ferenczi.   

Abstract

1. Structural changes following the photolytic release of ATP were observed in single, permeabilised fibres of frog skeletal muscle at 5-6 C, using time-resolved, low-angle X-ray diffraction. The structural order in the fibres and their isometric function were preserved by cross-linking 10-20 % of the myosin cross-bridges to the thin filaments. 2. The time courses of the change in force, stiffness and in intensity of the main equatorial reflections (1,0) and (1,1), of the third myosin layer line (M3) at a reciprocal spacing of (14.5 nm)-1 on the meridian and of the first myosin-actin layer line (LL1) were measured with 1 ms time resolution. 3. In the absence of Ca2+, photolytic release of ATP in muscle fibres initially in the rigor state caused the force and stiffness to decrease monotonically towards their values in relaxed muscle fibres. 4. In the presence of Ca2+, photolytic release of ATP resulted in an initial rapid decrease in force, followed by a slower increase to the isometric plateau. Muscle fibre stiffness decreased rapidly to approximately 65 % of its value in rigor. 5. In the absence of Ca2+, changes on the equator, in LL1 and in M3 occurred with a time scale comparable to that of the changes in tension and stiffness. 6. In the presence of Ca2+, the changes on the equator and LL1 occurred simultaneously with the early phase of tension decrease. The changes in the intensity of M3 (IM3) occurred on the time scale of the subsequent increase in force. The time courses of the changes in tension and IM3 were similar following the photolytic release of 0. 33 or 1.1 mM ATP. However the gradual return towards the rigor state began earlier when only 0.33 mM ATP was released. 7. In the presence of Ca2+, the time course of changes in IM3 closely mimicked that of force development following photolytic release of ATP. This is consistent with models that propose that force development results from a change in the average orientation of cross-bridges, although other factors, such as their redistribution, may also be involved.

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Year:  1999        PMID: 10545136      PMCID: PMC2269614          DOI: 10.1111/j.1469-7793.1999.00681.x

Source DB:  PubMed          Journal:  J Physiol        ISSN: 0022-3751            Impact factor:   5.182


  25 in total

1.  Evidence for structurally different attached states of myosin cross-bridges on actin during contraction of fish muscle.

Authors:  J J Harford; J M Squire
Journal:  Biophys J       Date:  1992-08       Impact factor: 4.033

2.  Mechanical and structural properties underlying contraction of skeletal muscle fibers after partial 1-ethyl-3-[3-dimethylamino)propyl]carbodiimide cross-linking.

Authors:  S Bershitsky; A Tsaturyan; O Bershitskaya; G Mashanov; P Brown; M Webb; M A Ferenczi
Journal:  Biophys J       Date:  1996-09       Impact factor: 4.033

3.  Muscle force is generated by myosin heads stereospecifically attached to actin.

Authors:  S Y Bershitsky; A K Tsaturyan; O N Bershitskaya; G I Mashanov; P Brown; R Burns; M A Ferenczi
Journal:  Nature       Date:  1997-07-10       Impact factor: 49.962

4.  ATPase kinetics on activation of rabbit and frog permeabilized isometric muscle fibres: a real time phosphate assay.

Authors:  Z H He; R K Chillingworth; M Brune; J E Corrie; D R Trentham; M R Webb; M A Ferenczi
Journal:  J Physiol       Date:  1997-05-15       Impact factor: 5.182

5.  Structural changes in the actomyosin cross-bridges associated with force generation.

Authors:  B Brenner; L C Yu
Journal:  Proc Natl Acad Sci U S A       Date:  1993-06-01       Impact factor: 11.205

6.  Kinetic mechanism of myofibril ATPase.

Authors:  Y Z Ma; E W Taylor
Journal:  Biophys J       Date:  1994-05       Impact factor: 4.033

7.  Mechanical study of rat soleus muscle using caged ATP and X-ray diffraction: high ADP affinity of slow cross-bridges.

Authors:  K Horiuti; N Yagi; S Takemori
Journal:  J Physiol       Date:  1997-07-15       Impact factor: 5.182

8.  X-ray equatorial diffraction during ATP-induced Ca(2+)-free muscle contraction and the effect of ADP.

Authors:  K Horiuti; N Yagi; K Kagawa; K Wakabayashi; K Yamada
Journal:  J Biochem       Date:  1994-05       Impact factor: 3.387

9.  Kinetics of relaxation from rigor of permeabilized fast-twitch skeletal fibers from the rabbit using a novel caged ATP and apyrase.

Authors:  H Thirlwell; J E Corrie; G P Reid; D R Trentham; M A Ferenczi
Journal:  Biophys J       Date:  1994-12       Impact factor: 4.033

10.  Inhibition of unloaded shortening velocity in permeabilized muscle fibres by caged ATP compounds.

Authors:  H Thirlwell; J A Sleep; M A Ferenczi
Journal:  J Muscle Res Cell Motil       Date:  1995-04       Impact factor: 2.698

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  5 in total

1.  Chronicle of skinned muscle fibres.

Authors:  G J Stienen
Journal:  J Physiol       Date:  2000-08-15       Impact factor: 5.182

2.  Single turnover of cross-bridge ATPase in rat muscle fibers studied by photolysis of caged ATP.

Authors:  K Horiuti; N Yagi; S Takemori
Journal:  J Muscle Res Cell Motil       Date:  2001       Impact factor: 2.698

3.  Structural transients of contractile proteins upon sudden ATP liberation in skeletal muscle fibers.

Authors:  Jun'ichi Wakayama; Takumi Tamura; Naoto Yagi; Hiroyuki Iwamoto
Journal:  Biophys J       Date:  2004-07       Impact factor: 4.033

Review 4.  Nanomolar ATP binding to single myosin cross-bridges in rigor: a molecular approach to studying myosin ATP kinetics using single human cardiomyocytes.

Authors:  Elvis Pandzic; Christian A Morkel; Amy Li; Roger Cooke; Renee M Whan; Cristobal G Dos Remedios
Journal:  Biophys Rev       Date:  2020-07-09

5.  Analysis methods and quality criteria for investigating muscle physiology using x-ray diffraction.

Authors:  John M Squire; Carlo Knupp
Journal:  J Gen Physiol       Date:  2021-08-05       Impact factor: 4.086

  5 in total

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