How does cholecystokinin stimulate exocrine pancreatic secretion? From birds, rodents, to humans

Wang, Bi Jue; Cui, Zong Jie

doi:10.1152/ajpregu.00131.2006

Cited by 40 publications

(45 citation statements)

References 150 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In freshly isolated rat pancreatic acini, ACh 100 nM induced significant amylase secretion and 1 lM is the maximal-stimulating concentration (Fig. 1a), this is consistent with previous reports (Nathanson et al 1992;Xiao and Cui 2004;Wang and Cui 2007). The dose-response curve for ACh-induced amylase secretion in duck pancreatic acini was rather similar (Fig.…”

Section: Discussionsupporting

confidence: 90%

“…CCK1 receptors, muscarinic receptors also exist in duck pancreatic acinar cells (Guo and Cui 1999;Xiao and Cui 2004;Wang and Cui 2007). CCK is also likely a physiological regulator of duck exocrine pancreatic secretion, but only with simultaneous activation of VPAC receptors (Xiao and Cui 2004;Wang and Cui 2007). However, whether muscarinic cholinergic receptors also play a similar physiological role in avian exocrine pancreatic secretion is not known.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Duck Pancreatic Acinar Cell as a Unique Model for Independent Cholinergic Stimulation–Secretion Coupling

2009

Self Cite

View full text Add to dashboard Cite

This paper investigated the role of acetylcholine (ACh) in physiological regulation of amylase secretion in avian exocrine pancreas. In the isolated duck pancreatic acini, ACh dose dependently stimulated amylase secretion, with a maximal effective concentration at 10 muM. The cAMP-mobilizing compounds forskolin, vasoactive intestinal peptide (VIP)/pituitary adenylate cyclase activating peptide (PACAP) receptor (VPAC) agonists PACAP-38 and PACAP-27 had no effect on the dose-response curve. ACh dose dependently induced increases in cytosolic Ca(2+) concentration ([Ca(2+)]( c )), with increasing concentrations transforming oscillations into plateau increases. Forskolin (10 muM), PACAP-38 (1 nM), PACAP-27 (1 nM), or VIP (10 nM) alone did not stimulate [Ca(2+)]( c ) increase; neither did they modulate ACh-induced oscillations, nor made ACh low concentration effective. These data indicate that ACh-stimulated zymogen secretion in duck pancreatic acinar cells is not subject to modulation from the cAMP signaling pathway; whereas it has been widely reported in the rodents that ACh-stimulated exocrine pancreatic secretion is significantly enhanced by cAMP-mobilizing agents. This makes the duck exocrine pancreas unique in that cholinergic stimulus-secretion coupling is not subject to cAMP regulation.

show abstract

Section: Discussionsupporting

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Duck Pancreatic Acinar Cell as a Unique Model for Independent Cholinergic Stimulation–Secretion Coupling

2009

Self Cite

View full text Add to dashboard Cite

show abstract

“…CCK also stimulates gallbladder contraction and enhances growth of the exocrine pancreas. Soybean agglutinin stimulates CCK release by opening l-type Ca 2+ channels in cultured rabbit jejunal cells (Wang and Cui, 2007).…”

Section: Discussionmentioning

confidence: 99%

Effect of extruded full-fat soybeans on performance, amino acids digestibility, trypsin activity, and intestinal morphology in broilers

Foltyn¹,

Rada²,

Lichovnikova³

et al. 2013

CZECH J ANIM SCI

View full text Add to dashboard Cite

Th e infl uence of diff erent levels of extruded full-fat soybean (EFFSB) in the diet on growth performance, apparent ileal amino acids digestibility (AIAAD), intestinal morphology, and trypsin activity in digesta of broilers was determined. In the fi rst experiment, two-hundred sixty ROSS 308 male chickens were used to investigate the eff ect of EFFSB on growth performance, intestinal morphology, and trypsin activity in the digesta and AIAAD. Five dietary treatments were used, containing 0, 40, 80, 120, and 160 g/kg of EFFSB. Th e experiment lasted from day 10 till day 38 of age. Th e inclusion of EFFSB at the level of 160 g/kg in the diet signifi cantly (P < 0.05) decreased fi nal body weight (2443 g in 0 group vs. 2093 in 160 group) and worsened feed effi ciency. AIAAD was lower when diet contained more than 40 g/kg EFFSB. But at the level of 160 g/kg AIAAD increased in several amino acids (threonine, isoleucine, leucine, histidine). Trypsin activity increased with increasing EFFSB in the diets. Th ere were no signifi cant (P > 0.05) diff erences in AIAAD between groups 80, 120, and 160. Villus height (groups 0: 966.2; 4: 852.1; 8: 792.6; 12: 836.3; 16: 926.7 μm) and crypt depth (groups 0: 160.1; 4: 134.8; 8: 122.9; 12: 129.5; 16: 134.6 μm) of ileum decreased with inclusion of EFFSB in the diet, but villi/crypt ratio increased. In the second experiment, male chickens ROSS 308 were divided into 4 groups with 2 replicates per 100 chicks each. Th e groups were fed 0, 40, 80, and 120 g/kg of EFFSB. Th e experiment lasted from day 10 till day 38 of age. Final body weight (2594 g in 0 group vs. 2624 g in 120 group) was not signifi cantly (P > 0.05) aff ected by the diet. Th e study showed that EFFSB at the level of 120 g/kg in grower broiler diet had no adverse eff ect on performance.

show abstract

“…Administration of high doses of cholecystokinin (CCK) or its analogue, cerulein, results in the development of pancreatitis that is characterized by increases of serum amylase and lipase activity and an acute necrosis of pancreatic exocrine cells (13). To compare the susceptibility of PACAP-Tg and wild-type mice to the cerulein-induced pancreatitis, the activities of serum amylase and lipase were determined (Fig.…”

Section: Cerulein-induced Secretion Of Amylase and Lipasementioning

confidence: 99%

Over-Expression of Pancreatic Pituitary Adenylate Cyclase–Activating Polypeptide (PACAP) Aggravates Cerulein-Induced Acute Pancreatitis in Mice

Hamagami¹,

Sakurai²,

Shintani³

et al. 2009

J Pharmacol Sci

View full text Add to dashboard Cite

Abstract. Development of human chronic pancreatitis is associated with intrapancreatic accumulation of pituitary adenylate cyclase-activating polypeptide (PACAP) accompanied with an altered inflammatory response (Michalski et al., Am J Physiol Gastrointest Liver Physiol. 2008;294:G50-G57). To investigate the role of pancreatic PACAP in the development of acute pancreatitis, we employed transgenic mice over-expressing PACAP in pancreatic β-cells (PACAP-Tg). In comparison to wild-type mice, PACAP-Tg mice exhibited more severe pathophysiological signs of the cerulein-induced pancreatitis at 12 h, as evidenced by higher serum amylase and lipase levels accompanied by the exacerbation of pancreatic edema, necrosis, and inflammation. Cerulein treatment increased mRNA expression of several proinflammatory cytokines (TNFα, IL-1β, and IL-6) at 12 h with similar magnitude both in wild-type and PACAPTg mice. In addition, the mRNA and protein levels of regenerating gene III β (RegIIIβ), a key factor in the pancreatic response to acute pancreatitis, were up-regulated at 24 h in wild-type mice upon cerulein administration, whereas they were attenuated in PACAP-Tg mice. These data indicate that over-expressed PACAP in pancreas enhances the cerulein-induced inflammatory response of both acinar cells, leading to aggravated acute pancreatitis, which was accompanied by a down-regulation of RegIIIβ, an anti-inflammatory factor.

show abstract

How does cholecystokinin stimulate exocrine pancreatic secretion? From birds, rodents, to humans

Cited by 40 publications

References 150 publications

Duck Pancreatic Acinar Cell as a Unique Model for Independent Cholinergic Stimulation–Secretion Coupling

Duck Pancreatic Acinar Cell as a Unique Model for Independent Cholinergic Stimulation–Secretion Coupling

Effect of extruded full-fat soybeans on performance, amino acids digestibility, trypsin activity, and intestinal morphology in broilers

Over-Expression of Pancreatic Pituitary Adenylate Cyclase–Activating Polypeptide (PACAP) Aggravates Cerulein-Induced Acute Pancreatitis in Mice

Contact Info

Product

Resources

About