Effect of ACTH and hydrocortisone on Ca++-ATPase activity of the sarcoplasmic reticulum of skeletal muscle

1987 ◽  
Vol 104 (2) ◽  
pp. 1080-1082 ◽  
Author(s):  
V. I. Korkach ◽  
A. N. Fedorov
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Atpase Activity

scholarly journals A model for the uptake and release of Ca2+ by sarcoplasmic reticulum

1987 ◽  
Vol 245 (3) ◽  
pp. 739-749 ◽  
Author(s):  
G W Gould ◽  
J M McWhirter ◽  
J M East ◽  
A G Lee
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
External Medium ◽  
Spontaneous Release ◽  
Calculated Concentration ◽  
Effects Of Ph ◽  
Hydrolysis Of ◽  
Uptake And Release

On addition of ATP to vesicles derived from the sarcoplasmic reticulum (SR) of skeletal muscle, Ca2+ is accumulated from the external medium. Following uptake, spontaneous release of Ca2+ occurs in the presence or in the absence of ATP. These processes of Ca2+ uptake and release were simulated by using the models derived for ATPase activity [Gould, East, Froud, McWhirter, Stefanova & Lee (1986) Biochem. J. 237, 217-227; Stefanova, Napier, East & Lee (1987) Biochem. J. 245, 723-730] and for Ca2+ release from passively loaded vesicles [McWhirter, Gould, East & Lee (1987) Biochem. J. 245, 713-722]. The simulations are consistent with measurements of the effects of pH, K+, Ca2+ and Mg2+ on uptake and release of Ca2+. The increase in maximal Ca2+ accumulation observed in the presence of maleate is explained in terms of complexing of Ca2+ and maleate within the SR. The calculated concentration of ADP generated by hydrolysis of ATP has a large effect on the simulations. The effects of an ATP-regenerating system on the measured Ca2+ uptake is explained in terms of both removal of ADP and precipitation of Ca3(PO4)2 within the vesicles. It is concluded that both the process of Ca2+ uptake and the process of Ca2+ release seen with SR vesicles can be interpreted quantitatively in terms solely of the properties of the Ca2+ + Mg2+-activated ATPase.

Effects of prolonged low frequency stimulation on skeletal muscle sarcoplasmic reticulum

1995 ◽  
Vol 73 (8) ◽  
pp. 1154-1164 ◽  
Author(s):  
E. R. Chin ◽  
H. J Green ◽  
F. Grange ◽  
J. Dossett-Mercer ◽  
P. J. O'Brien
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Metabolic Response ◽  
Contractile Activity ◽  
Creatine Phosphate ◽  
Energy Status ◽  
Muscle Lactate ◽  
Muscle Energy

The role of prolonged electrical stimulation on sarcoplasmic reticulum (SR) Ca2+sequestration measured in vitro and muscle energy status in fast white and red skeletal muscle was investigated. Fatigue was induced by 90 min intermittent 10-Hz stimulation of rat gastrocnemius muscle, which led to reductions (p < 0.05) in ATP, creatine phosphate, and glycogen of 16, 55, and 49%, respectively, compared with non-stimulated muscle. Stimulation also resulted in increases (p < 0.05) in muscle lactate, creatine, Pi, total ADP, total AMP, IMP, and inosine. Calculated free ADP (ADPf) and free AMP (AMPf) were elevated 3- and 15-fold, respectively. No differences were found in the metabolic response between tissues obtained from the white (WG) and red (RG) regions of the gastrocnemius. No significant reductions in SR Ca2+ATPase activity were observed in homogenate (HOM) or a crude SR fraction (CM) from WG or RG muscle following exercise. Maximum Ca2+uptake in HOM and CM preparations was similar in control (C) and stimulated (St) muscles. However, Ca2+uptake at 400 nM free Ca2+was significantly reduced in CM from RG (0.108 ± 0.04 to 0.076 ± 0.02 μmol∙mg−1protein∙min−1in RG–C and RG–St, respectively). Collectively, these data suggest that reductions in muscle energy status are dissociated from changes in SR Ca2+ATPase activity in vitro but are related to Ca2+uptake at physiological free [Ca2+] in fractionated SR from highly oxidative muscle. Dissociation of SR Ca2+ATPase activity from Ca2+uptake may reflect differences in the mechanisms evaluated by these techniques.Key words: sarcoplasmic reticulum, contractile activity, Ca2+sequestration, energy status, red and white gastrocnemius.

Hypochlorous acid inhibits Ca2+-ATPase from skeletal muscle sarcoplasmic reticulum

1998 ◽  
Vol 84 (2) ◽  
pp. 425-430 ◽  
Author(s):  
Terence G. Favero ◽  
David Colter ◽  
Paul F. Hooper ◽  
Jonathan J. Abramson
Keyword(s):  
Reactive Oxygen Species ◽  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Structural Damage ◽  
Hypochlorous Acid ◽  
Reactive Oxygen ◽  
Sulfhydryl Groups ◽  
Dependent Manner ◽  
Oxygen Species

Favero, Terence G., David Colter, Paul F. Hooper, and Jonathan J. Abramson. Hypochlorous acid inhibits Ca2+-ATPase from skeletal muscle sarcoplasmic reticulum. J. Appl. Physiol. 84(2): 425–430, 1998.—Hypochlorous acid (HOCl) is produced by polymorphonuclear leukocytes that migrate and adhere to endothelial cells as part of the inflammatory response to tissue injury. HOCl is an extremely toxic oxidant that can react with a variety of cellular components, and concentrations reaching 200 μM have been reported in some tissues. In this study, we show that HOCl interacts with the skeletal sarcoplasmic reticulum Ca2+-adenosinetriphosphatase (ATPase), inhibiting transport function. HOCl inhibits sarcoplasmic reticulum Ca2+-ATPase activity in a concentration-dependent manner with a concentration required to inhibit ATPase activity by 50% of 170 μM and with complete inhibition of activity at 3 mM. A concomitant reduction in free sulfhydryl groups after HOCl treatment was observed, paralleling the inhibition of ATPase activity. It was also observed that HOCl inhibited the binding of the fluorescent probe fluorescein isothiocyanate to the ATPase protein, indicating some structural damage may have occurred. These findings suggest that the reactive oxygen species HOCl inhibits ATPase activity via a modification of sulfhydryl groups on the protein, supporting the contention that reactive oxygen species disrupt the normal Ca2+-handling kinetics in muscle cells.

scholarly journals Ethanol has different effects on Ca2+-transport ATPases of muscle, brain and blood platelets

1995 ◽  
Vol 312 (3) ◽  
pp. 733-737 ◽  
Author(s):  
F Mitidieri ◽  
L de Meis
Keyword(s):  
Skeletal Muscle ◽  
Endoplasmic Reticulum ◽  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Blood Platelets ◽  
Activity Increase ◽  
Low Concentrations ◽  
Biphasic Effect ◽  
Transport Atpases

The effects of ethanol on different sarco/endoplasmic reticulum Ca(2+)-transport ATPases (SERCAs) were studied. In sarcoplasmic reticulum vesicles, ethanol concentrations varying from 5 to 20% promoted a progressive inhibition of Ca2+ uptake, enhancement of Ca2+ efflux, activation of the ATPase activity, increase of the enzyme phosphorylation by ATP and inhibition of enzyme phosphorylation by P1. The effects of ethanol on Ca2+ uptake and Ca2+ efflux were antagonized by Mg2+, P(i) and spermine. The increased efflux promoted by ethanol was antagonized by Ca2+ and thapsigargin. In brain and platelet vesicles a biphasic effect of ethanol was observed, so that activation occurred at low concentrations (5-10%) and inhibition at higher concentrations. The activation was not observed with the use of n-propanol and n-butanol. Different from the situation in sarcoplasmic reticulum, the decrease of the Ca2+ uptake in brain and platelet vesicles was associated with an inhibition of the ATPase activity. Mg2+ and P(i) antagonized the enhancement of Ca2+ efflux and the inhibition of Ca2+ uptake promoted by ethanol. However, thapsigargin and Ca2+ did not arrest the Ca2+ efflux promoted by ethanol in brain and platelet preparations. These results suggest that, in sarcoplasmic reticulum vesicles, ethanol uncouples the pump, promoting its activity as a Ca2+ channel. The SERCA isoform found in skeletal muscle has different properties from the isoforms found in brain and blood platelets.

scholarly journals Iodination of Calsequestrin in the Sarcoplasmic Reticulum of Rabbit Skeletal Muscle: A Re-Examination

1979 ◽  
Vol 32 (2) ◽  
pp. 177 ◽  
Author(s):  
Ronald K Tume
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Calcium Binding ◽  
Local Environment ◽  
Maximal Inhibition ◽  
High Affinity ◽  
Tris Maleate ◽  
Sepharose 4B

The exposed proteins of sarcoplasmic reticulum (SR) vesicles from skeletal muscle were iodinated with the use of Sepharose 4B-bound lactoperoxidase, so that the location of the proteins in the membrane could be determined. It was found that the pattern of protein labelling could be modified simply by changing the constituents of the incubation media. This implies that the position or configuration of a particular protein in the membrane can be altered by the local environment. When the reaction was performed in the presence of 25 mM tris-maleate, pH 7 �0, alone, the Ca2+ pump ATPase (molecular weight 105000) and calsequestrin (47000) were both heavily labelled, suggesting they are at least partially exposed on the outer surface of the membrane. By contrast the high affinity calcium-binding protein (55000) was not labelled. However, when the vesicles were iodinated under conditions that were suitable for ATPase activity and Ca2+ accumulation, namely in the presence of 25 mM tris-maleate, pH 7 �0, 5 mM ATP, 5 mM Mg2+ and 0�05 mM Ca2+, a different pattern of labelling was obtained. No labelling of calsequestrin was observed whereas the extent of labelling of the Ca2+ pump ATPase remained about the same. The inclusion of anyone of the additives mentioned was effective in inhibiting the iodination of calsequestrin in the SR vesicle. When added alone, Ca2+ was more effective than Mg2+ in preventing labelling of calsequestrin. Half-maximal inhibition was observed at concentrations of approximately 0�05 mM Ca 2+ and 0�2-0�3 mM Mg2+ . Although much reduced, significant labelling of calsequestrin was observed even in the presence of 5 mM ATP. Investigations with partially purified calsequestrin revealed that the iodination of calsequestrin was the same in both the presence and absence of 1 mM Ca2 +. Therefore the reduction in label observed in intact SR vesicles probably represents a change in the location of calsequestrin within the membrane, rather than inhibition by Ca2+ of the iodination sites of the protein itself.

scholarly journals A kinetic model for Ca2+ efflux mediated by the Ca2+ + Mg2+-activated ATPase of sarcoplasmic reticulum

1987 ◽  
Vol 245 (3) ◽  
pp. 713-721 ◽  
Author(s):  
J M McWhirter ◽  
G W Gould ◽  
J M East ◽  
A G Lee
Keyword(s):  
Experimental Data ◽  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Kinetic Model ◽  
Atpase Activity ◽  
Binding Site ◽  
Binding Sites ◽  
Adenine Nucleotides ◽  
Contraction Coupling ◽  
High Affinity

We present a model for Ca2+ efflux from vesicles of sarcoplasmic reticulum (SR). It is proposed that efflux is mediated by the Ca2+ + Mg2+-activated ATPase that is responsible for Ca2+ uptake in this system. In the normal ATPase cycle of the ATPase, phosphorylation of the ATPase is followed by a conformational change in which the Ca2+-binding sites change from being outward-facing and of high affinity to being inward-facing and of low affinity. To mediate Ca2+ efflux, it is proposed that the ATPase can adopt a conformation in which the Ca2+-binding sites are of low affinity but still outward-facing. It is shown that experimental data on the rates of Ca2+ efflux can be simulated in terms of this model, with Ca2+-binding-site affinities previously proposed to explain ATPase activity [Gould, East, Froud, McWhirter, Stefanova & Lee (1986) Biochem. J. 237, 217-227]. Effects of Mg2+ and adenine nucleotides on efflux rates are explained. It is suggested that Ca2+ efflux from SR mediated by the ATPase could be important in excitation-contraction coupling in skeletal muscle.

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