Muscle cell and motor protein function in patients with a IIa myosin missense mutation (Glu-706 to Lys)

Li, Mingxin; Lionikas, Arimantas; Yu, Fang; Tajsharghi, Homa; Oldfors, Anders; Larsson, Lars

doi:10.1016/j.nmd.2006.07.023

Cited by 15 publications

(14 citation statements)

References 39 publications

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“…In accordance with previous studies, the motility speed of all the species demonstrated a high temperature dependence (Rossi et al. 2005, Li et al. 2006), i.e.…”

Section: Discussionsupporting

confidence: 92%

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There is no slowing of motility speed with increased body size in rat, human, horse and rhinoceros independent on temperature and skeletal muscle myosin isoform

Marx

Larsson

2011

Acta Physiologica

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The scaling effect of body size and limb length on shortening velocity at the muscle fibre level, i.e. the decreasing shortening velocity associated with increasing body weight and limb length, was not confirmed at the motor protein level when including mammals of very large size. Thus, other factors than myosin structure and function appear to cause this scaling effect and thin filament isoform expression or myofilament lattice spacing are forwarded as alternative underlying factors.

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“…In accordance with previous studies, the motility speed of all the species demonstrated a high temperature dependence (Rossi et al. 2005, Li et al. 2006), i.e.…”

Section: Discussionsupporting

confidence: 92%

“…However, the relative and frequently absolute differences in motility speed between different MyHC isoforms decreased with increasing temperature in accordance with previous studies in rat, rabbit and humans (Rossi et al. 2005, Li et al. 2006).…”

Section: Discussionsupporting

confidence: 92%

There is no slowing of motility speed with increased body size in rat, human, horse and rhinoceros independent on temperature and skeletal muscle myosin isoform

Marx

Larsson

2011

Acta Physiologica

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“…The results from this study confirmed and extended our previous studies: (i) The significant difference between different myosin isoforms in speed and force-generating capacity was confirmed at the motor protein level (Hook et al ., 1999 ; Hook & Larsson, 2000 ; Hook et al ., 2001 ; Li et al ., 2006 ; Li & Larsson, 2010 ). (ii) An aging-related slowing of motility speed was observed in both type I and IIa MyHC assays, but the force-generating capacity was unaffected by age, irrespective of MyHC isoform.…”

Section: Discussionmentioning

confidence: 99%

Aberrant post-translational modifications compromise human myosin motor function in old age

Ogilvie

Ochala

et al. 2015

Aging Cell

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Novel experimental methods, including a modified single fiber in vitro motility assay, X-ray diffraction experiments, and mass spectrometry analyses, have been performed to unravel the molecular events underlying the aging-related impairment in human skeletal muscle function at the motor protein level. The effects of old age on the function of specific myosin isoforms extracted from single human muscle fiber segments, demonstrated a significant slowing of motility speed (P < 0.001) in old age in both type I and IIa myosin heavy chain (MyHC) isoforms. The force-generating capacity of the type I and IIa MyHC isoforms was, on the other hand, not affected by old age. Similar effects were also observed when the myosin molecules extracted from muscle fibers were exposed to oxidative stress. X-ray diffraction experiments did not show any myofilament lattice spacing changes, but unraveled a more disordered filament organization in old age as shown by the greater widths of the 1, 0 equatorial reflections. Mass spectrometry (MS) analyses revealed eight age-specific myosin post-translational modifications (PTMs), in which two were located in the motor domain (carbonylation of Pro79 and Asn81) and six in the tail region (carbonylation of Asp900, Asp904, and Arg908; methylation of Glu1166; deamidation of Gln1164 and Asn1168). However, PTMs in the motor domain were only observed in the IIx MyHC isoform, suggesting PTMs in the rod region contributed to the observed disordering of myosin filaments and the slowing of motility speed. Hence, interventions that would specifically target these PTMs are warranted to reverse myosin dysfunction in old age.

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“…To keep sarcomeres in a relaxed state, embryos were incubated in relaxation buffer (20 mM imadazole, 5 mM EGTA, 7 mM MgCl2, 5 mM creatine phosphate, 10 mM ATP, 100 mM KCl) for 1.5 h before flxation (Brixius et al, 2000; Li et al, 2006). The following antibodies were used at the indicated dilutions: anti-sarcomeric α-actinin (clone EA53, Sigma) at 1:1000, F59 (Developmental Studies Hybridoma Bank, DSHB) at 1:10, MEF2 (C-21, Santa Cruz Biotechnology) at 1:50, anti-myomesin (DSHB) at 1:100, anti-tropomyosin (CH1, Sigma) at 1:100, anti-troponin T (Sigma) at 1:200, anti-cardiac and skeletal troponin I (ABR-Affinity BioReagents) at 1:200, and Zn5 (ZIRC) at 1:500.…”

Section: Methodsmentioning

confidence: 99%

Myofibrillogenesis in the developing zebrafish heart: A functional study of tnnt2

Huang

Zhang

2009

Developmental Biology

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Various hypotheses have been proposed to explain the molecule processes of sarcomere assembly, partially due to the lack of systematic genetic studies of sarcomeric genes in an in vivo model. Towards the goal of developing zebrafish as a vertebrate model for this purpose, we characterized myofibrillogenesis in a developing zebrafish heart and went on to examine the functions of cardiac troponin T (tnnt2). We found that sarcomere assembly in zebrafish heart was initiated from a non-striated actin filament network at the perimembrane region, whereas sarcomeric myosin is independently assembled into thick filaments of variable length before integrating into the thin filament network. Compared to Z-discs that are initially aligned to form shorter periodic dots and expanded longitudinally at a later time, M-lines assemble later and have a constant length. Depletion of full-length tnnt2 disrupted the striation of thin filaments and Z-bodies, which sequentially affects the striation of thick filaments and M-lines. Conversely, truncation of a C-terminal troponin complex-binding domain did not affect the striation of these sarcomere sub-structures, but resulted in reduced cardiomyocyte size. In summary, our data indicates that zebrafish are a valuable in vivo model for studying both myofibrillogenesis and sarcomere-based cardiac diseases.

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Muscle cell and motor protein function in patients with a IIa myosin missense mutation (Glu-706 to Lys)

Cited by 15 publications

References 39 publications

There is no slowing of motility speed with increased body size in rat, human, horse and rhinoceros independent on temperature and skeletal muscle myosin isoform

There is no slowing of motility speed with increased body size in rat, human, horse and rhinoceros independent on temperature and skeletal muscle myosin isoform

Aberrant post-translational modifications compromise human myosin motor function in old age

Myofibrillogenesis in the developing zebrafish heart: A functional study of tnnt2

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