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Cardiac sarcoplasmic reticulum-glycogenolytic complex, isolated as a single peak on sucrose density gradient, may function as a "compartmented" effector site for cyclic AMP resulting in modulation of both glycogenolysis and calcium transport. The conversion of phosphorylase b to a is stimulated by ATP and inhibited by protein kinase inhibitor. Cyclic AMP alone stimulated neither phosphorylase b to a conversion nor calcium uptake. An inhibitor of adenylate cyclase depressed both calcium uptake and phosphorylase activation and both functions were subsequently stimulated by micromolar concentrations of cyclic AMP. Endogenous phosphorylation of sarcoplasmic reticulum was also inhibited by adenylate cyclase inhibitor and the inhibition was reversed by cyclic AMP. These results suggest that the sarcoplasmic reticulum of cardiac muscle is an internal effector site for cyclic AMP which may regulate both calcium and metabolism. It appears that cyclic AMP formation in vitro is not the rate-controlling step in the activation sequence.
M L Entman, and
E P Bornet, and
A J Barber, and
A Schwartz, and
G S Levey, and
D C Lehotay, and
L A Bricker
December 1976,
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M L Entman, and
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A Schwartz, and
G S Levey, and
D C Lehotay, and
L A Bricker
August 1975,
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M L Entman, and
E P Bornet, and
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A Schwartz, and
G S Levey, and
D C Lehotay, and
L A Bricker
January 1976,
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M L Entman, and
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G S Levey, and
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L A Bricker
May 1986,
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M L Entman, and
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A Schwartz, and
G S Levey, and
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L A Bricker
December 1980,
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M L Entman, and
E P Bornet, and
A J Barber, and
A Schwartz, and
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July 1980,
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M L Entman, and
E P Bornet, and
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A Schwartz, and
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June 1975,
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M L Entman, and
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January 1983,
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M L Entman, and
E P Bornet, and
A J Barber, and
A Schwartz, and
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D C Lehotay, and
L A Bricker
September 1977,
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M L Entman, and
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G S Levey, and
D C Lehotay, and
L A Bricker
January 1996,
Zeitschrift fur Naturforschung. C, Journal of biosciences,
