Literature DB >> 9562033

The filament lattice of striated muscle.

B M Millman1.   

Abstract

The filament lattice of striated muscle is an overlapping hexagonal array of thick and thin filaments within which muscle contraction takes place. Its structure can be studied by electron microscopy or X-ray diffraction. With the latter technique, structural changes can be monitored during contraction and other physiological conditions. The lattice of intact muscle fibers can change size through osmotic swelling or shrinking or by changing the sarcomere length of the muscle. Similarly, muscle fibers that have been chemically or mechanically skinned can be compressed with bathing solutions containing very large inert polymeric molecules. The effects of lattice change on muscle contraction in vertebrate skeletal and cardiac muscle and in invertebrate striated muscle are reviewed. The force developed, the speed of shortening, and stiffness are compared with structural changes occurring within the lattice. Radial forces between the filaments in the lattice, which can include electrostatic, Van der Waals, entropic, structural, and cross bridge, are assessed for their contributions to lattice stability and to the contraction process.

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Mesh:

Year:  1998        PMID: 9562033     DOI: 10.1152/physrev.1998.78.2.359

Source DB:  PubMed          Journal:  Physiol Rev        ISSN: 0031-9333            Impact factor:   37.312


  107 in total

1.  Time-resolved X-ray diffraction by skinned skeletal muscle fibers during activation and shortening.

Authors:  B K Hoskins; C C Ashley; G Rapp; P J Griffiths
Journal:  Biophys J       Date:  2001-01       Impact factor: 4.033

2.  Morphology and transverse stiffness of Drosophila myofibrils measured by atomic force microscopy.

Authors:  L R Nyland; D W Maughan
Journal:  Biophys J       Date:  2000-03       Impact factor: 4.033

3.  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

4.  Sarcomeric visco-elasticity of chemically skinned skeletal muscle fibres of the rabbit at rest.

Authors:  K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  2001       Impact factor: 2.698

Review 5.  M-band: a safeguard for sarcomere stability?

Authors:  Irina Agarkova; Elisabeth Ehler; Stephan Lange; Roman Schoenauer; Jean-Claude Perriard
Journal:  J Muscle Res Cell Motil       Date:  2003       Impact factor: 2.698

6.  Sarcomere-length dependence of lattice volume and radial mass transfer of myosin cross-bridges in rat papillary muscle.

Authors:  Naoto Yagi; Hiroshi Okuyama; Hiroko Toyota; Junichi Araki; Juichiro Shimizu; Gentaro Iribe; Kazufumi Nakamura; Satoshi Mohri; Katsuhiko Tsujioka; Hiroyuki Suga; Fumihiko Kajiya
Journal:  Pflugers Arch       Date:  2004-02-06       Impact factor: 3.657

7.  Troponin I in the murine myocardium: influence on length-dependent activation and interfilament spacing.

Authors:  John P Konhilas; Thomas C Irving; Beata M Wolska; Eias E Jweied; Anne F Martin; R John Solaro; Pieter P de Tombe
Journal:  J Physiol       Date:  2003-01-24       Impact factor: 5.182

8.  Random walk analysis of restricted metabolite diffusion in skeletal myofibril systems.

Authors:  Mayis K Aliev; Alexander N Tikhonov
Journal:  Mol Cell Biochem       Date:  2004 Jan-Feb       Impact factor: 3.396

9.  Second harmonic generation microscopy probes different states of motor protein interaction in myofibrils.

Authors:  Sebastian Schürmann; Frederic von Wegner; Rainer H A Fink; Oliver Friedrich; Martin Vogel
Journal:  Biophys J       Date:  2010-09-22       Impact factor: 4.033

Review 10.  Strategies for targeting the cardiac sarcomere: avenues for novel drug discovery.

Authors:  Joshua B Holmes; Chang Yoon Doh; Ranganath Mamidi; Jiayang Li; Julian E Stelzer
Journal:  Expert Opin Drug Discov       Date:  2020-02-18       Impact factor: 6.098

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