Stimulation of Pancreatic Growth by Secretin, Caerulein, and Pentagastrin*

Dembiński, Artur; Johnson, Leonard R.

doi:10.1210/endo-106-1-323

Cited by 177 publications

(54 citation statements)

References 24 publications

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“…The observation is consistent with many similar observations (Griffiths & Moseley, 1980;Mohammed & Ahmed, 1987) , 1967;Johnson & Guthrie, 1974;Solomon et al 1978;Dembinski & Johnson, 1980) have demonstrated the roles of gastrointestinal hormones, particularly cholecystokinin (CCK) and secretin, on pancreatic growth. Pancreatic enlargement similar to that obtained in the present experiment has been reported previously in response to soya-bean trypsin inhibitor (Levison et al 1979) and lectins (Abbey et al 1979;Grant et al 1987).…”

Section: Meansupporting

confidence: 91%

Activities of enzymes of the pancreas, and the lumen and mucosa of the small intestine in growing broiler cockerels fed on tannin-containing diets

1991

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Diets containing vegetable tannins, predominantly hydrolysable gallotannins, at levels of 13.5, 25 and 50 g/kg were fed to growing broiler cockerels to examine their effect on enzymes in the pancreas, the intestinal lumen and the intestinal mucosa. Pancreas weight per unit live weight showed a significant (P < 0.05) increase with increasing level of dietary tannin while that of the liver remained unaffected. Trypsin (EC 3 . 4 . 2 1 .4) and a-amylase (EC 3.2.1.1) activities in the pancreas of birds fed at the highest level of tannins were more than double those from birds fed on a tannin-free control diet. In the intestinal lumen inhibition of trypsin activity increased with increasing level of dietary tannin; a-amylase activity was inhibited at intermediate tannin levels but was restored at the highest level. Dipeptidase (EC 3.4.13.11) and sucrose a-glucosidase (disaccharidase) (EC 3.2.1.48) in the intestinal mucosa were both inhibited by tannins. Growth of the birds and digestibility of nitrogen were adversely affected by the tannin-containing diets.Tannin : Pancreatic enzymes : Brush border enzymes : Cockerel It is well established that tannins are potential protein precipitants (Hagerman & Butler, 1980;Hagerman & Klucher, 1986; Makker et al. 1987) and that they reduce the digestibilities of proteins (Mohammed & Ahnied, 1987) when present in animal feeds. Elevated faecal nitrogen excretion associated with ingestion of tannin-containing feeds is ascribed largely to interactions between either tannins and dietary protein or tannins and digestive enzymes, or both. However, Mitjavilla et al. (1977) concluded that the excess faecal N is mostly a result of mucus hypersecretion.Studies in vitro (Griffiths, 1981 ;Lumen & Salamat, 1980;Horigome et al. 1988) and in vivo (Griffiths & Moseley, 1980; Horigome er al. 1988) have demonstrated the formation of tannin-enzyme complexes. However, adopting a technique in vitro more relevant to the situation in vivo, Mole & Waterman (1987) showed that trypsin retained all its activity in the presence of tannic acid when the system included a substrate protein (bovine serum albumin ; BSA) and glycocholic acid, indicating that under such conditions tannins have a preferential affinity for dietary protein over enzyme protein. In previous work Mole & Waterman (1985) had shown that the formation of complexes between tannins and BSA, used as a substrate for proteolysis, could result in either enhancement or inhibition of proteolysis, or no effect at all depending on the tannin:BSA ratio in the complex.In contrast to what had been reported with rats (Griffiths & Moseley, 1980; Horigome et ul. 1988), tannins were shown to exert no effect on protein digestion by insect herbivores (Martin et ul. 1985(Martin et ul. , 1987 in terms of changes in activities of enzymes in the lumen of the small intestine, in order to provide further insight into the mode of action of dietary tannins. A further aim was to examine the effect of dietary tannins on the activity of membrane-bound enzymes wh...

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Section: Meansupporting

confidence: 91%

Activities of enzymes of the pancreas, and the lumen and mucosa of the small intestine in growing broiler cockerels fed on tannin-containing diets

1991

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“…CCK stimulates proliferation of pancreatic acinar cell in vivo and in vitro (10)(11)(12). Nevertheless, it is unlikely that CCK regulates pancreatic growth during fetal development since the levels 'fCCK peptide expressed in fetal life are negligible ( 13).…”

Section: Introductionmentioning

confidence: 99%

Pancreatic gastrin stimulates islet differentiation of transforming growth factor alpha-induced ductular precursor cells.

Wang¹,

Bonner-Weir²,

Oates³

et al. 1993

J. Clin. Invest.

261

190

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Gastrin is transiently expressed in fetal islets during a critical period of their development from protodifferentiated islet precursors in fetal pancreatic ducts. To examine the possible role of gastrin as an islet cell growth factor, postnatal islet growth was studied in transgenic mice which overexpress gastrin and TGFa in their pancreas. Overexpression of a TGFa transgene causes metaplastic ductules containing numerous insulin expressing cells that resemble protodifferentiated precursors of the fetal pancreas. However, islet mass of the TGFa transgenic mice was not increased. Pancreatic overexpression of gastrin from a chimeric insulin/gastrin transgene transcribed from the insulin promoter markedly decreased the TGFa-stimulated increase in pancreatic duct mass. Furthermore, pancreatic coexpression of both gastrin and TGFa significantly increased islet mass in mice expressing both transgenes. These findings indicate that TGFa and gastrin can act synergistically to stimulate islet growth, although neither peptide alone is sufficient. Islet growth may possibly be stimulated through gastrin promoting the differentiation of insulin-positive cells in the TGFa-induced metaplastic ducts. This transgenic study suggests that islet neogenesis can be reactivated in the ductular epithelium of the adult pancreas by local expression of two growth factors, gastrin and TGFa. (J. Clin. Invest. 1993. 92:1349-1356

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“…Dietary protein stimulates secretion of the gastrointestinal hormone cholecystokinin (CCK) (15,21), and administration of exogenous CCK induces both growth of the pancreas in vivo (5,11,27) and pancreatic acinar cell division in vitro (22). Moreover, feeding oral trypsin inhibitors causes circulating CCK levels to be chronically elevated and stimulates pancreatic growth in rats (13) and mice (27,35), largely through an increase in cell number (hyperplasia).…”

mentioning

confidence: 99%

CCK-independent mTORC1 activation during dietary protein-induced exocrine pancreas growth

Crozier

Sans

Wang

et al. 2010

American Journal of Physiology-Gastrointestinal and Liver Physi

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JA. CCK-independent mTORC1 activation during dietary proteininduced exocrine pancreas growth. Am J Physiol Gastrointest Liver Physiol 299: G1154 -G1163, 2010. First published August 26, 2010 doi:10.1152/ajpgi.00445.2009.-Dietary protein can stimulate pancreatic growth in the absence of CCK release, but there is little data on the regulation of CCK-independent growth. To identify mechanisms whereby protein stimulates pancreatic growth in the absence of CCK release, C57BL/6 control and CCK-null male mice were fed normal-protein (14% casein) or high-protein (75% casein) chow for 7 days. The weight of the pancreas increased by 32% in C57BL/6 mice and 26% in CCK-null mice fed high-protein chow. Changes in pancreatic weight in control mice were due to both cell hypertrophy and hyperplasia since there was an increase in protein-to-DNA ratio, total DNA content, and DNA synthesis. In CCK-null mice pancreatic growth was almost entirely due to hypertrophy with both protein-to-DNA ratio and cell size increasing without significant increases in DNA content or DNA synthesis. ERK, calcineurin, and mammalian target of rapamycin complex 1 (mTORC1) are activated in models of CCK-induced growth, but there were no differences in ERK or calcineurin activation between fasted and fed CCK-null mice. In contrast, mTORC1 activation was increased after feeding and the duration of activation was prolonged in mice fed high-protein chow compared with normal-protein chow. Changes in pancreatic weight and RNA content were completely inhibited, and changes in protein content were partially abated, when the mTORC1 inhibitor rapamycin was administered during high-protein chow feeding. Prolonged mTORC1 activation is thus required for dietary protein-induced pancreatic growth in the absence of CCK.

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Stimulation of Pancreatic Growth by Secretin, Caerulein, and Pentagastrin*

Cited by 177 publications

References 24 publications

Activities of enzymes of the pancreas, and the lumen and mucosa of the small intestine in growing broiler cockerels fed on tannin-containing diets

Activities of enzymes of the pancreas, and the lumen and mucosa of the small intestine in growing broiler cockerels fed on tannin-containing diets

Pancreatic gastrin stimulates islet differentiation of transforming growth factor alpha-induced ductular precursor cells.

CCK-independent mTORC1 activation during dietary protein-induced exocrine pancreas growth

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