Faculty Opinions recommendation of S-nitrosylation and S-glutathionylation of Cys134 on troponin I have opposing competitive actions on Ca2+ sensitivity in rat fast-twitch muscle fibers.

2017 ◽  
Author(s):  
Håkan Westerblad
Keyword(s):  
Troponin I ◽  
Muscle Fibers ◽  
Fast Twitch Muscle ◽  
Competitive Actions ◽  
Fast Twitch

S-nitrosylation and S-glutathionylation of Cys134 on troponin I have opposing competitive actions on Ca2+ sensitivity in rat fast-twitch muscle fibers

2017 ◽  
Vol 312 (3) ◽  
pp. C316-C327 ◽  
Author(s):  
T. L. Dutka ◽  
J. P. Mollica ◽  
C. R. Lamboley ◽  
V. C. Weerakkody ◽  
D. W. Greening ◽  
...  
Keyword(s):  
Troponin I ◽  
Muscle Fibers ◽  
Contractile Apparatus ◽  
Slow Twitch ◽  
Mechanistic Basis ◽  
Opposing Effects ◽  
Slow Twitch Fibers ◽  
Competitive Actions ◽  
Fast Twitch ◽  
Biotin Switch

Nitric oxide is generated in skeletal muscle with activity and decreases Ca2+ sensitivity of the contractile apparatus, putatively by S-nitrosylation of an unidentified protein. We investigated the mechanistic basis of this effect and its relationship to the oxidation-induced increase in Ca2+ sensitivity in mammalian fast-twitch (FT) fibers mediated by S-glutathionylation of Cys134 on fast troponin I (TnIf). Force-[Ca2+] characteristics of the contractile apparatus in mechanically skinned fibers were assessed by direct activation with heavily Ca2+-buffered solutions. Treatment with S-nitrosylating agents, S-nitrosoglutathione (GSNO) or S-nitroso- N-acetyl-penicillamine (SNAP), decreased pCa50 ( = −log10 [Ca2+] at half-maximal activation) by ~−0.07 pCa units in rat and human FT fibers without affecting maximum force, but had no effect on rat and human slow-twitch fibers or toad or chicken FT fibers, which all lack Cys134. The Ca2+ sensitivity decrease was 1) fully reversed with dithiothreitol or reduced glutathione, 2) at least partially reversed with ascorbate, indicative of involvement of S-nitrosylation, and 3) irreversibly blocked by low concentration of the alkylating agent, N-ethylmaleimide (NEM). The biotin-switch assay showed that both GSNO and SNAP treatments caused S-nitrosylation of TnIf. S-glutathionylation pretreatment blocked the effects of S-nitrosylation on Ca2+ sensitivity, and vice-versa. S-nitrosylation pretreatment prevented NEM from irreversibly blocking S-glutathionylation of TnIf and its effects on Ca2+ sensitivity, and likewise S-glutathionylation pretreatment prevented NEM block of S-nitrosylation. Following substitution of TnIf into rat slow-twitch fibers, S-nitrosylation treatment caused decreased Ca2+ sensitivity. These findings demonstrate that S-nitrosylation and S-glutathionylation exert opposing effects on Ca2+ sensitivity in mammalian FT muscle fibers, mediated by competitive actions on Cys134 of TnIf.

scholarly journals High-speed jaw-opening exercise in training suprahyoid fast-twitch muscle fibers

2018 ◽  
Vol Volume 13 ◽  
pp. 125-131 ◽  
Author(s):  
Mariko Matsubara ◽  
Haruka Tohara ◽  
Koji Hara ◽  
Hiromichi Shinozaki ◽  
Yasuhiro Yamazaki ◽  
...  
Keyword(s):  
High Speed ◽  
Muscle Fibers ◽  
Jaw Opening ◽  
Fast Twitch Muscle ◽  
Fast Twitch

scholarly journals lncRNA-Six1 Is a Target of miR-1611 that Functions as a ceRNA to Regulate Six1 Protein Expression and Fiber Type Switching in Chicken Myogenesis

Cells ◽  
2018 ◽  
Vol 7 (12) ◽  
pp. 243 ◽  
Author(s):  
Manting Ma ◽  
Bolin Cai ◽  
Liang Jiang ◽  
Bahareldin Ali Abdalla ◽  
Zhenhui Li ◽  
...  
Keyword(s):  
Fiber Type ◽  
Muscle Fibers ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Proliferation And Differentiation ◽  
Slow Twitch Muscle ◽  
Fast Twitch Muscle ◽  
Slow Twitch ◽  
Slow Twitch Fibers ◽  
Fast Twitch

Emerging studies indicate important roles for non-coding RNAs (ncRNAs) as essential regulators in myogenesis, but relatively less is known about their function. In our previous study, we found that lncRNA-Six1 can regulate Six1 in cis to participate in myogenesis. Here, we studied a microRNA (miRNA) that is specifically expressed in chickens (miR-1611). Interestingly, miR-1611 was found to contain potential binding sites for both lncRNA-Six1 and Six1, and it can interact with lncRNA-Six1 to regulate Six1 expression. Overexpression of miR-1611 represses the proliferation and differentiation of myoblasts. Moreover, miR-1611 is highly expressed in slow-twitch fibers, and it drives the transformation of fast-twitch muscle fibers to slow-twitch muscle fibers. Together, these data demonstrate that miR-1611 can mediate the regulation of Six1 by lncRNA-Six1, thereby affecting proliferation and differentiation of myoblasts and transformation of muscle fiber types.

scholarly journals S-Glutathionylation of troponin I (fast) increases contractile apparatus Ca2+sensitivity in fast-twitch muscle fibres of rats and humans

2012 ◽  
Vol 590 (6) ◽  
pp. 1443-1463 ◽  
Author(s):  
J. P. Mollica ◽  
T. L. Dutka ◽  
T. L. Merry ◽  
C. R. Lamboley ◽  
G. K. McConell ◽  
...  
Keyword(s):  
Troponin I ◽  
Muscle Fibres ◽  
Contractile Apparatus ◽  
Fast Twitch Muscle ◽  
Fast Twitch

scholarly journals Ca2+ activation of troponin C-extracted vertebrate striated fast-twitch muscle fibers

FEBS Letters ◽  
1986 ◽  
Vol 203 (1) ◽  
pp. 20-24 ◽  
Author(s):  
Aravind Babu ◽  
Suzanne Pemrick ◽  
Jagdish Gulati
Keyword(s):  
Muscle Fibers ◽  
Troponin C ◽  
Fast Twitch Muscle ◽  
Fast Twitch

scholarly journals Size and Proportions of Slow-Twitch and Fast-Twitch Muscle Fibers in Human Costal Diaphragm

2016 ◽  
Vol 2016 ◽  
pp. 1-6 ◽  
Author(s):  
Marija Meznaric ◽  
Erika Cvetko
Keyword(s):  
Vastus Lateralis ◽  
Muscle Fibers ◽  
Hybrid Fibers ◽  
Cross Sectional ◽  
Myosin Heavy Chain Isoform ◽  
Diaphragmatic Muscle ◽  
Fast Twitch Muscle ◽  
The Mean ◽  
Slow Twitch ◽  
Fast Twitch

Smaller diaphragmatic motor unit potentials (MUPs) compared to MUPs of limb muscles lead to the hypothesis that diaphragmatic muscle fibers, being the generators of MUPs, might be also smaller. We compared autopsy samples of costal diaphragm and vastus lateralis of healthy men with respect to fibers’ size and expression of slow myosin heavy chain isoform (MyHC-1) and fast 2A isoform (MyHC-2A). Diaphragmatic fibers were smaller than fibers in vastus lateralis with regard to the mean minimal fiber diameter of slow-twitch (46.8 versus 72.2 μm,p<0.001), fast-twitch (45.1 versus 62.4 μm,p<0.001), and hybrid fibers (47.3 versus 65.0 μm,p<0.01) as well as to the mean fiber cross-sectional areas of slow-twitch (2376.0 versus 5455.9 μm2,p<0.001), fast-twitch (2258.7 versus 4189.7 μm2,p<0.001), and hybrid fibers (2404.4 versus 4776.3 μm2,p<0.01). The numerical proportion of slow-twitch fibers was higher (50.2 versus 36.3%,p<0.01) in costal diaphragm and the numerical proportion of fast-twitch fibers (47.2 versus 58.7%,p<0.01) was lower. The numerical proportion of hybrid fibers did not differ. Muscle fibers of costal diaphragm have specific characteristics which support increased resistance of diaphragm to fatigue.

Prolonged contraction-relaxation cycle of fast-twitch muscles in parvalbumin knockout mice

1999 ◽  
Vol 276 (2) ◽  
pp. C395-C403 ◽  
Author(s):  
B. Schwaller ◽  
J. Dick ◽  
G. Dhoot ◽  
S. Carroll ◽  
G. Vrbova ◽  
...  
Keyword(s):  
Knockout Mice ◽  
Calcium Binding ◽  
Muscle Fibers ◽  
Relaxation Cycle ◽  
Single Twitch ◽  
Intracellular Ca ◽  
Fast Twitch Muscle ◽  
High Concentrations ◽  
Time Required ◽  
Fast Twitch

The calcium-binding protein parvalbumin (PV) occurs at high concentrations in fast-contracting vertebrate muscle fibers. Its putative role in facilitating the rapid relaxation of mammalian fast-twitch muscle fibers by acting as a temporary buffer for Ca2+ is still controversial. We generated knockout mice for PV (PV −/−) and compared the Ca2+ transients and the dynamics of contraction of their muscles with those from heterozygous (PV +/−) and wild-type (WT) mice. In the muscles of PV-deficient mice, the decay of intracellular Ca2+ concentration ([Ca2+]i) after 20-ms stimulation was slower compared with WT mice and led to a prolongation of the time required to attain peak twitch tension and to an extension of the half-relaxation time. The integral [Ca2+]iin muscle fibers of PV −/− mice was higher and consequently the force generated during a single twitch was ∼40% greater than in PV +/− and WT animals. Acceleration of the contraction-relaxation cycle of fast-twitch muscle fibers by PV may confer an advantage in the performance of rapid, phasic movements.

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