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.

On the Problem of Season and Cold Dependence of Calcium Transport by Skeletal Muscle Sarcoplasmic Reticulum

1990 ◽  
Vol 45 (6) ◽  
pp. 671-675 ◽  
Author(s):  
Bruno Agostini ◽  
Luisa De Martino ◽  
Wilhelm Hasselbach
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Cold Acclimation ◽  
Uptake Rate ◽  
Calcium Transport ◽  
Calcium Uptake ◽  
Kinetic Studies ◽  
Cold Season ◽  
Free Calcium ◽  
Calcium Affinity

Abstract Calcium transport of skeletal muscle sarcoplasmic reticulum from golden hamsters was studied in January and in June on animals kept at 22 °C under natural photoperiod and in January after cold-acclimation at ±2 °C in the dark for 55 days. Crude homogenates from psoas and soleus muscles and from mixed skeletal muscles were used. No differences were observed in the calcium storing capacity of sarcoplasmic reticulum among the three groups of animals. Kinetic studies on the dependence of the calcium uptake rate on the concentration of free calcium revealed a significant increase of the uptake rates and a decrease of the calcium affinity in the control animals sacrificed in winter as compared to those killed in June. Cold-acclimation in winter leads to a further small reduction of the calcium affinity. This shift of calcium uptake rate and affinity in the sense of that of a fast-twitch muscle may be related to the functional demands of the cold season and cold-acclimation respectively.

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.

Calcium-dependent halothane activation of sarcoplasmic reticulum calcium channels from frog skeletal muscle

1994 ◽  
Vol 266 (2) ◽  
pp. C391-C396 ◽  
Author(s):  
R. Bull ◽  
J. J. Marengo
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Channels ◽  
Lipid Bilayers ◽  
Single Channel ◽  
Free Calcium ◽  
Frog Skeletal Muscle ◽  
Time Constants ◽  
Calcium Dependent ◽  
Open Time

The effect of halothane on calcium channels present in sarcoplasmic reticulum membranes isolated from frog skeletal muscle was studied at the single channel level after fusing the isolated vesicles into planar lipid bilayers. Addition of 91 microM halothane to the cytosolic compartment containing 1 microM free calcium activated the channel by increasing fractional open time from 0.11 to 0.59, without changing the channel conductance. The activation of the channels by halothane was calcium dependent. At resting calcium concentrations in the cytosolic compartment, halothane failed to activate the channel, whereas maximal activation was found at 10 microM calcium. The free energy of halothane binding to the channel decreased from -5.8 kcal/mol at 1 microM calcium to -6.6 kcal/mol at 10 microM calcium. Halothane increased the open time constants and decreased the closed time constants, indicating that it binds to both the open and the closed configurations of the channel.

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.

Tryptic Fragmentation of the Calcium Transport System in the Sarcoplasmic Reticulum

1973 ◽  
Vol 28 (3-4) ◽  
pp. 178-182 ◽  
Author(s):  
A. Migala ◽  
B. Agostini ◽  
W. Hasselbach
Keyword(s):  
Molecular Weight ◽  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Calcium Transport ◽  
Smooth Surface ◽  
Calcium Uptake ◽  
Surface Structures ◽  
Transport Atpase ◽  
Protein Fragments ◽  
Calcium Dependent

Two protein fragments with a molecular weight of 50-60 000 daltons are formed when the calcium transport ATPase of the SR is mildly digested with trypsin. The initial fragmentation of the ATPase does not interfere with calcium transport, calcium dependent ATPase activity and phosphoprotein formation. The decay of the initially formed protein fragments after prolonged tryptic digestion is accompanied by the decline of the rate of calcium uptake and the calcium concentrating ability while the activity of the calcium activated ATPase is reduced only moderately. The initial tryptic fragmentation does not give rise to any change in the morphological appearance in the SR membranes. After prolonged digestion brush border or smooth surface structures are observed depending on the agent used for negative staining.

Alteration of Acylphosphate Formation of Cardiac Sarcoplasmic Reticulum ATPase by Calmodulin-Dependent Phosphorylation

1984 ◽  
Vol 39 (3-4) ◽  
pp. 289-292 ◽  
Author(s):  
Christian Pifl ◽  
Brigitte Plank ◽  
Gertrude Hellmann ◽  
Wolfgang Wyskovsky ◽  
Josef Suko
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Calcium Transport ◽  
State Level ◽  
Hill Coefficient ◽  
Free Calcium ◽  
Sr Protein ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Transport Atpase ◽  
Calcium Dependent ◽  
Calcium Calmodulin Dependent

The calcium-dependent acylphosphate formed by the calcium transport ATPase of cardiac sarcoplasmic reticulum and the calcium-, calm odulin-dependent phosphoester(s) of sarcoplasmic reticulum fractions formed by a calcium-, calmodulin-dependent membrane-bound protein kinase can be distinguished by removal of calcium and/or magnesium by EDTA or hydroxylamine treatment of the acid denaturated membranes. Both procedures decompose the acylphosphate with little effect on the phosphoester(s). Calmodulin-dependent phosphorylation (2.44 nmol/mg SR protein) reduces the apparent K(Ca) of the acylphosphate steady state level of the calcium transport ATPase from 0.56 to 0.34 μM free calcium, without affecting the maximum phosphoenzyme level (0.93 versus 0.89 nmol/mg protein), and has little, if any, effect on the Hill-coefficient (1.32 versus 1.54)

Sarcoplasmic reticulum Ca2+ transport and long chain acylcarnitines in hyperthyroidism

1988 ◽  
Vol 66 (2) ◽  
pp. 159-165 ◽  
Author(s):  
Shawn C. Black ◽  
John H. McNeill ◽  
Sidney Katz
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Calcium Transport ◽  
Wistar Rats ◽  
Free Calcium ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Calcium Dependent ◽  
Endogenous Level ◽  
Male Wistar Rats ◽  
Carnitine Derivatives ◽  
Long Chain

Male Wistar rats were treated with L-3,5,3′-triiodothyronine (T3) (500 μg∙kg∙−1∙day−1) for 3 days. Cardiac sarcoplasmic reticulum (SR) was isolated at several time points during the induction of the hyperthyroid state and calcium transport and the levels of carnitine derivatives were determined. Calcium transport was augmented at all free calcium concentrations assayed (0.1–5.3 μM) 24 h following a single dose of T3; at 48 and 72 h, calcium transport was further augmented. Calcium-dependent phosphoprotein levels were increased in the SR of the 48- and 72-h T3-treated groups. Total SR carnitine was reduced after 24, 48, and 72 h of treatment. Long chain acylcarnitine (LCAC) levels were decreased in T3-treated SR at 48 and 72 h. This study shows that calcium transport is increased in T3-treated rat heart SR and that this increase may be related to a reduction in the endogenous level of LCAC in the SR membrane.

Competition between Oxalate and Phosphate during Active Calcium Accumulation by Sarcoplasmic Vesicles

1977 ◽  
Vol 32 (3-4) ◽  
pp. 281-287 ◽  
Author(s):  
Frank-Ulrich Beil ◽  
Dorothee von Chak ◽  
Wilhelm Hasselbach ◽  
Hans-Hermann Weber
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Calcium Binding ◽  
Calcium Transport ◽  
Calcium Uptake ◽  
Phosphate Uptake ◽  
Mutual Exclusion ◽  
Calcium Dependent ◽  
Uptake Activity ◽  
Active Calcium ◽  
Narrow Concentration Range

Abstract Sarcoplasmic Calcium Uptake, Oxalate and Phosphate Uptake, Oxalate-Phosphate Competition, Calcium Turnover 1. During ATP supported active calcium uptake oxalate as well as phosphate are accumulated with calcium. The uptake of calcium exceeds that of both anions by a small quantity - accounting for calcium binding to vesicular proteins and lipids. 2. From assay media containing phosphate and oxalate - nearly exclusively either oxalate or phosphate are taken up together with calcium by the sarcoplasmic reticulum vesicles. The mutual exclusion occurs in a very narrow concentration range of the anions. 3. In solutions containing phosphate and oxalate, calcium phosphate or calcium oxalate pre­ cipitates are formed according to their solubility properties. 4. When phosphate prevents oxalate from being taken up, calcium transport is inhibited. In­ hibition occurs, because the concentration of ionized calcium inside the vesicles rises approximately 100-fold when oxalate is replaced by phosphate. The activity of the calcium dependent ATPase parallels the calcium uptake activity. 5. It is excluded that the inhibition of calcium uptake produced by phosphate is caused by an enhanced permeability of the sarcoplasmic reticulum membranes for calcium in the presence of phosphate.

scholarly journals Calcium dependence of inactivation of calcium release from the sarcoplasmic reticulum in skeletal muscle fibers.

1991 ◽  
Vol 97 (3) ◽  
pp. 437-471 ◽  
Author(s):  
B J Simon ◽  
M G Klein ◽  
M F Schneider
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Binding ◽  
Calcium Release ◽  
Muscle Fibers ◽  
Calcium Transients ◽  
Calcium Dependence ◽  
Fura 2 ◽  
Test Pulse ◽  
Calcium Dependent

The steady-state calcium dependence of inactivation of calcium release from the sarcoplasmic reticulum was studied in voltage-clamped, cut segments of frog skeletal muscle fibers containing two calcium indicators, fura-2 and anti-pyrylazo III (AP III). Fura-2 fluorescence was used to monitor resting calcium and relatively small calcium transients during small depolarizations. AP III absorbance signals were used to monitor larger calcium transients during larger depolarizations. The rate of release (Rrel) of calcium from the sarcoplasmic reticulum was calculated from the calcium transients. The equilibrium calcium dependence of inactivation of calcium release was determined using 200-ms prepulses of various amplitudes to elevate [Ca2+] to various steady levels. Each prepulse was followed by a constant test pulse. The suppression of peak Rrel during the test pulse provided a measure of the extent of inactivation of release at the end of the prepulse. The [Ca2+] dependence of inactivation indicated that binding of more than one calcium ion was required to inactivate each release channel. Half-maximal inactivation was produced at a [Ca2+] of approximately 0.3 microM. Variation of the prepulse duration and amplitude showed that the suppression of peak release was consistent with calcium-dependent inactivation of calcium release but not with calcium depletion. The same calcium dependence of inactivation was obtained using different amplitude test pulses to determine the degree of inactivation. Prepulses that produced near maximal inactivation of release during the following test pulse produced no suppression of intramembrane charge movement during the test pulse, indicating that inactivation occurred at a step beyond the voltage sensor for calcium release. Three alternative set of properties that were assumed for the rapidly equilibrating calcium-binding sites intrinsic to the fibers gave somewhat different Rrel records, but gave very similar calcium dependence of inactivation. Thus, equilibrium inactivation of calcium release appears to be produced by rather modest increases in [Ca2+] above the resting level and in a steeply calcium-dependent manner. However, the inactivation develops relatively slowly even during marked elevation of [Ca2+], indicating that a calcium-independent transition appears to occur after the initial calcium-binding step.

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