scholarly journals Development transitions of thin filament proteins in rat extraocular muscles

2013 ◽  
Vol 319 (3) ◽  
pp. 23-31 ◽  
Author(s):  
Carole L. Moncman ◽  
Miguel E. Andrade ◽  
Andrea A. McCool ◽  
Colleen A. McMullen ◽  
Francisco H. Andrade
Keyword(s):  
Thin Filament ◽  
Extraocular Muscles ◽  
Thin Filament Proteins

scholarly journals Spaceflight results in increase of thick filament but not thin filament proteins in the paramyosin mutant of Caenorhabditis elegans

2008 ◽  
Vol 41 (5) ◽  
pp. 816-823 ◽  
Author(s):  
R. Adachi ◽  
T. Takaya ◽  
K. Kuriyama ◽  
A. Higashibata ◽  
N. Ishioka ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Thin Filament ◽  
Thick Filament ◽  
Thin Filament Proteins

scholarly journals KLHL40 deficiency destabilizes thin filament proteins and promotes nemaline myopathy

2014 ◽  
Vol 124 (8) ◽  
pp. 3529-3539 ◽  
Author(s):  
Ankit Garg ◽  
Jason O’Rourke ◽  
Chengzu Long ◽  
Jonathan Doering ◽  
Gianina Ravenscroft ◽  
...  
Keyword(s):  
Thin Filament ◽  
Nemaline Myopathy ◽  
Thin Filament Proteins

Expression of Fast Thin Filament Proteins. Defining Fiber Archetypes in a Molecular Continuum

1990 ◽  
pp. 279-292 ◽  
Author(s):  
Fred Schachat ◽  
Margaret M. Briggs ◽  
Edward K. Williamson ◽  
Hirschel McGinnis ◽  
Michael S. Diamond ◽  
...  
Keyword(s):  
Thin Filament ◽  
Thin Filament Proteins

Pig platelet tropomyosin: Interactions with the other thin-filament proteins

1986 ◽  
Vol 192 (4) ◽  
pp. 815-830 ◽  
Author(s):  
G. Pruliere ◽  
S.D. Fuller ◽  
A.G. Weeds ◽  
A. d'Albis ◽  
E. der Terrossian
Keyword(s):  
Thin Filament ◽  
The Other ◽  
Thin Filament Proteins

Doxorubicin and covalently crosslinked doxorubicin derivatives binding to purified cardiac thin-filament proteins in vitro

1985 ◽  
Vol 43 (1) ◽  
pp. 64-73 ◽  
Author(s):  
William Lewis ◽  
Kevin Beckenstein ◽  
Lawrence Shapiro ◽  
Saul Puszkin
Keyword(s):  
Thin Filament ◽  
Thin Filament Proteins

scholarly journals Mechanism of regulation of phosphate dissociation from actomyosin-ADP-Pi by thin filament proteins

2002 ◽  
Vol 99 (26) ◽  
pp. 16731-16736 ◽  
Author(s):  
D. H. Heeley ◽  
B. Belknap ◽  
H. D. White
Keyword(s):  
Thin Filament ◽  
Thin Filament Proteins

Thin Filament Proteins and Thin Filament-Linked Regulation of Vertebrate Muscle Contractio

1984 ◽  
Vol 16 (3) ◽  
pp. 235-305 ◽  
Author(s):  
Paul C. Leavis ◽  
John Gergely ◽  
Andrew G. Szent-Gyorgyi
Keyword(s):  
Thin Filament ◽  
Vertebrate Muscle ◽  
Thin Filament Proteins

Myosin MgADP release rate decreases at longer sarcomere length to prolong myosin attachment time in skinned rat myocardium

2015 ◽  
Vol 309 (12) ◽  
pp. H2087-H2097 ◽  
Author(s):  
Bertrand C. W. Tanner ◽  
Jason J. Breithaupt ◽  
Peter O. Awinda
Keyword(s):  
Release Rate ◽  
Thin Filament ◽  
Molecular Mechanisms ◽  
Sarcomere Length ◽  
Cardiac Contractility ◽  
Force Production ◽  
Cross Bridge ◽  
Thin Filament Proteins ◽  
Filament Activation ◽  
Ventricular Filling

Cardiac contractility increases as sarcomere length increases, suggesting that intrinsic molecular mechanisms underlie the Frank-Starling relationship to confer increased cardiac output with greater ventricular filling. The capacity of myosin to bind with actin and generate force in a muscle cell is Ca2+ regulated by thin-filament proteins and spatially regulated by sarcomere length as thick-to-thin filament overlap varies. One mechanism underlying greater cardiac contractility as sarcomere length increases could involve longer myosin attachment time ( t on) due to slowed myosin kinetics at longer sarcomere length. To test this idea, we used stochastic length-perturbation analysis in skinned rat papillary muscle strips to measure t on as [MgATP] varied (0.05–5 mM) at 1.9 and 2.2 μm sarcomere lengths. From this t on-MgATP relationship, we calculated cross-bridge MgADP release rate and MgATP binding rates. As MgATP increased, t on decreased for both sarcomere lengths, but t on was roughly 70% longer for 2.2 vs. 1.9 μm sarcomere length at maximally activated conditions. These t on differences were driven by a slower MgADP release rate at 2.2 μm sarcomere length (41 ± 3 vs. 74 ± 7 s−1), since MgATP binding rate was not different between the two sarcomere lengths. At submaximal activation levels near the pCa50 value of the tension-pCa relationship for each sarcomere length, length-dependent increases in t on were roughly 15% longer for 2.2 vs. 1.9 μm sarcomere length. These changes in cross-bridge kinetics could amplify cooperative cross-bridge contributions to force production and thin-filament activation at longer sarcomere length and suggest that length-dependent changes in myosin MgADP release rate may contribute to the Frank-Starling relationship in the heart.

scholarly journals Ubiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and thin filaments in muscle atrophy

2012 ◽  
Vol 198 (4) ◽  
pp. 575-589 ◽  
Author(s):  
Shenhav Cohen ◽  
Bo Zhai ◽  
Steven P. Gygi ◽  
Alfred L. Goldberg
Keyword(s):  
Muscle Atrophy ◽  
Ubiquitin Ligase ◽  
Thin Filament ◽  
Thick Filament ◽  
Myofibrillar Proteins ◽  
Rapid Loss ◽  
Thin Filaments ◽  
Thin Filament Proteins ◽  
Rapid Destruction ◽  
Fiber Atrophy

During muscle atrophy, myofibrillar proteins are degraded in an ordered process in which MuRF1 catalyzes ubiquitylation of thick filament components (Cohen et al. 2009. J. Cell Biol. http://dx.doi.org/10.1083/jcb.200901052). Here, we show that another ubiquitin ligase, Trim32, ubiquitylates thin filament (actin, tropomyosin, troponins) and Z-band (α-actinin) components and promotes their degradation. Down-regulation of Trim32 during fasting reduced fiber atrophy and the rapid loss of thin filaments. Desmin filaments were proposed to maintain the integrity of thin filaments. Accordingly, we find that the rapid destruction of thin filament proteins upon fasting was accompanied by increased phosphorylation of desmin filaments, which promoted desmin ubiquitylation by Trim32 and degradation. Reducing Trim32 levels prevented the loss of both desmin and thin filament proteins. Furthermore, overexpression of an inhibitor of desmin polymerization induced disassembly of desmin filaments and destruction of thin filament components. Thus, during fasting, desmin phosphorylation increases and enhances Trim32-mediated degradation of the desmin cytoskeleton, which appears to facilitate the breakdown of Z-bands and thin filaments.

scholarly journals Desensitization of Myofilaments to Ca 2+ as a Therapeutic Target for Hypertrophic Cardiomyopathy With Mutations in Thin Filament Proteins

2014 ◽  
Vol 7 (2) ◽  
pp. 132-143 ◽  
Author(s):  
Marco L. Alves ◽  
Fernando A.L. Dias ◽  
Robert D. Gaffin ◽  
Jillian N. Simon ◽  
Eric M. Montminy ◽  
...  
Keyword(s):  
Hypertrophic Cardiomyopathy ◽  
Therapeutic Target ◽  
Thin Filament ◽  
Thin Filament Proteins
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