The cyclic AMP-dependent modulation of cardiac sarcolemmal slow calcium channels

Rinaldi, Murielle L.; Capony, Jean‐Paul; Demaille, Jacques

doi:10.1016/0022-2828(82)90206-1

Cited by 74 publications

(15 citation statements)

References 42 publications

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“…The presence of 14-and 26-kD proteins, in addition to the well-known 9-to 11-kD proteins, is a more definite proof for the SL origin of the membrane preparation used in the present study (Kranias and Solaro, 1982;Lamers and Stinis, 1982;Rinaldi et al, 1982). The recent report of Kranias and Solaro (1982) showed SDS-PAGE profiles of Coomassie blue and 32 P-stained SR proteins from rabbit heart that were very different from those presented for SL in Figure 5, except for the presence of the 9-to 11-kD phosphoprotein.…”

Section: Controlmentioning

confidence: 91%

“…A 9-to 11-kD 'phospholambanlike' phosphoprotein, otherwise known as 'calciductin,* has been implicated in the regulation of both the SL Ca ++ pump and the voltage-dependent Ca ++ channel (Lamers et al, 1981;Rinaldi et al, 1982;Lamers, in press). According to a recent study (Manalan and Jones, 1982), phospholamban in SL preparations is most likely an adventitious contaminant.…”

Section: Lamers Et Al /Membrane Properties In Calcium-depleted Heartsmentioning

confidence: 99%

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Biochemical properties of membranes isolated from calcium-depleted rabbit hearts.

Lamers¹,

Stinis²,

Ruigrok³

1984

Circulation Research

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SUMMARY. The purpose of this study was to define the biochemical properties of sarcolemma from the caldum-depleted rabbit heart. Caldum repletion after caldum-free perfusion results in irreversible damage to the heart (caldum paradox). No difference was found in specific activity of the Na + -Ca ++ antiporter in a crude preparation of sarcolemmal vesicles that was isolated from caldum-depleted hearts, compared with control perfused hearts. Likewise, the passive caldum efflux from sarcolemmal vesicles, preloaded with caldum via the Na + -Ca ++ antiporter, showed rates that were identical with control values. This indicates that the sarcolemma caldum permeability is not affected by caldum-free perfusion of the heart. Na + ,K + -ATPase activity in sarcolemma isolated from caldum-depleted hearts was reduced by 75% (P < 0.005) compared with the control activity. Sarcolemmal phosphoproteins, whether produced by endogenous cyclic AMP-or caldum-calmodulin-dependent protein kinase, were not altered by caldum-free perfusion of the heart. The content of an important caldum-binding site in the myocardial cell, the sialic add residues, was also estimated. Only a long period (60 minutes) of caldum-free perfusion resulted in a significant decrease (by 68%, P < 0.025) of sialic add content in the homogenate but not in the sarcolemma preparation. In hearts that were reperfused for 15 minutes with a normal caldum concentration (1.3 mM), sarcolemmal Na + ,K + -ATPase remained depressed and caldum permeability was still unchanged. It is possible that the sarcolemma isolation method selected a distinct part of the sarcolemma from the caldum-depleted and repleted heart that had no modified glycocalyx and permeability barriers to caldum ions, and that another part of the sarcolemma with altered properties was lost during the isolation procedure. Another possibility is that reconstitution processes during isolation affected membrane permeability properties. The results of the Na + ,K + -ATPase measurements provide evidence that the net caldum gain of the cells after caldum repletion may be associated, in part, with a loss in ability of the sarcolemma to remove caldum from the cytosol. (Circ Res 54: 217-226, 1984)

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Section: Controlmentioning

confidence: 91%

Section: Lamers Et Al /Membrane Properties In Calcium-depleted Heartsmentioning

confidence: 99%

Biochemical properties of membranes isolated from calcium-depleted rabbit hearts.

Lamers¹,

Stinis²,

Ruigrok³

1984

Circulation Research

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“…They disagree with the conclusions of a recently published study showing that cyclic AMP-mediated renin secretion is unaffected by A23187, the Ca2+ ionophore which is believed to raise cellular Ca2+ (Bondar et al 1984). An obvious explanation for the discrepancy may be that the concentration of A23187 used in the study of Bondar et al (1984) (Rinaldi, Capony & Demaille, 1982;Reuter, 1983;Bean, Nowycky & Tsien, 1984;Cachelin, de Peyer, Kokubum & Reuter, 1983;Siegelbaum & Tsien, 1983;Mauger, Poggioli, Guesdon & Claret, 1984). Recent evidence has also suggested another mechanism whereby forskolin (and thereby cyclic AMP) may stimulate renin secretion.…”

Section: Renin Secretionmentioning

confidence: 99%

Forskolin and calcium: interactions in the control of renin secretion and perfusate flow in the isolated rat kidney.

Fray¹,

Park²

1986

The Journal of Physiology

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SUMMARY1. Forskolin (activator of adenyl cyclase), high concentrations of K+ and high renal perfusion pressure (manoeuvres known to increase Ca2+ permeability), and calmidazolium (the specific blocker of calmodulin) were used to investigate the mechanisms whereby adenosine 3',5'-phosphate (cyclic AMP) and Ca2+ interact to control renin secretion and perfusate flow in the isolated perfused rat kidney.2. Forskolin stimulated renin secretion and caused vasodilation in a dose-dependent manner in medium containing 5 mM-Ca2+. Reducing the Ca2+ concentration to 1P25 mm did not affect the renin stimulatory response but blunted the vasodilation.3. High K+ concentration reversed the forskolin-induced renin secretion and vasodilation. Conversely, forskolin reversed the high K+-induced renin inhibition of renin secretion and vasoconstriction. These effects of forskolin and high K+ were absent when Ca2+ was withheld from the perfusion medium. High renal perfusion pressure also reversed the forskolin-induced renin secretion.4. Calmidazolium prevented the inhibition mediated by high K+ and high perfusion pressure and thereby restored the forskolin-induced stimulation. Calmidazolium also caused a prompt and marked vasoconstriction.5. The calmidazolium-induced stimulation of renin secretion was Ca2+-dependent since the drug was ineffective in the absence of Ca2+. On the other hand, the prompt and potent vasoconstriction was present even in the Ca2+-free medium.6. These results support the hypothesis that cyclic AMP stimulates renin secretion by a mechanism which involves a lowering of membrane permeability to Ca2+ in addition to lowering cytosolic Ca2+ concentration. High K+ and high renal perfusion pressure inhibit renin secretion by raising the membrane permeability to Ca2+, thereby raising the intracellular Ca2+ concentration which then inhibits renin secretion by a calmodulin-dependent process. A further general conclusion from these studies is that membrane permeability to Ca2+ and cellular Ca2+ concentration are of central importance in the control of renin secretion and renal blood flow.

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“…1981;Cachelin, de Peyer, Kokubun & Reuter, 1983) and by intracellular application of cyclic AMP or cyclic-AMP-dependent protein kinase (Tsien, 1973;Tsien & Weingart, 1976;Vogel & Sperelakis, 1981;Trautwein, Taniguchi & Noma, 1982;Osterrieder, Brum, Hescheler, Trautwein, Flockerzi & Hofmann, 1982;Brum, Flockerzi, Hofmann, Osterrieder & Trautwein, 1983;Irisawa & Kokubun, 1983;Brum, Osterrieder & Trautwein, 1984). It has been suggested that cyclic-AMP-dependent protein kinase activates Ca channels by phosphorylation of either the Ca channel itself or a protein that regulates the Ca channel (Rinaldi, LePeuch & Demaille, 1981;Rinaldi, Capony & Demaille, 1982;Manalan & Jones, 1982).…”

mentioning

confidence: 99%

Mechanism of action of acetylcholine on calcium current in single cells from frog ventricle.

Fischmeister¹,

Hartzell²

1986

The Journal of Physiology

199

122

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SUMMARY1. Ca currents (ICa) were measured by whole-cell patch clamp in single cells isolated from frog ventricle in which K currents were blocked with intracellular (120 mM) and extracellular (20 mM) Cs. Inward currents elicited by depolarizing voltage steps from a holding potential of -80 mV were blocked completely by 0 5 mM-Cd.2. The quality of the voltage clamp was assessed using two patch electrodes on a single cell. One electrode was used in the voltage-clamp mode to measure membrane currents and the other in current-clamp to measure membrane potential. Ca currents as large as 2 nA were well clamped in cells as long as 210 ,um.3. Acetylcholine (ACh) had no effect on ICa in the absence of fl-adrenergic stimulation but reduced to control levels ICa elevated by isoprenaline. Nanomolar concentrations of ACh were able to reduce significantly ICa elevated by 2 ,LM-isoprenaline. 4. ACh had no effect on the shape of the I-V curve, on the reactivation (recovery from inactivation), or on the inactivation Of Ica. Although isoprenaline increased ICa by an average of 6-5-fold, it had no effect on the shape of the I-V curve or on the inactivation at test potentials negative to +40 mV. However, isoprenaline slowed the half-reactivation time from a control value of 120+10 ms (mean+ S.D.) to 153 + 12 ms at -80 mV.5. The efect of cyclic AMP on ICa was investigated using two patch electrodes, one filled with cyclic AMP. Maximal effects of cyclic AMP were observed with 5 /SM-cyclic AMP in the pipette. Maximal Ica was recorded several minutes after breaking the patch with the second electrode. After removing the cyclic-AMPcontaining electrode, Ica declined to control levels after 10 min.6. 5/M-cyclic AMP in the patch electrode increased Ica by an average of 6-9-fold, but had no effect on the shape of the I-V curve or on inactivation. Cyclic AMP had a slowing effect on reactivation (half-reactivation time = 155 + 24 ms) similar to that of isoprenaline.

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The cyclic AMP-dependent modulation of cardiac sarcolemmal slow calcium channels

Cited by 74 publications

References 42 publications

Biochemical properties of membranes isolated from calcium-depleted rabbit hearts.

Biochemical properties of membranes isolated from calcium-depleted rabbit hearts.

Forskolin and calcium: interactions in the control of renin secretion and perfusate flow in the isolated rat kidney.

Mechanism of action of acetylcholine on calcium current in single cells from frog ventricle.

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