Correlation between protein kinase-mediated stimulation of calcium transport by cardiac sarcoplasmic reticulum and phosphorylation of a 22 000 dalton protein

Kirchberger, Madeleine A.; Chu, Gregory H.

doi:10.1016/0005-2736(76)90269-8

“…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. These PK, after activation by cyclic AMP, catalyze the phosphorylation of various intracellular proteins (Walsh et al, 1968;Miyamoto et al, 1969), including the cardiac sarcoplasmic reticulum (La Raia and Morkin, 1973;Tada et al, 1975;Kirchberger and Chu, 1976;Kirchberger and Raffo, 1977;Wray et al, 1973;Kirchberger et al, 1974;Wray and Gray, 1977.) It is now generally accepted that calcium uptake by cardiac sarcoplasmic reticulum vesicles is increased by as much as 2-to 3-fold after preincubation with cyclic AMP and cyclic AMP-dependent PK (La Raia and Morkin, 1973;Katz et al, 1975;Tada et al, 1975;Kirchberger et al, 1972;Tada et al, 1975;.…”

Section: Discussionmentioning

confidence: 99%

“…Initial rates of both Ca 2+ -dependent ATPase activity and calcium uptake are increased two to three times following incubation of cardiac sarcoplasmic reticulum vesicles with PK and cyclic AMP without a change in the stoichiometry of 2 mol of calcium transported per mole ATP hydrolyzed . This stimulation of calcium transport is associated with the phosphorylation of phospholamban, a 22,000-dalton component of the sarcoplasmic reticulum vesicles which is separable from the Ca 2+ -dependent ATPase protein (mol wt 100,000) on polyacrylamide gel electrophoresis (La Raia and Morkin, 1974;Kirchberger and Chu, 1976;Kirchberger and Raffo, 1977).…”

mentioning

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

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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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“…The phospholamban is phosphorylated primarily at serine (80%) and threonine (20%) residues (286); the total amount of phosphate incorporated into the 22,000-dalton component of cardiac microsomes isolated from dog, cat, rabbit, and guinea pig is 0.75, 0.25, 0.30, and 0.14 nmol/mg protein, respectively (285); this is only slightly less than the estimated concentration of Ca 2+-ATPase in the membrane (283,286), suggesting a 1:1 stoichiometry between phospholamban and the Ca 2+-transport ATPase.…”

Section: Kinetic Differences Between Sr Of Fast-twitch and Slow-twitcmentioning

confidence: 99%

Mechanism of Ca²⁺Transport by Sarcoplasmic Reticulum

Martonosi

¹

,

Beeler

²

1983

Comprehensive Physiology

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The sections in this article are: Structure of Sarcoplasmic Reticulum and Transverse Tubules Structure of Plasmalemma and T Tubules Sarcoplasmic Reticulum Junction Between T Tubules and SR Mechanism of Excitation‐Contraction Coupling Isolation of SR , T Tubules, and Surface Membrane Elements from Skeletal Muscle Separation of Membrane Fractions by Calcium Oxalate or Calcium Phosphate Loading Protein Composition of SR Structure of Ca 2+ ‐Transport ATP ase and Its Disposition in SR Membrane Fragmentation of Ca 2+ ‐ ATP ase With Proteolytic Enzymes Primary Sequence of Ca 2+ ‐Transport ATP ase From Rabbit SR Structure of Proteolipids Structure and Distribution of Calsequestrin and High‐Affinity Ca 2+ ‐Binding Protein in SR Lipid Composition of SR Distribution of Phospholipids in Membrane Bilayer Role of Phospholipids in Atpase Activity and CA 2+ Transport Boundary Lipids and the Problem of Lipid Annulus Rate of ATP Hydrolysis and Physical Properties of the Lipid Phase Mobility of Phospholipids and Ca 2+ ‐Transport ATP ase in SR Mechanism of ATP Hydrolysis and CA 2+ Transport Introduction of Reaction Sequence Ca 2+ Binding to SR Binding of Ca 2+ to Ca 2+ ‐Transport ATP ase Binding of Mg 2+ to Ca 2+ ‐ ATPase Binding of ATP to Ca 2+ ‐ ATPase Binding of Various Substrates to Ca 2+ ‐ ATPase Influence of ATP on Mobility and Reactivity of Protein Side‐Chain Groups Formation of Enzyme‐Substrate Complex Formation and Properties of Phosphoproteins Kinetics of E∼P Formation Relationship Between Enzyme Phosphorylation and Translocation of Calcium Changes in Ca 2+ Affinity of Phosphoenzyme During Ca 2+ Translocation ADP ‐Sensitive and ADP ‐insensitive Phosphoprotein Intermediates Effect of Potassium on ATPase Activity and Ca 2+ Transport Reversal of the CA 2+ Pump Ca 2+ Release Induced by ADP + P i Ca 2+ Gradient‐Dependent Phosphorylation of ATPase by P i Arsenate‐Induced Ca 2+ Release Mechanism of Ca 2+ Release Induced by ADP + P i Ca 2+ Gradient‐Independent Phosphorylation of Ca 2+ ‐ ATPase by P i Role of Ca 2+ ‐Protein Interactions in ATP Synthesis P i HOH Exchange NTP P i Exchange Physical Basis of CA 2+ Translocation Protein‐Protein Interactions in SR and Their Functional Significance Electron Microscopy Fluorescence‐Energy Transfer Electron Spin Resonance Studies ATP ase‐ ATP ase Interactions in Detergent Solutions Chemical Cross‐Linking Effects of Inhibitors on ATPase Activity Possibility of Subunit Heterogeneity Conclusion Permeability of SR Monovalent‐Cation Channels in SR Anion Channels in SR Effect of Membrane Proteins on Permeability of SR Membranes Relationship Between Membrane Potential and Calcium Fluxes Across SR Membrane Probes as Indicators of SR Membrane Potential Influence of SR Membrane Potential on Calcium Permeability Influence of Membrane Potential on Active Calcium Transport Effect of Calcium Uptake on Membrane Potential of SR A Critical Analysis of Experimental Findings on Effects of Ca 2+ Transport on Membrane Potential Effect of Calcium on Optical Response of Positive Cyanine Dyes Response of Negatively Charged Dyes to Calcium Transport by SR Vesicles Membrane Potential of SR In Vivo Effect of Ca 2+ Release on Membrane Potential of SR Transport of CA 2+ by Cardiac SR Kinetic Differences Between SR of Fast‐Twitch and Slow‐Twitch Skeletal Muscles Regulation of CA 2+ Transport by Membrane Phosphorylation Role of Protein Kinase‐Dependent Membrane Phosphorylation in Regulation of Ca 2+ Transport by Skeletal Muscle SR Physiological Significance of Phospholamban Phosphorylation Biosynthesis of SR Studies on SR Development In Vivo Assembly of SR in Cultured Skeletal and Cardiac Muscle Synthesis of Ca 2+ ‐Transport ATPase in Cell‐Free Systems and Its Insertion into the Membrane Synthesis of Calsequestrin Regulation of Synthesis of Ca 2+ ‐Transport ATPase Myogenic Regulation Neural Influence on Concentration of Ca 2+ ‐ ATPase in Muscle Cells

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“…The second is activation of cyclic AMP-dependent protein kinase which then phosphorylates phospholamban (22,000 dalton protein). This in turn enhances the sarcoplasmic reticular Ca2+-dependent ATPase which is linked to the Ca2+-sequestering pump (Kirchberger & Chu, 1976;Tada, Ohmori, Yamada & Abe, 1979). Recent evidence suggests a third mechanism whereby P-adrenoceptor agonists might affect muscle contractions.…”

Section: Discussionmentioning

confidence: 99%

Effects of increasing the frequency of twitches and of isoprenaline on maximal twitches and cyclic AMP levels in slow‐ and fast‐contracting cat skeletal muscles

Merican

¹

,

Nott

²

,

Sunbhanich

³

1983

British J Pharmacology

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1Increasing the frequency of twitches and treatment with isoprenaline have been been compared for effects on twitch tension, tension-time integral and cyclic adenosine 3', 5'-monophosphate (cyclic AMP) levels in the slow-contracting soleus muscle of cats, anaesthetized with chloralose and pentobarbitone. The effect of change in frequency of contractions on cyclic AMP in the fastcontracting extensor digitorum longus muscle was also examined. 2 Although both isoprenaline and increasing the frequency of contractions depressed twitch tension in the soleus, only isoprenaline enhanced cyclic AMP levels. The effects of isoprenaline were independent of the existing frequency of contractions of the muscle. Increasing the frequency of contractions enhanced twitches in the extensor digitorum longus muscle but did not change cyclic AMP levels. 3 It is concluded that cyclic AMP may mediate effects of ,B-adrenoceptor agonists but not those caused by increasing the frequency of contractions on slow-or fast-contracting skeletal muscles.

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Correlation between protein kinase-mediated stimulation of calcium transport by cardiac sarcoplasmic reticulum and phosphorylation of a 22 000 dalton protein

Cited by 50 publications

References 9 publications

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

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

Mechanism of Ca²⁺Transport by Sarcoplasmic Reticulum

Effects of increasing the frequency of twitches and of isoprenaline on maximal twitches and cyclic AMP levels in slow‐ and fast‐contracting cat skeletal muscles

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Correlation between protein kinase-mediated stimulation of calcium transport by cardiac sarcoplasmic reticulum and phosphorylation of a 22 000 dalton protein

Cited by 50 publications

References 9 publications

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

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

Mechanism of Ca2+Transport by Sarcoplasmic Reticulum

Effects of increasing the frequency of twitches and of isoprenaline on maximal twitches and cyclic AMP levels in slow‐ and fast‐contracting cat skeletal muscles

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Mechanism of Ca²⁺Transport by Sarcoplasmic Reticulum