Literature DB >> 4033798

Actomyosin structure in contracting muscle detected by rapid freezing.

S Tsukita, M Yano.   

Abstract

It is now widely accepted that the ATP-induced active sliding of adjacent thin and thick filaments mediated by myosin heads (cross-bridges) is responsible for muscle contraction. Despite intensive studies, the behaviour of the myosin heads during muscle contraction is still unclear. Recent progress in the rapid freezing electron microscope technique has greatly improved the temporal resolution of the images that can be obtained. Here, we report a new type of actomyosin structure captured by rapid freezing. We have analysed images from thin sections of freeze-substituted rabbit skeletal muscle rapidly frozen during isometric contraction. For comparison, we also studied relaxed and rigor muscles. Our results show that, during isometric contraction, most myosin heads are regularly arrayed along the helix of the actin filaments and that this actomyosin structure appears to be distinct from that observed in rigor muscle.

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Year:  1985        PMID: 4033798     DOI: 10.1038/317182a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  29 in total

Review 1.  Myosin step size: estimates from motility assays and shortening muscle.

Authors:  K Burton
Journal:  J Muscle Res Cell Motil       Date:  1992-12       Impact factor: 2.698

2.  X-ray diffraction indicates that active cross-bridges bind to actin target zones in insect flight muscle.

Authors:  R T Tregear; R J Edwards; T C Irving; K J Poole; M C Reedy; H Schmitz; E Towns-Andrews; M K Reedy
Journal:  Biophys J       Date:  1998-03       Impact factor: 4.033

3.  Structure and periodicities of cross-bridges in relaxation, in rigor, and during contractions initiated by photolysis of caged Ca2+.

Authors:  T D Lenart; J M Murray; C Franzini-Armstrong; Y E Goldman
Journal:  Biophys J       Date:  1996-11       Impact factor: 4.033

4.  Metabolic iteration, evolution and cognition in cellular proliferation.

Authors:  E Cervén
Journal:  Experientia       Date:  1987-10-15

Review 5.  Actin filament organization and myosin head labelling patterns in vertebrate skeletal muscles in the rigor and weak binding states.

Authors:  J M Squire; J J Harford
Journal:  J Muscle Res Cell Motil       Date:  1988-08       Impact factor: 2.698

6.  Intensity increases of actin layer-lines on activation of the Limulus muscle.

Authors:  Y Maéda; C Boulin; A Gabriel; I Sumner; M H Koch
Journal:  Biophys J       Date:  1986-12       Impact factor: 4.033

7.  Constraints on the attachment of myosin to actin.

Authors:  R Tregear
Journal:  J Muscle Res Cell Motil       Date:  1988-08       Impact factor: 2.698

8.  Localization of adhesive proteins in two newly subdivided zones in electron-lucent matrix of human platelet alpha-granules.

Authors:  H Suzuki; Y Katagiri; S Tsukita; K Tanoue; H Yamazaki
Journal:  Histochemistry       Date:  1990

9.  Transients of fluorescence polarization in skeletal muscle fibers labeled with rhodamine on the regulatory light chain.

Authors:  T S Allen; C Sabido-David; N Ling; M Irving; Y E Goldman
Journal:  Biophys J       Date:  1995-04       Impact factor: 4.033

10.  Structural change of crossbridges of rabbit skeletal muscle during isometric contraction.

Authors:  K Hirose; T Wakabayashi
Journal:  J Muscle Res Cell Motil       Date:  1993-08       Impact factor: 2.698

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