In vivo effects of pancreozymin, secretin, vasoactive intestinal polypeptide and pilocarpine on the levels of cyclic AMP and cyclic GMP in the rat pancreas

Robberecht, Patrick; Deschodt-Lanckman, M; Neef, Philippe De; Borgeat, Pierre; Christophe, Jean

doi:10.1016/0014-5793(74)80986-5

Cited by 60 publications

(17 citation statements)

References 23 publications

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“…Temporally, Ca2+ efflux was associated with a rise in cyclic GMP levels in pancreatic tissue (Christophe, Frandsen, Conlon, Krishna & Gardner, 1976). The rise in cyclic GMP in pancreatic tissue in vivo following CCK-PZ and pilocarpine administration suggested that cyclic GMP may be an essential link in stimulus-secretion coupling (Robberecht et al 1974). Results obtained in vitro confirmed these observations (Albano, Bhoola & Harvey, 1976;Christophe et al 1976;Haymovits & Scheele, 1976).…”

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Calcium and cyclic nucleotide interaction in secretion of amylase from rat pancreas in vitro.

Singh¹

1979

The Journal of Physiology

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SUMMARY1. Interaction of Ca2+ and cyclic nucleotides in stimulus-secretion coupling in rat pancreas in vitro was studied utilizing the divalent cation inophore A23187. phosphodiesterase inhibitors, cyclic nucleotides and cholera toxin.2. Amylase secretion was increased by the ionophore in the presence of extracellular Ca2+ in a dose-dependent fashion. Activation of CCK-PZ receptors simultaneously with induction of amylase secretion by A23187 did not alter amylase secretion whereas theophylline or caffeine had effects additive to A23187. Dibutyryl cyclic AMP potentiated the effect of ionophore whereas dibutyryl cyclic GMP had no effect on basal or ionophore-induced amylase secretion. Cholera toxin by itself did not effect amylase secretion whereas it potentiated the effect ofionophore.3. A23187 increased bidirectional fluxes of 45Ca and increased efflux of 45Ca in a fashion similar to CCK-PZ. Theophylline did not alter basal efflux of 45Ca. Dibutyryl cyclic AMP increased the basal efflux of 45Ca whereas, cholera toxin, dibutyryl cyclic GMP and sodium butyrate had no effect.4. Theophylline increased basal cyclic AMP levels with a peak effect observed at 5 min. Combination of theophylline and ionophore did not lead to an increase in levels of cyclic AMP greater than that observed with theophylline alone. Cholera toxin increased cyclic AMP levels at 30 and 60 min of incubation.5. Ionophore and CCK-PZ increased tissue cyclic GMP levels significantly greater than that obtained with theophylline alone. This effect was dependent on extracellular Ca2+. The effect of ionophore on tissue levels of cyclic GMP could be dissociated from its effect on 45Ca efflux and amylase secretion.6. It is concluded from these studies that Ca2+ plays a predominant role in regulating amylase secretion with interactions occurring between Ca2+ and cyclic AMP and Ca2+ and cyclic GMP. It appears that by themselves cyclic AMP and cyclic GMP do not play a significant role in regulating enzyme secretion.

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“…cells (Kulka & Sternlicht, 1968;Robberecht & Christophe, 1971; Deschodt-Lanckman, De Neef, Borgeat & Christophe, 1974). Using dissociated acinar cells, it was reported that pancreatic secretagogues acted by increasing the rate of Ca2+ transfer into the cells (Kondo & Schulz, 1976).…”

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Calcium and cyclic nucleotide interaction in secretion of amylase from rat pancreas in vitro.

Singh¹

1979

The Journal of Physiology

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“…The involvement of cyclic nucleotides in this process is still controversial, however the bulk of evidence suggests that cyclic adenosine-3',5'-monophosphate (cyclic AMP) is not involved in either acetylcholine or pancreozymin-stimulated enzyme secretion (Benz, Eckstein, Matthews & Williams, 1972;Case & Scratcherd, 1972;Heisler et al, 1972). It has been suggested that cyclic GMP mediates the effects of acetylcholine in some tissues (Goldberg, O'Dea & Haddox, 1973) including the exocrine pancreas (Robberecht, Deschodt-Lanckman, De Neef, Borgeat & Christophe, 1974) but the evidence that this nucleotide plays a role in secretion from this tissue is preliminary. Heisler et al (1972) reported that dibutyryl cyclic AMP was itself a poor secretagogue in the rat exocrine pancreas but that it potentiated the secretory effect of carbachol.…”

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THE EFFECT OF DIBUTYRYL CYCLIC ADENOSINE‐3′,5′‐MONOPHOSPHATE ON PROTEIN SECRETION FROM THE RAT EXOCRINE PANCREAS in vitro

Fast

Tenenhouse

1976

British J Pharmacology

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1 The mechanism by which dibutyryl cyclic adenosine-3'-5'-monophosphate (dibutyryl cyclic AMP) potentiates the secretory effect ofcarbachol in rat exocrine pancreas was investigated. 2 Dibutyryl cyclic AMP potentiated the secretory effect of carbachol only at carbachol concentrations 5 10-7 mol/l; was independent of carbachol at concentrations > 10-7 mol/l and was inversely proportional to extracellular [Ca2+].

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“…The secretory mechanisms are not fully understood but they appear to involve calcium movements [l, 21 and transient increases in cyclic GMP [3,4,5]. Cyclic AMP has been implicated in the process [6,7].…”

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The Interaction of Caerulein with the Rat Pancreas. 1. Specific Binding of [3H]Caerulein on Plasma Membranes and Evidence for Negative Cooperativity

et al. 1978

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1. The binding of [3H]caerulein (a stable, biologically active labeled analog of cholecystokininpancreozymin) to semi-purified rat pancreatic plasma membranes was investigated. The binding was dependent on time and temperature, as well as saturable, specific and reversible. This process was pH-dependent and optimal at pH 7.0. Cysteine and serine residues in plasma membranes were of importance for binding. Mg2 ' favored the binding. The acceleration of the dissociation of [3H]caerulein in the presence of an excess of native caerulein suggests that binding was characterized by a negative cooperativity. The fast dissociation state evoked by a high degree of occupancy by caerulein was inhibited by lowering the temperature, by decreasing the pH, or by the presence of wheat germ agglutinin.

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In vivo effects of pancreozymin, secretin, vasoactive intestinal polypeptide and pilocarpine on the levels of cyclic AMP and cyclic GMP in the rat pancreas

Cited by 60 publications

References 23 publications

Calcium and cyclic nucleotide interaction in secretion of amylase from rat pancreas in vitro.

Calcium and cyclic nucleotide interaction in secretion of amylase from rat pancreas in vitro.

THE EFFECT OF DIBUTYRYL CYCLIC ADENOSINE‐3′,5′‐MONOPHOSPHATE ON PROTEIN SECRETION FROM THE RAT EXOCRINE PANCREAS in vitro

The Interaction of Caerulein with the Rat Pancreas. 1. Specific Binding of [3H]Caerulein on Plasma Membranes and Evidence for Negative Cooperativity

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