scholarly journals The effects of thimerosal on calcium uptake and inositol 1,4,5-trisphosphate-induced calcium release in cerebellar microsomes

1993 ◽  
Vol 289 (3) ◽  
pp. 883-887 ◽  
Author(s):  
L G Sayers ◽  
G R Brown ◽  
R H Michell ◽  
F Michelangeli
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Calcium Uptake ◽  
Calcium Release ◽  
Hill Coefficient ◽  
Cysteine Residues ◽  
Experimental Conditions ◽  
Inositol 1,4,5 Trisphosphate ◽  
Insp3 Receptor

Thimerosal inhibits calcium uptake in skeletal muscle sarcoplasmic reticulum and rat cerebellar microsomes by inhibiting the Ca(2+)-ATPase. In the presence of 5 mM dithiothreitol (DTT), Ca2+ uptake and ATPase activity were not inhibited by thimerosal, indicating that thimerosal modifies cysteine residues of the Ca(2+)-ATPase. Low thimerosal concentrations (2 microM) sensitize the inositol 1,4,5-trisphosphate (InsP3)-sensitive Ca2+ channel, making it open at lower InsP3 concentrations. Higher concentrations of thimerosal, however, cause inhibition of InsP3-induced Ca2+ release. Both sensitization and inhibition of the InsP3 receptor by thimerosal can be prevented by DTT. The binding and metabolism of InsP3 by cerebellar microsomes is not affected by thimerosal. The amount of InsP3-induced Ca2+ release is co-operatively linked to the InsP3 concentration with a Hill coefficient of 2.0 +/- 0.3. This is decreased to 1.0 +/- 0.2 at inhibitory concentrations of thimerosal. Under our experimental conditions, we observed no dependence of quantal Ca2+ release on intraluminal Ca2+ concentration.

scholarly journals Inhibitors of Calmodulin-Dependent Phosphorylation Simultaneously Inhibit Calcium Uptake and Calcium-Dependent ATPase Activity in Skeletal Muscle Sarcoplasmic Reticulum and Transiently Induce Calcium Release

1984 ◽  
Vol 39 (11-12) ◽  
pp. 1189-1191 ◽  
Author(s):  
Wilhelm Hasselbach
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Uptake ◽  
Calcium Release ◽  
Atp Hydrolysis ◽  
Calmodulin Antagonists ◽  
Experimental Conditions ◽  
Calcium Dependent ◽  
Inhibiting Effect ◽  
Hydrolysis Of

Keywords Under adequate experimental conditions calmodulin antagonists like compound 48/80 do not dissociate calcium uptake from the calcium -dependent ATP hydrolysis of skeletal muscle sarcoplasmic reticulum membranes but simultaneously inhibit both processes. Apart from the agent’s pump inhibiting effect, they interact with the caffeine sensitive calcium channel in the sarcoplasmic reticulum causing a rapid transient calcium release.

The Modulation of the Calcium Transport by Skeletal Muscle Sarcoplasmic Reticulum in the Hibernating European Hamster

1991 ◽  
Vol 46 (11-12) ◽  
pp. 1109-1126 ◽  
Author(s):  
◽  
Luisa De Martino ◽  
Barbara Soltau ◽  
Wilhelm Hasselbach
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Transport ◽  
Calcium Uptake ◽  
Calcium Release ◽  
Ion Homeostasis ◽  
Free Calcium ◽  
Type I ◽  
Calcium Dependent ◽  
Calcium Affinity

Calcium transport of skeletal muscle sarcoplasmic reticulum was comparatively studied in hibernating and summer active European hamsters (Cricetus cricetus L.). Crude homogenates from psoas, soleus and mixed skeletal muscles were used. Protein yield was strongly reduced in the muscle homogenates of hibernating hamsters. The calcium concentration in the muscle of hibernating hamsters was increased to a much higher content than in the serum. In the same animals the maximal rate of calcium uptake and the calcium storing capacity of sarcoplasmic reticulum were augmented by 43% and respectively 17%. Kinetic experiments with various concentrations of free calcium revealed in the hibernating animals higher uptake rates and a lower apparent calcium affinity than in the summer active hamsters. Some shift of calcium uptake rate and calcium affinity similar to that of a fast-twitch muscle was also observed in winter active animals kept at 22 C under natural photoperiod. By contrast, the activity of the calcium dependent ATPase was not increased, suggesting a tighter coupling during hibernation between calcium dependent ATP-hydrolysis and calcium transport. No seasonal difference was observed in the calcium release by KCl-caffeine from calcium loaded vesicles of sarcoplasmic reticulum.Proportion and size of fibre types were studied with cold cross sections from psoas and soleus muscles. An average atrophy of about 25% was found during hibernation in both muscles. Cytochemistry revealed, however, a different reduction of cross area between type-I- and type-11-fibres, which reaches values up to 46% in the type-I I-fast-fibres of the slow soleus muscle. Electron microscopy did not show any definite change in the distribution and amount of sarcoplasmic reticulum.The results suggest that during hibernation a modulation in the properties of calcium transport ATPase of sarcoplasmic reticulum occurs to better support the calcium transport function at low temperatures, which in turn warrants the restoration of ion homeostasis in the course of the arousal.

Effects of diltiazem or verapamil on calcium uptake and release from chicken skeletal muscle sarcoplasmic reticulum

2005 ◽  
Vol 83 (11) ◽  
pp. 967-975 ◽  
Author(s):  
Mehrak Javadi Paydar ◽  
Abbas Pousti ◽  
Hasan Farsam ◽  
Massoud Amanlou ◽  
Shahram Ejtemaei Mehr ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Release Rate ◽  
Calcium Release ◽  
Inhibitory Effect ◽  
Channel Blockers ◽  
Uptake Inhibition ◽  
Drug Dependent ◽  
Chicken Skeletal Muscle

The purpose of this study was to determine the effects of 2 Ca2+ channel blockers, verapamil and diltiazem, on calcium loading (active Ca2+ uptake) and the following Ca2+ release induced by silver ion (Ag+) and Ca2+ from the membrane of heavy sarcoplasmic reticulum (SR) of chicken skeletal muscle. A fluorescent probe technique was employed to determine the calcium movement through the SR. Pretreatment of the medium with diltiazem and verapamil resulted in a significant decrease in the active Ca2+ uptake, with IC50 of about 290 µmol/L for verapamil and 260 µmol/L for diltiazem. Inhibition of Ca2+ uptake was not due to the development of a substantial drug-dependent leak of Ca2+ from the SR. It might, in part, have been mediated by a direct inhibitory effect of these drugs on the Ca2+ ATPase activity of the SR Ca2+ pump. We confirmed that Ca2+ channel blockers, administered after SR Ca2+ loading and before induction of Ca2+ release, caused a dose-dependent inhibition of both Ca2+- and Ag+-induced Ca2+ release rate. Moreover, if Ca2+ channel blockers were administered prior to SR Ca2+ loading, in spite of Ca2+ uptake inhibition the same reduction in Ca2+- and Ag+-induced Ca2+ release rate was seen. We showed that the inhibition of Ag+-induced Ca2+ release by L-channel blockers is more sensitive than Ca2+-induced Ca2+ release inhibition, so the IC50 for Ag+- and Ca2+-induced Ca2+ release was about 100 and 310 µmol/L for verapamil and 79 and 330 µmol/L for diltiazem, respectively. Our results support the evidence that Ca2+ channel blockers affect muscle microsome of chicken skeletal muscle by 2 independent mechanisms: first, reduction of Ca2+ uptake rate and Ca2+-ATPase activity inhibition, and second, inhibition of both Ag+- and Ca2+-induced Ca2+ release by Ca2+ release channels. These findings confirm the direct effect of Ca2+ channel blockers on calcium release channels. Our results suggest that even if the SR is incompletely preloaded with Ca2+ because of inhibition of Ca2+ uptake by verapamil and diltiazem, no impairment in Ca2+ release occurs. Key words: calcium, sarcoplasmic reticulum, diltiazem, verapamil, chicken, skeletal muscle.

Inositol 1,4,5-trisphosphate induces calcium release from sarcoplasmic reticulum of skeletal muscle

Nature ◽  
1985 ◽  
Vol 316 (6026) ◽  
pp. 347-349 ◽  
Author(s):  
Pompeo Volpe ◽  
Giovanni Salviati ◽  
Francesco Di Virgilio ◽  
Tullio Pozzan
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Release ◽  
Inositol 1,4,5 Trisphosphate

Abnormal sarcoplasmic reticulum Ca2+-sequestering properties in skeletal muscle in chronic obstructive pulmonary disease

2008 ◽  
Vol 295 (2) ◽  
pp. C350-C357 ◽  
Author(s):  
H. J. Green ◽  
M. Burnett ◽  
T. A. Duhamel ◽  
C. D'Arsigny ◽  
D. E. O'Donnell ◽  
...  
Keyword(s):  
Chronic Obstructive Pulmonary Disease ◽  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Pulmonary Disease ◽  
Hill Coefficient ◽  
Chronic Obstructive ◽  
Maximal Velocity ◽  
Obstructive Pulmonary Disease ◽  
Wide Range

The objective of this study was to investigate the hypothesis that alterations in sarcoplasmic reticulum (SR) Ca2+-cycling properties would occur in skeletal muscle in patients with moderate to severe chronic obstructive pulmonary disease (COPD). To investigate this hypothesis, tissue samples were obtained from the vastus lateralis of 8 patients with COPD [age 65.6 ± 3.2 yr; forced expiratory volume in 1 s (FEV1)/forced vital capacity (FVC) = 44 ± 2%; mean ± SE] and 10 healthy age-matched controls (CON, age 67.5 ± 2.5 yr; FEV1/FVC = 77 ± 2%), and homogenates were analyzed for a wide range of SR properties. Compared with CON, COPD displayed (in μmol·g protein−1·min−1) a 16% lower maximal Ca2+-ATPase activity [maximal velocity ( Vmax), 158 ± 10 vs. 133 ± 7, P < 0.05] and a 17% lower Ca2+uptake (4.65 ± 0.039 vs. 3.85 ± 0.26, P < 0.05) that occurred in the absence of differences in Ca2+release. The lower Vmaxin COPD was also accompanied by an 11% lower ( P < 0.05) Ca2+sensitivity, as measured by the Hill coefficient (defined as the relationship between Ca2+-ATPase activity and free cytosolic Ca2+concentration for 10–90% Vmax). For the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) isoforms, SERCA1a was 16% higher ( P < 0.05) and SERCA2a was 14% lower ( P < 0.05) in COPD. It is concluded that moderate to severe COPD results in abnormalities in SR Ca2+-ATPase properties that cannot be explained by changes in the SERCA isoform phenotypes. The reduced catalytic properties of SERCA in COPD suggest a disturbance in Ca2+cycling, possibly resulting in impairment in Ca2+-mediated mechanical function and/or second messenger regulated processes.

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