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.

scholarly journals Deficiency in parvalbumin increases fatigue resistance in fast-twitch muscle and upregulates mitochondria

2001 ◽  
Vol 281 (1) ◽  
pp. C114-C122 ◽  
Author(s):  
Gaoping Chen ◽  
Stefanie Carroll ◽  
Peter Racay ◽  
Jim Dick ◽  
Dirk Pette ◽  
...  
Keyword(s):  
Fatigue Resistance ◽  
Binding Protein ◽  
Muscle Relaxation ◽  
Physiological Role ◽  
Capillary Density ◽  
Tetanic Contraction ◽  
Relaxation Cycle ◽  
Intracellular Ca ◽  
Fast Twitch Muscle ◽  
Fast Twitch

The soluble Ca2+-binding protein parvalbumin (PV) is expressed at high levels in fast-twitch muscles of mice. Deficiency of PV in knockout mice (PV −/−) slows down the speed of twitch relaxation, while maximum force generated during tetanic contraction is unaltered. We observed that PV-deficient fast-twitch muscles were significantly more resistant to fatigue than were the wild type. Thus components involved in Ca2+ homeostasis during the contraction-relaxation cycle were analyzed. No upregulation of another cytosolic Ca2+-binding protein was found. Mitochondria are thought to play a physiological role during muscle relaxation and were thus analyzed. The fractional volume of mitochondria in the fast-twitch muscle extensor digitorum longus (EDL) was almost doubled in PV −/− mice, and this was reflected in an increase of cytochrome coxidase. A faster removal of intracellular Ca2+concentration ([Ca2+]i) 200–700 ms after fast-twitch muscle stimulation observed in PV −/− muscles supports the role for mitochondria in late [Ca2+]iremoval. The present results also show a significant increase of the density of capillaries in EDL muscles of PV −/− mice. Thus alterations in the dynamics of Ca2+ transients detected in fast-twitch muscles of PV −/− mice might be linked to the increase in mitochondria volume and capillary density, which contribute to the greater fatigue resistance of these muscles.

Calmitine: A calcium-binding mitochondrial protein specific for fast-twitch muscle fibers

1990 ◽  
Vol 115 (1) ◽  
pp. 103-107 ◽  
Author(s):  
Brigitte Lucas-Heron ◽  
Nelly Schmitt ◽  
Béatrice Ollivier
Keyword(s):  
Calcium Binding ◽  
Muscle Fibers ◽  
Mitochondrial Protein ◽  
Fast Twitch Muscle ◽  
Fast Twitch

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.

Increased susceptibility to fatigue of slow- and fast-twitch muscles from mice lacking the MG29 gene

2000 ◽  
Vol 4 (1) ◽  
pp. 43-49 ◽  
Author(s):  
RAMAKRISHNAN Y. NAGARAJ ◽  
CHRISTOPHER M. NOSEK ◽  
MARCO A. P. BROTTO ◽  
MIYUKI NISHI ◽  
HIROSHI TAKESHIMA ◽  
...  
Keyword(s):  
Major Protein ◽  
Force Frequency ◽  
Wild Type ◽  
Membrane Structures ◽  
Intracellular Ca ◽  
Slow Twitch Muscle ◽  
Fast Twitch Muscle ◽  
Frequency Relationship ◽  
Fast Twitch

Mitsugumin 29 (MG29), a major protein component of the triad junction in skeletal muscle, has been identified to play roles in the formation of precise junctional membrane structures important for efficient signal conversion in excitation-contraction (E-C) coupling. We carried out several experiments to not only study the role of MG29 in normal muscle contraction but also to determine its role in muscle fatigue. We compared the in vitro contractile properties of three muscles types, extensor digitorum longus (EDL) (fast-twitch muscle), soleus (SOL) (slow-twitch muscle), and diaphragm (DPH) (mixed-fiber muscle), isolated from mice lacking the MG29 gene and wild-type mice prior to and after fatigue. Our results indicate that the mutant EDL and SOL muscles, but not DPH, are more susceptible to fatigue than the wild-type muscles. The mutant muscles not only fatigued to a greater extent but also recovered significantly less than the wild-type muscles. Following fatigue, the mutant EDL and SOL muscles produced lower twitch forces than the wild-type muscles; in addition, fatiguing produced a downward shift in the force-frequency relationship in the mutant mice compared with the wild-type controls. Our results indicate that fatiguing affects the E-C components of the mutant EDL and SOL muscles, and the effect of fatigue in these mutant muscles could be primarily due to an alteration in the intracellular Ca homeostasis.

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.

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