The Stimulatory Effect of PACAP 38 on Amylase Release in Dispersed Rat Pancreatic Acini.

Kashimura, Junya; Shimosegawa, Tooru; Kikuchi, Yoshihiro; Koizumi, Masaru; Toyota, Takayoshi

doi:10.1620/tjem.164.309

Cited by 11 publications

(8 citation statements)

References 16 publications

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“…We therefore concluded that PACAP27 stimulates pancreatic amylase secretion chiefly via intracellular CAMP. This conclusion is in agreement with our previous results (Kashimura et al 1991(Kashimura et al , 1992) and the observation by Raufman et al (1991) that PACAP38 stimulates pancreatic enzyme secretion via cAMP production.…”

Section: Discussionsupporting

confidence: 94%

“…However, the secretagogues working via intracellular cAMP, including VIP, stimulate the amylase release at a constant rate (Peikin et al 1978;Pandol et al 1983Pandol et al , 1985. The initial burst of PACAP-stimulated amylase secretion demonstrated by our present and former (Kashimura et al 1992) studies indicate that PACAP stimulates exocrine pancreas partly via mechanisms other than the elevation of intracellular cAMP.…”

Section: Discussionsupporting

confidence: 67%

“…Similar to PACAP38 (Kashimura et al 1992), the time course study of amylase secretion stimulated by 1 nM PACAP27 was different from that by 1 nM VIP. The initial amylase secretion by PACAP27 was larger than that by VIP, especially during the first 5 min.…”

Section: Discussionmentioning

confidence: 83%

“…These findings suggest that PACAP might regulate various functions of the pancreas including exocrine secretion. We have previously reported that PACAP38 stimulates intracellular cAMP production and amylase secretion in rat pancreatic acini, and augments CCK-OP-and carbachol-stimulated amylase secretion synergistically (Kashimura et al 1991(Kashimura et al , 1992. Although the specific receptors for PACAP have been identified in the plasma membrane of AR4-2J cells, a cell line of rat pancreatic acinar tumor (Buscail et al 1990; Gourlet et al 1991), the binding sites for PACAP in the normal pancreas have not been identified yet (Lam et al 1990).…”

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confidence: 99%

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The Stimulatory Effects and Binding Characteristics of PACAP27 in Rat Dispersed Pancreatic Acini.

Kashimura

Shimosegawa

Iguchi

et al. 1993

Tohoku J. Exp. Med.

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Pituitary adenylate cyclase activating polypeptide (PACAP) is a recently isolated active peptide of the VIP (vasoactive intestinal peptide) family. Two bioactive forms, PACAP38 and PACAP27, a shorter N-terminal amidated peptide of PACAP38, have been identified. In this study, we explored the action of PACAP27 in rat dispersed pancreatic acini and the characteristics of its binding sites. PACAP27 stimulated amylase secretion and intracellular cAMP production in a dose-dependent manner. Adding 0.5 mM IBMX increased the potency of PACAP27 on the amylase secretion, but did not change the efficacy. The biological action of PACAP27 was mediated via intracellular cAMP as is also the case with PACAP38 or VIP. The time course study, however, revealed that PACAP stimulated the initial amylase secretion greater than VIP, suggesting an involvement of mechanisms other than intracellular CAMP. Binding studies using '25I-PACAP27 and '25I-VIP indicated that the binding sites for PACAP27 interacted with PACAP27 and VIP with a similar affinity. These observations suggested the presence of type II PACAP-binding sites in the normal acini of the rat pancreas which may be functionally coupled with acinar enzyme secretion. PACAP27; pancreas; amylase release; receptor; rat Pituitary adenylate cyclase activating polypeptide 38 (PACAP38) was originally isolated from the ovine hypothalamus.The peptide was named on the basis of its ability to activate adenylate cyclase in rat anterior pituitary cells (Miyata et al. 1989). The N-terminal 28 amino acid-sequence of PACAP38 exhibits 68% structural homology with that of vasoactive intestinal peptide (VIP). PACAP

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Section: Discussionsupporting

confidence: 94%

Section: Discussionsupporting

confidence: 67%

Section: Discussionmentioning

confidence: 83%

mentioning

confidence: 99%

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The Stimulatory Effects and Binding Characteristics of PACAP27 in Rat Dispersed Pancreatic Acini.

Kashimura

Shimosegawa

Iguchi

et al. 1993

Tohoku J. Exp. Med.

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“…In guinea pig pancreatic acini, PACAP-38 alone has a dose-dependent stimulating effect on amylase secretion, with significant stimulation from 1 nM; on top of that, PACAP-38 also shifted CCK dose-response curve to the left by one order of magnitude (28). In rat pancreatic acini, PACAP-38 and VIP alone each stimulated amylase secretion; both enhanced CCKinduced amylase secretion without any shift in maximal CCKstimulating concentration (27).…”

Section: ϫ12mentioning

confidence: 89%

Mutual dependence of VIP/PACAP and CCK receptor signaling for a physiological role in duck exocrine pancreatic secretion

Xiao

Cui

2004

American Journal of Physiology-Regulatory, Integrative and Comp

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Unlike in rodents, CCK has not been established as a physiological regulator in avian exocrine pancreatic secretion. In the isolated duck pancreatic acini, 1 nM CCK was required for stimulation of amylase secretion, maximal effect being achieved at 10 nM; picomolar CCK was without effect. Vasoactive intestinal peptide (VIP)/pituitary adenylate cyclase activating peptide (PACAP) receptor (VPAC) agonists PACAP-38 and PACAP-27 (10-12-10-7 M) alone had no effect, but made picomolar CCK effective. VPAC agonist VIP 10-10-10-7 M stimulated amylase secretion marginally, but made CCK 10-12-10-10 M effective also. PACAP-27 and VIP both shifted the maximal CCK concentration from 10-8 to 10-9 M. This sensitizing effect was mimicked by forskolin. CCK dose dependently induced intracellular Ca2+ concentration ([Ca2+]i) oscillations. PACAP-38 (1 nM), PACAP-27 (1 nM), VIP (10 nM), or forskolin (10 μM) alone did not stimulate [Ca2+]i increase, neither did they modulate CCK (1 nM)-induced oscillations; but when they were added to cells simultaneously exposed to subthreshold CCK (10 pM), calcium spikes emerged. Amylase secretion induced by the simultaneous presence of 10 pM CCK and VPAC agonists was completely blocked by removing extracellular calcium, but the protein kinase C inhibitor staurosporine (1 μM) was without effect. CCK (10 nM)-induced secretion was inhibited by CCK1 receptor antagonist FK480 (1 μM). Gastrin from 10-12 to 10-6 M did not stimulate amylase secretion nor did it (100 nM) induce [Ca2+]i increase. The above data suggest that duck pancreatic acini possess both CCK1 and VPAC receptors; simultaneous activation of both is required for each to play a physiological role.

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PACAP Receptor Signaling

Shioda

Zhou

Ohtaki

et al. 2003

Pituitary Adenylate Cyclase-Activating Polypeptide

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The Stimulatory Effect of PACAP 38 on Amylase Release in Dispersed Rat Pancreatic Acini.

Cited by 11 publications

References 16 publications

The Stimulatory Effects and Binding Characteristics of PACAP27 in Rat Dispersed Pancreatic Acini.

The Stimulatory Effects and Binding Characteristics of PACAP27 in Rat Dispersed Pancreatic Acini.

Mutual dependence of VIP/PACAP and CCK receptor signaling for a physiological role in duck exocrine pancreatic secretion

PACAP Receptor Signaling

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