Adenosine 3', 5'-Monophosphate-Dependent Membrane Phosphorylation

LaRaia, Paul J.; Morkin, Eugene

doi:10.1161/01.res.35.2.298

Cited by 156 publications

(20 citation statements)

References 33 publications

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“…Phosphorylated cardiac SR, isolated by Sephadex G-50, was subjected to gel electrophoresis under denaturing conditions, and a 22 000 M, protein was identified as the only 32P-acceptor protein (Kranias et al, 1980). These results are in agreement with previous observations (LaRaia & Morkin, 1974;Kirchberger & Tada, 1976;Schwartz et al, 1976;Wray & Gray, 1977). Phosphorylation of the 22000 M, protein was abolished in the presence of the heat-stable protein kinase inhibitor isolated from rabbit skeletal muscle.…”

Section: Camp-dependent Phosphorylation Of Cardiac Srsupporting

confidence: 90%

“…The stimulation of calcium transport may be associated with phosphorylation of a 22 000-dalton, membrane-bound protein referred to as phospholamban by Kirchberger et al (1975). It has been known that phospholamban can be phosphorylated by both endogenous, membrane-bound (LaRaia & Morkin, 1974;Wray & Gray, 1977) and exogenous, soluble Kirchberger & Tada, 1976;Schwartz et al, 1976;) CAMP-dependent protein kinases (EC 2.7.1.37, ATP:protein phosphotransferase).…”

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confidence: 99%

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Mechanism of the stimulation of calcium ion dependent ATPase of cardiac sarcoplasmic reticulum by adenosine 3',5'-monophosphate dependent protein kinase

Kranias¹,

Mandel²,

Wang³

et al. 1980

Biochemistry

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Canine cardiac sarcoplasmic reticulum (SR) is known to be phosphorylated by adenosine 3',5'-monophosphate (cAMP) dependent protein kinase on a 22 000-dalton protein. Phosphorylation enhances the initial rate of Ca2+ uptake and Ca2+-ATPase activity. To determine the molecular mechanism by which phosphorylation regulates the calcium pump in SR, we examined the effect of cAMP-dependent protein kinase on the individual steps of the Ca2+-ATPase reaction sequence. Cardiac sarcoplasmic reticulum was preincubated with cAMP and cAMP-dependent protein kinse in the presence (phosphorylated SR) and absence (control) of adenosine 5'-triphosphate (ATP). Control and phosphorylated SR were subsequently assayed for formation (4-200 ms) and decomposition (0-73 ms) of the acid-stable phosphorylated enzyme (E approximately P) of Ca2+-ATPase in media containing 100 microM [ATP] and various free [Ca2+]. cAMP-dependent phosphorylation of SR resulted in pronounced stimulation of initial rates and levels of E approximately P formed at low free [Ca2+] (less than or equal to 7 microM), but the effect was less at high free Ca2+ (greater than or equal to 10 microM). This stimulation was associated with a decrease in the dissociation constant for Ca2+ binding and a possible increase in Ca2+ sites. The observed rate constant for E approximately P formation of calcium-preincubated SR was not significantly altered by phosphorylation. Phosphorylation also increased the initial rate of E approximately P decomposition. These findings indicate that phosphorylation of cardiac SR by cAMP-dependent protein kinase regulates several steps in the Ca2+-ATPase reaction sequence which result in an overall stimulation of the calcium pump observed at steady state.

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Section: Camp-dependent Phosphorylation Of Cardiac Srsupporting

confidence: 90%

mentioning

confidence: 99%

Mechanism of the stimulation of calcium ion dependent ATPase of cardiac sarcoplasmic reticulum by adenosine 3',5'-monophosphate dependent protein kinase

Kranias¹,

Mandel²,

Wang³

et al. 1980

Biochemistry

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“…It has been suggested that cAMP increases the I~i by stim-(, (( 'f 1Hulating direct phosphorylation of a Ca2" channel (3,43,44 (45,46) and this might acsec count for the cAMP-induced modulation of Isi (34)(35)(36). One might (A) Rapid response to flashes in an especially stable preppredict that these mechanisms would result in different reosed to 30 ,uM o-nitrobenzyl cAMP.…”

Section: Resultsmentioning

confidence: 99%

Time course of the increase in the myocardial slow inward current after a photochemically generated concentration jump of intracellular cAMP.

Nargeot¹,

Nerbonne²,

Engels³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

119

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Voltage-clamped atrial trabeculae from bullfrog hearts were exposed to membrane-permeant photolyzable o-nitrobenzyl esters of cAMP and cGMP. UV flashes produced intracellular concentration jumps of cAMP or cGMP. With the cAMP derivative, flashes resulted in an increased slow inward current (Is;), producing a broadened action potential. The ISi reached a maximum 10-30 sec after the flash and decreased over the next 60-300 sec. The first increases were observable within 150 msec; this value is an upper limit imposed by the instrumentation. Responses to flashes lasted longer at higher drug concentrations and in the presence of the phosphodiesterase inhibitor papaverine; effects of flashes developed and decreased faster at higher temperature. Although the amplitude of the 'Si was increased, its waveform and voltage sensitivity were not affected. Intracellular concentration jumps of cAMP failed to affect the muscarinic K+ conductance. There were no observable effects of cGMP concentration jumps. The data confirm (i) that cAMP regulates the Ii and (ii) that the 5-to 10-sec delay between application of .8-agonists and the onset of positive inotropic effects, observed in previous studies, has been correctly ascribed to events prior to the interaction between cAMP and protein kdnase.Cyclic nucleotides are thought to play a pivotal role in the regulation of the strength and frequency of the heartbeat by autonomic neurotransmitters. Electrophysiological investigations show that such inotropic and chronotropic effects arise partly through changes in the slow inward current (Isi), which is carried mainly by calcium ions (1-5). The amplitude of the Isi is enhanced, and the plateau of the action potential is consequently lengthened, by many treatments that increase intracellular cAMP, such as /3-adrenergic stimulation (1, 3, 6), direct intracellular application of cAMP itself (5, 7-11), phosphodiesterase inhibition (12), exposure to membrane-permeant analogues of cAMP (13), and GTPase inhibition (14). On the other hand, this slow inward current is inhibited by muscarinic stimulation (4, 15, 16), which also inhibits adenylate cyclase (17,18 (22,23). Therefore, one expects that the positive inotropic effects would appear much more quickly in an experiment in which the intracellular cAMP concentration itself is jumped directly.We have therefore developed a method for producing concentration jumps of cyclic nucleotides within cells under physiological investigation. Our procedure exploits the properties of o-nitrobenzyl cAMP ( Fig. 1) and its cGMP analog. These molecules are members of a group of phosphotriesters that enter cells (24-26). The o-nitrobenzyl esters can then be photolyzed to produce the cyclic nucleotides themselves, presumably within a few msec (27-30). We find that the Is4 is indeed increased by photochemically generated concentration jumps of intracellular cAMP and that the latency of this action (< 150 msec) is no more than 3% of the latency for ,B-adrenergic stimulation.There are additional questions ab...

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“…PLB was first described in the sarcoplasmic reticulum of cardiac muscle and slowtwitch skeletal muscle [2], but has also been demonstrated in smooth muscle [3]. Cyclic AMP-dependent protein kinase [4], cyclic GMP-dependent protein kinase [5], Ca2" + calmodulin-dependent protein kinase [6] and protein kinase C [7] each phosphorylates PLB. Phosphorylation of PLB causes a conformational change of the protein that might be responsible for the observed changes in activities of Ca2"-stimulated Mg2+-dependent ATPase and of Ca2`transport into sarcoplasmicreticulum vesicles.…”

Section: Introductionmentioning

confidence: 99%

cDNA cloning and sequencing of phospholamban from pig stomach smooth muscle

Verboomen

Wuytack

Eggermont

et al. 1989

Biochemical Journal

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Phospholamban cDNA from pig stomach smooth muscle was cloned and sequenced. The 737-nucleotide-residue cDNA contained an open reading frame of 156 nucleotide residues encoding a peptide of 52 amino acid residues (Mr 6080). This peptide shares 100% sequence identity with dog cardiac-muscle phospholamban. It differs from rabbit cardiac-muscle and slow-twitch skeletal-muscle phospholamban only at position 2, which is a glutamic acid residue in rabbit phospholamban, but an aspartic acid residue in the pig smooth-muscle protein. Northern-blot analysis reveals the presence of several phospholamban mRNAs in smooth muscle, but a 900-nucleotide-residue and a 2800-nucleotide-residue transcript predominate.

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Adenosine 3', 5'-Monophosphate-Dependent Membrane Phosphorylation

Cited by 156 publications

References 33 publications

Mechanism of the stimulation of calcium ion dependent ATPase of cardiac sarcoplasmic reticulum by adenosine 3',5'-monophosphate dependent protein kinase

Mechanism of the stimulation of calcium ion dependent ATPase of cardiac sarcoplasmic reticulum by adenosine 3',5'-monophosphate dependent protein kinase

Time course of the increase in the myocardial slow inward current after a photochemically generated concentration jump of intracellular cAMP.

cDNA cloning and sequencing of phospholamban from pig stomach smooth muscle

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