Myosin Filament Structure and Myosin Crossbridge Dynamics in Fish and Insect Muscles

2003 ◽  
pp. 251-266 ◽  
Author(s):  
John M. Squire ◽  
Hind A. AL-Khayat ◽  
Jeffrey J. Harford ◽  
Liam Hudson ◽  
Tom C. Irving ◽  
...  
Keyword(s):  
Myosin Filament ◽  
Filament Structure

scholarly journals Sarcomere-length dependence of myosin filament structure in skeletal muscle fibres of the frog

2014 ◽  
Vol 592 (5) ◽  
pp. 1119-1137 ◽  
Author(s):  
Massimo Reconditi ◽  
Elisabetta Brunello ◽  
Luca Fusi ◽  
Marco Linari ◽  
Manuel Fernandez Martinez ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sarcomere Length ◽  
Myosin Filament ◽  
Muscle Fibres ◽  
Length Dependence ◽  
Filament Structure ◽  
Skeletal Muscle Fibres

General model of myosin filament structure

1972 ◽  
Vol 72 (1) ◽  
pp. 125-138 ◽  
Author(s):  
J.M. Squire
Keyword(s):  
General Model ◽  
Myosin Filament ◽  
Filament Structure

scholarly journals Stabilizing effect of natural osmolyte on myosin filament structure

1999 ◽  
Vol 39 (supplement) ◽  
pp. S195
Author(s):  
Y. Okamoto ◽  
R. Nakamura ◽  
L. Yan ◽  
H. Mae ◽  
A. Kawabata
Keyword(s):  
Myosin Filament ◽  
Filament Structure ◽  
Stabilizing Effect

scholarly journals Myosin filament structure in vertebrate smooth muscle.

1996 ◽  
Vol 134 (1) ◽  
pp. 53-66 ◽  
Author(s):  
J Q Xu ◽  
B A Harder ◽  
P Uman ◽  
R Craig
Keyword(s):  
Smooth Muscle ◽  
Striated Muscle ◽  
Smooth Muscles ◽  
Helical Structure ◽  
Structure Characteristic ◽  
Myosin Filament ◽  
Filament Structure ◽  
Myosin Filaments ◽  
Intact Muscle

The in vivo structure of the myosin filaments in vertebrate smooth muscle is unknown. Evidence from purified smooth muscle myosin and from some studies of intact smooth muscle suggests that they may have a nonhelical, side-polar arrangement of crossbridges. However, the bipolar, helical structure characteristic of myosin filaments in striated muscle has not been disproved for smooth muscle. We have used EM to investigate this question in a functionally diverse group of smooth muscles (from the vascular, gastrointestinal, reproductive, and visual systems) from mammalian, amphibian, and avian species. Intact muscle under physiological conditions, rapidly frozen and then freeze substituted, shows many myosin filaments with a square backbone in transverse profile. Transverse sections of fixed, chemically skinned muscles also show square backbones and, in addition, reveal projections (crossbridges) on only two opposite sides of the square. Filaments gently isolated from skinned smooth muscles and observed by negative staining show crossbridges with a 14.5-nm repeat projecting in opposite directions on opposite sides of the filament. Such filaments subjected to low ionic strength conditions show bare filament ends and an antiparallel arrangement of myosin tails along the length of the filament. All of these observations are consistent with a side-polar structure and argue against a bipolar, helical crossbridge arrangement. We conclude that myosin filaments in all smooth muscles, regardless of function, are likely to be side-polar. Such a structure could be an important factor in the ability of smooth muscles to contract by large amounts.

General model of myosin filament structure

1973 ◽  
Vol 77 (2) ◽  
pp. 291-323 ◽  
Author(s):  
J.M. Squire
Keyword(s):  
General Model ◽  
Myosin Filament ◽  
Filament Structure

scholarly journals Calcium Dependence of Myosin Filament Structure in Demembranated Trabeculae from Rat Heart

2021 ◽  
Vol 120 (3) ◽  
pp. 252a
Author(s):  
Luca Fusi ◽  
Yanhong Wang ◽  
So-Jin Park-Holohan ◽  
Andrea Ghisleni ◽  
Theyencheri Narayanan ◽  
...  
Keyword(s):  
Rat Heart ◽  
Myosin Filament ◽  
Calcium Dependence ◽  
Filament Structure

Structure of Myosin Subfragment-1 from Electron Microscopy and Crystallography

1988 ◽  
Vol 46 ◽  
pp. 156-157
Author(s):  
Donald A. Winkelmann
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Actin Filaments ◽  
Light Chains ◽  
Myosin Filament ◽  
Primary Role ◽  
Heavy Chains ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Globular Head

The primary role of the interaction of actin and myosin is the generation of force and motion as a direct consequence of the cyclic interaction of myosin crossbridges with actin filaments. Myosin is composed of six polypeptides: two heavy chains of molecular weight 220,000 daltons and two pairs of light chains of molecular weight 17,000-23,000. The C-terminal portions of the myosin heavy chains associate to form an α-helical coiled-coil rod which is responsible for myosin filament formation. The N-terminal portion of each heavy chain associates with two different light chains to form a globular head that binds actin and hydrolyses ATP. Myosin can be fragmented by limited proteolysis into several structural and functional domains. It has recently been demonstrated using an in vitro movement assay that the globular head domain, subfragment-1, is sufficient to cause sliding movement of actin filaments.The discovery of conditions for crystallization of the myosin subfragment-1 (S1) has led to a systematic analysis of S1 structure by x-ray crystallography and electron microscopy. Image analysis of electron micrographs of thin sections of small S1 crystals has been used to determine the structure of S1 in the crystal lattice.

The Hierarchic Order of Intermediate Filament Structure and Assembly

1985 ◽  
Vol 43 ◽  
pp. 722-725
Author(s):  
U. Aebi ◽  
E.C. Glavaris ◽  
R. Eichner
Keyword(s):  
Tissue Specificity ◽  
Structural Model ◽  
Eukaryotic Cells ◽  
Cdna Sequencing ◽  
Filament Structure ◽  
Keratin Filaments ◽  
Isoelectric Points ◽  
Immunological Crossreactivity

Five different classes of intermediate-sized filaments (IFs) have been identified in differentiated eukaryotic cells: vimentin in mesenchymal cells, desmin in muscle cells, neurofilaments in nerve cells, glial filaments in glial cells and keratin filaments in epithelial cells. Despite their tissue specificity, all IFs share several common attributes, including immunological crossreactivity, similar morphology (e.g. about 10 nm diameter - hence ‘10-nm filaments’) and the ability to reassemble in vitro from denatured subunits into filaments virtually indistinguishable from those observed in vivo. Further more, despite their proteinchemical heterogeneity (their MWs range from 40 kDa to 200 kDa and their isoelectric points from about 5 to 8), protein and cDNA sequencing of several IF polypeptides (for refs, see 1,2) have provided the framework for a common structural model of all IF subunits.

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