Molecular mechanism of active calcium transport by sarcoplasmic reticulum.

Tada, Michihiko; Yamamoto, Tameyoshi; Tonomura, Yūji

doi:10.1152/physrev.1978.58.1.1

Cited by 574 publications

(167 citation statements)

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“…So the fast decrease of the ATP concentration in the absence of the regenerating system provides the fast inactivation of the Ca2' channels, whereas in the presence of the regenerating system ATP keeps these channels in the open state longer. To investigate further the mode of Ca2+ efflux via Ca2+-gated Ca2+ channels and the kinetics of Ca2+ efflux via channels not inhibited by ruthenium red, different nucleotide triphosphate substrates were employed to drive the Ca2+ pump [15,16]. Fig.2 shows that the rate of Ca2+ uptake in the presence of CTP ( fig.2a) and ITP (fig.2b) into heavy sarcoplasmic reticulum vesicles is similar to that when ATP is the substrate.…”

Section: Resultsmentioning

confidence: 99%

Pathways of calcium release from heavy sarcoplasmic reticulum vesicles isolated from rabbit skeletal muscle

1988

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The active uptake and efflux of Ca2+ from suspensions of vesicles from heavy rabbit muscle sarcoplasmic reticulum have been examined using the antipyrylazo III dye method in the presence of various nueleotide triphosphate substrates to support active Ca2+ accumulation. On addition of ATP, Ca2+ is rapidly accumulated and maintained at high internal concentrations until the substrate for pump protein is exhausted. Ca2+ ‐induced Ca2+ release which is inhibited by ruthenium red can be demonstrated. The kinetics of Ca2+ release via these channels is different from the Ca2+ efflux observed after substrate exhaustion. This rate was found to be dependent on the type of nucleotide triphosphate, decreasing in the order ATP > GTP > CTP > ITP UTP. It is suggested that different conformations of the Ca2+ pump protein induced by the different substrates may result in the creation of pathways for the facilitated diffusion of Ca2+.

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Section: Resultsmentioning

confidence: 99%

Pathways of calcium release from heavy sarcoplasmic reticulum vesicles isolated from rabbit skeletal muscle

1988

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“…Active calcium transport by sarcoplasmic reticulum vesicles has been found to be mediated by a Ca 2+ -dependent ATPase that transports 2 mol of Ca 2+ per mol ATP hydrolyzed in both skeletal and cardiac sarcoplasmic reticulum (Tada et al, 1978). Early attempts to define the mechanism by which catecholamines mediate the increased rate of cardiac relaxation yielded conflicting results (Hess et al, 1968;Entman et al, 1969;Shinebourne and White, 1970), which came to be understood better only after the discovery that intracellular effects of cyclic AMP were, in many instances, mediated by cyclic AMP-dependent PK.…”

Section: Discussionmentioning

confidence: 99%

Mechanism by which cyclic adenosine 3':5'-monophosphate-dependent protein kinase stimulates calcium transport in cardiac sarcoplasmic reticulum.

Hicks¹,

Shigekawa²,

Katz³

1979

Circulation Research

133

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SUMMARY We examined the mechanism by which cyclic AMP-dependent protein kinase (PK) stimulates the calcium pump of cardiac sarcoplasmic reticulum vesicles. The Ca 1+ dependence of calcium uptake rates by 30 /ig/ml canine cardiac sarcoplasmic reticulum was measured at 25 °C in 120 mM KCl, 40 mM histidine buffer (pH 6.8), 5 mM MgATP, and an ATP-regenerating system (75 fig/ml pyruvate kinase + 5 mM phosphoenolpyruvate) with 50 mM phosphate as calcium-precipitating anion. Preincubation with PK, 100 /ig/ml, plus 1 fiM cyclic AMP for 10 minutes increased calcium uptake rates from 2-to 3-fold at Ca 1+ concentrations between 0.25 and 2.0 fiM. This stimulation was associated with a decrease in the Ca 1+ concentration needed to produce 50% maximal calcium uptake velocity from 2.38 ± 0.21 to 1.07 ± 0.10 /IM (n -7, P< 0.001). The Ca 1+ dependence of calcium uptake in nonphosphorylated cardiac sarcoplasmic reticulum vesicles exhibited positive cooperativity, whereas cooperativity was not evident in the corresponding preparations from "fast" rabbit skeletal muscle. The estimated Hill coefficient for control vesicles was 1.77 ± 0.15; this value decreased significantly to 1.24 ± 0.08 (P < 0.01) after preincubation with PK. After exposure to PK, therefore, cardiac sarcoplasmic reticulum exhibited the low Ca 1+ cooperativity seen with fast skeletal sarcoplasmic reticulum. Phosphorylation of cardiac sarcoplasmic reticulum by PK thus appears to increase the apparent Ca 1+ -sensitivity of the calcium pump while decreasing positive cooperativity between the two Ca 1+ -binding sites of the calcium pump. Ore Res 44: 384-391,1979

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“…Isolated rabbit skeletal muscle sarcoplasmic reticulure (SR) contains, as an intrinsic membrane component, the 100 000 M r Ca2+-transport ATPase (~70% of the total protein) (review [1 ]). The peripheral proteins in this membrane are calsequestrin, Ca 2+ high affinity binding protein [1 ], calmodulin [2] as well as protein-kinases and -phosphatases [3][4][5][6][7].…”

mentioning

confidence: 99%

“…The peripheral proteins in this membrane are calsequestrin, Ca 2+ high affinity binding protein [1 ], calmodulin [2] as well as protein-kinases and -phosphatases [3][4][5][6][7]. During Ca 2+ transport the 100 000M r ATPase becomes phosphorylated at an aspartyl residue, and the product is a high energy acylphosphate intermediate of the catalytic cycle (review [1 ]). Characteristically, it reacts with hydroxylamine to yield the corresponding hydroxamate [8].…”

mentioning

confidence: 99%

Phosphorylation of the 100 000 M_r Ca²⁺‐transport ATPase by Ca²⁺ or cyclic AMP‐dependent and ‐independent protein kinases

Varsányi

Heilmeyer

1981

FEBS Letters

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Molecular mechanism of active calcium transport by sarcoplasmic reticulum.

Cited by 574 publications

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Pathways of calcium release from heavy sarcoplasmic reticulum vesicles isolated from rabbit skeletal muscle

Pathways of calcium release from heavy sarcoplasmic reticulum vesicles isolated from rabbit skeletal muscle

Mechanism by which cyclic adenosine 3':5'-monophosphate-dependent protein kinase stimulates calcium transport in cardiac sarcoplasmic reticulum.

Phosphorylation of the 100 000 M_r Ca²⁺‐transport ATPase by Ca²⁺ or cyclic AMP‐dependent and ‐independent protein kinases

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Molecular mechanism of active calcium transport by sarcoplasmic reticulum.

Cited by 574 publications

References 0 publications

Pathways of calcium release from heavy sarcoplasmic reticulum vesicles isolated from rabbit skeletal muscle

Pathways of calcium release from heavy sarcoplasmic reticulum vesicles isolated from rabbit skeletal muscle

Mechanism by which cyclic adenosine 3':5'-monophosphate-dependent protein kinase stimulates calcium transport in cardiac sarcoplasmic reticulum.

Phosphorylation of the 100 000 Mr Ca2+‐transport ATPase by Ca2+ or cyclic AMP‐dependent and ‐independent protein kinases

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Phosphorylation of the 100 000 M_r Ca²⁺‐transport ATPase by Ca²⁺ or cyclic AMP‐dependent and ‐independent protein kinases