scholarly journals Effect of Dietary Nitrate on Force Production and Sarcoplasmic Reticulum Ca<sup>2+</sup> Handling in Rat Fast-Twitch Muscles Following Eccentric Contraction

2018 ◽  
Vol 08 (12) ◽  
pp. 607-618 ◽  
Author(s):  
Satoshi Matsunaga ◽  
Chihiro Aibara ◽  
Daiki Watanabe ◽  
Keita Kanzaki ◽  
Yurie Morizaki ◽  
...  
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Force Production ◽  
Eccentric Contraction ◽  
Dietary Nitrate ◽  
Fast Twitch

Role of calpain in eccentric contraction-induced proteolysis of Ca2+-regulatory proteins and force depression in rat fast-twitch skeletal muscle

2017 ◽  
Vol 122 (2) ◽  
pp. 396-405 ◽  
Author(s):  
Keita Kanzaki ◽  
Daiki Watanabe ◽  
Mai Kuratani ◽  
Takashi Yamada ◽  
Satoshi Matsunaga ◽  
...  
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Ryanodine Receptor ◽  
Force Production ◽  
Eccentric Contraction ◽  
Dihydropyridine Receptor ◽  
Regulatory Proteins ◽  
Calpain Inhibitor ◽  
Contributing Factors ◽  
Fast Twitch

The aim of this study was to examine the in vivo effects of eccentric contraction (ECC) on calpain-dependent proteolysis of Ca2+-regulatory proteins and force production in fast-twitch skeletal muscles. Rat extensor digitorum longus muscles were exposed to 200 repeated ECC in situ and excised immediately [recovery 0 (REC0)] or 3 days [recovery 3 (REC3)] after cessation of ECC. Calpain inhibitor (CI)-treated rats were intraperitoneally injected with MDL-28170 before ECC and during REC3. Tetanic force was markedly reduced at REC0 and remained reduced at REC3. CI treatment ameliorated the ECC-induced force decline but only at REC3. No evidence was found for proteolysis of dihydropyridine receptor (DHPR), junctophilin (JP)1, JP2, ryanodine receptor (RyR), sarcoplasmic reticulum Ca2+-ATPase (SERCA)1a, or junctional face protein-45 at REC0. At REC3, ECC resulted in decreases in DHPR, JP1, JP2, RyR, and SERCA1a. CI treatment prevented the decreases in DHPR, JP1, and JP2, whereas it had little effect on RyR and SERCA1a. These findings suggest that DHPR, JP1, and JP2, but not RyR and SERCA1a, undergo calpain-dependent proteolysis in in vivo muscles subjected to ECC and that impaired function of DHPR and/or JP might cause prolonged force deficits with ECC. NEW & NOTEWORTHY Calpain-dependent proteolysis is one of the contributing factors to muscle damage that occurs with eccentric contraction (ECC). It is unclear, however, whether calpains account for proteolysis of Ca2+-regulatory proteins in in vivo muscles subjected to ECC. Here, we provide evidence that dihydropyridine receptor and junctophilin, but not ryanodine receptor and sarcoplasmic reticulum Ca2+-ATPase, undergo calpain-dependent proteolysis.

Calcium activation of sarcoplasmic reticulum ATPase following strenuous activity

1981 ◽  
Vol 59 (12) ◽  
pp. 1214-1218 ◽  
Author(s):  
A. N. Belcastro ◽  
M. Rossiter ◽  
M. P. Low ◽  
M. M. Sopper
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Wistar Rats ◽  
Force Production ◽  
Tetraacetic Acid ◽  
Strenuous Activity ◽  
Significant Difference ◽  
Significant Depression ◽  
Gastrocnemius Muscles ◽  
Fast Twitch

The purpose of this study was to examine the effects of varying Ca2+ concentration on the Ca2+ activated sarcoplasmic reticulum (SR) ATPase activity of fast-twitch (FT) skeletal muscle at exhaustion and during recovery. Wistar rats (200 g) were assigned to control (C), exhausted (E), and three recovery groups (R) at 5, 15, and 30 min. Following exhaustion on a motor-driven treadmill, the gastrocnemius muscles from all groups were excised and frozen. Muscle samples were assayed for ATPase activity in a Ca2+ – ethyleneglycol bis (β-aminoethyl ether)-N,N′-tetraacetic acid (EGTA) buffering system. At 1.25 μM Ca2+, a significant depression in Ca2+ activated ATPase activity occurred in the E, 5R, 15R, and 30R groups (1.61 ± 0.17, 1.87 ± 0.14, 1.43 ± 0.29, and 1.62 ± 0.1 μmol Pi∙mg−1∙10 min−1) compared with C values (2.41 ± 0.34 μmol Pi∙mg−1∙10 min−1) (p ≤ 0.05). At 5.0 μM, Ca2+ activated ATPase activity remained depressed in the E, 5R, and 15R groups compared with C and 30R groups (p ≤ 0.05). At 0.75 μM Ca2+, there was no significant difference between groups (p ≥ 0.05). The results suggest that Ca2+ activated SR ATPase activity of fatigued FT muscle may contribute to the decreased force production at exhaustion.

Skeletal muscle overload upregulates the sarcoplasmic reticulum slow calcium pump gene

1994 ◽  
Vol 266 (5) ◽  
pp. C1190-C1197 ◽  
Author(s):  
S. C. Kandarian ◽  
D. G. Peters ◽  
J. A. Taylor ◽  
J. H. Williams
Keyword(s):  
Skeletal Muscle ◽  
Monoclonal Antibody ◽  
Sarcoplasmic Reticulum ◽  
Cdna Probe ◽  
Force Production ◽  
Surgical Removal ◽  
Muscle Loading ◽  
Protein Isoform ◽  
Fast Twitch ◽  
Kinetics Of

Functional data suggest that the kinetics of force production and relaxation are slowed in hypertrophied skeletal muscle because of chronic overload. The purpose of this study was to determine whether gene expression of the slow/cardiac isoform of the sarcoplasmic reticulum (SR) Ca(2+)-adenosinetriphosphatase (ATPase) pump is upregulated in overloaded fast-twitch plantaris muscles. Increased active muscle loading was induced in rat plantaris muscles bilaterally by surgical removal of gastrocnemius and soleus muscles. Mass of the plantaris muscle was 80% greater 5 wk after surgery than in age-matched unoperated control rats (P < 0.05). Expression of the slow pump mRNA was 135% greater in hypertrophied muscles, as determined from autoradiograms of Northern blots with use of a cDNA probe specific for the slow/cardiac isoform. A monoclonal antibody (7E6) was used to quantify slow Ca2+ pump in SR vesicles with use of Western blot analysis. Densitometry of blots showed that the relative expression of the slow pump protein was 130% greater in hypertrophied plantaris muscles. Expression of the fast SR Ca2+ pump protein isoform, assessed using monoclonal antibody A52, was 25% less in hypertrophied than in control muscles. The Ca2+ uptake rate and ATPase activity of SR vesicles was approximately 15% lower in hypertrophied plantaris muscles (P < 0.05). Differential phospholamban expression could not account for changes in SR Ca2+ handling, because it could not be detected in rat slow- or fast-twitch skeletal muscle.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Evidence for membrane microheterogeneity in the sarcoplasmic reticulum of fast twitch skeletal muscle.

1982 ◽  
Vol 257 (19) ◽  
pp. 11689-11695
Author(s):  
W B Van Winkle ◽  
R J Bick ◽  
D E Tucker ◽  
C A Tate ◽  
M L Entman
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Fast Twitch ◽  
Membrane Microheterogeneity

Loss of α-actinin-3 confers protection from eccentric contraction damage in fast-twitch EDL muscles from aged mdx dystrophic mice by reducing pathological fibre branching

2021 ◽  
Author(s):  
Leonit Kiriaev ◽  
Peter J. Houweling ◽  
Kathryn N. North ◽  
Stewart I. Head
Keyword(s):  
Morphological Changes ◽  
Eccentric Contraction ◽  
Muscle Fibres ◽  
Double Knockout ◽  
Reduction In Force ◽  
The Common ◽  
Fast Twitch ◽  
Skeletal Muscle Fibres ◽  
Dystrophic Mice

ABSTRACTThe common null polymorphism (R577X) in the ACTN3 gene is present in over 1.5 billion people worldwide and results in the absence of the protein α-actinin-3 from the Z-discs of fast-twitch skeletal muscle fibres. We have previously reported that this polymorphism is a modifier of dystrophin deficient Duchenne Muscular Dystrophy. To investigate the mechanism underlying this we use a double knockout (dk)Actn3KO/mdx (dKO) mouse model which lacks both dystrophin and sarcomere α-actinin-3. We used dKO mice and mdx dystrophic mice at 12 months (aged) to investigate the correlation between morphological changes to the fast-twitch dKO EDL and the reduction in force deficit produced by an in vitro eccentric contraction protocol. In the aged dKO mouse we found a marked reduction in fibre branching complexity that correlated with protection from eccentric contraction induced force deficit. Complex branches in the aged dKO EDL fibres (28%) were substantially reduced compared to aged mdx EDL fibres (68%) and this correlates with a graded force loss over three eccentric contractions for dKO muscles (∼35% after first contraction, ∼66% overall) compared to an abrupt drop in mdx upon the first eccentric contraction (∼73% after first contraction, ∼89% after three contractions). In dKO protection from eccentric contraction damage was linked with a doubling of SERCA1 pump density the EDL. We propose that the increased oxidative metabolism of fast-twitch glycolytic fibres characteristic of the null polymorphism (R577X) and increase in SR Ca2+ pump proteins reduces muscle fibre branching and decreases susceptibility to eccentric injury in the dystrophinopathies.

Repeated force production and metabolites in two medial gastrocnemius muscle compartments of the rat

1995 ◽  
Vol 79 (6) ◽  
pp. 1855-1861 ◽  
Author(s):  
C. J. De Ruiter ◽  
A. De Haan ◽  
A. J. Sargeant
Keyword(s):  
Blood Flow ◽  
Motor Nerve ◽  
Force Production ◽  
Oxidative Capacity ◽  
Medial Gastrocnemius ◽  
Train Duration ◽  
Functional Consequences ◽  
Force Recovery ◽  
The Difference ◽  
Fast Twitch

The most proximal and distal motor nerve branches in the rat medial gastrocnemius innervate discrete muscle compartments dominated by fast-twitch oxidative and fast-twitch glycolytic fibers, respectively. The functional consequences of the difference in oxidative capacity between these compartments were investigated. Wistar rats were anesthetized with pentobarbital sodium (90 mg/kg ip). Changes in force of both compartments during 21 isometric contractions (train duration 200 ms, stimulation frequency 120 Hz, 3 s between contractions) were studied in situ with and without blood flow. Without blood flow, force and phosphocreatine declined to a greater extent in the proximal than the distal compartment compared with the run with intact flow. After the protocol without blood flow, when flow was restored, the time constants for force recovery (which were closely associated to the recovery of phosphocreatine) were 37 +/- 7 (SD) (proximal compartment) and 148 +/- 20 s (distal compartment). It was concluded that the proximal compartment had a four times higher oxidative capacity and, therefore, a superior ability for repeated force production.

Expression of sarcoplasmic reticulum Ca(2+)-ATPase isoforms in marlin and swordfish muscle and heater cells

1996 ◽  
Vol 271 (1) ◽  
pp. R262-R275 ◽  
Author(s):  
A. Tullis ◽  
B. A. Block
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Fiber Type ◽  
Direct Sequencing ◽  
Rectus Muscle ◽  
Superior Rectus ◽  
Cardiac Muscles ◽  
Slow Twitch ◽  
Fast Twitch ◽  
Sarcoplasmic Reticulum Calcium ◽  
Superior Rectus Muscle

The superior rectus muscles of marlin, swordfish, sailfish, and spearfish are modified for generating heat rather than force. This study focuses on the sarcoplasmic reticulum calcium-adenosinetriphosphatase (SR Ca(2+)-ATPase) to gain further insight into the muscle fiber type origin of the billfish “heater cell.” Direct sequencing and immunolocalization demonstrated that marlin and swordfish epaxial swimming muscles express two forms of the SR Ca(2+)-ATPase in a fiber type-specific manner; red slow-twitch skeletal and cardiac muscles express the same SERCA2 message, whereas white fast-twitch skeletal muscles express a SERCA1 message. Thus the expression pattern of the SR Ca2+ pump is similar in both billfish and tetrapod muscles. Molecular and immunological studies revealed that billfish heater tissue and superior rectus muscle express both fast and slow SR Ca2+ pump isoforms. Immunohistochemical results suggest that heater cells and most extraocular muscle fibers express the fast SR Ca2+ pump. Expression of the fast SR Ca(2+)-ATPase by heater cells has implications for heater cell origin and thermogenic control.

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