Inhibitory influence of amino acids on Secretagogues induced exocrine secretion in isolated perfused rat pancreas.

Harada, Emiko; Habara, Yoshiaki; Kanno, Tomio

doi:10.2170/jjphysiol.34.167

Cited by 12 publications

(5 citation statements)

References 24 publications

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“…In the present study, fresh primary pancreatic acinar cells were used to study effects of leucine dosages on amylase release. The results obtained here shows that leucine inhibits release of α-amylase, which differs from results observed in in vivo ruminant experiments, but similar with the results investigated in isolated perfused rat pancreas [7]. Leucine inhibited the α-amylase release in primary pancreatic acinar cells, and when concentration of leucine increased from 0 to 1.35 mM, the α-amylase release was decreased by 73%.…”

Section: Discussionsupporting

confidence: 88%

“…Leucine not only serves as substrates for protein synthesis but also participates in regulation of some physiological processes. In isolated perfused rat pancreas, leucine infusion could inhibit the secretion of pancreatic enzymes [7]. However, it was reported that duodenum infusion of leucine could increase secretion of pancreatic α-amylase in dairy goat [5] and Holstein cow [6].…”

Section: Discussionmentioning

confidence: 99%

“…It was reported that amino acids could inhibit pancreatic enzyme secretion by reducing Ca 2+ concentration in pancreatic acinar cells [7]. Intracellular Ca 2+ concentration is a direct signal for secretion of digestive enzymes.…”

Section: Discussionmentioning

confidence: 99%

“…In addition to being the basic unit for the synthesis of proteins, peptides, and small peptides, leucine is involved in regulation of gene expression [2], protein expression [3], cell signal pathways [4], and other physiological activities. Recent studies have shown the efficacious roles of leucine on promoting pancreatic juice secretion in dairy goat [5] and cow [6], while reduced secretion of pancreatic enzymes in rat [7]. These inconsistent results indicated that the interactions occurring in vivo complicate the interpretation of experimental data; while in vitro experiment, which uses the primary acinar cells as the model, may help us understand the molecular mechanism of secretory regulation in exocrine pancreas [8].…”

Section: Introductionmentioning

confidence: 99%

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Inhibitory effect of high leucine concentration on α-amylase secretion by pancreatic acinar cells: possible key factor of proteasome

et al. 2018

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The present study aimed to investigate whether leucine affects the pancreatic exocrine by controlling the antisecretory factor (AF) and cholecystokinin receptor (CCKR) expression as well as the proteasome activity in pancreatic acinar cells of dairy calves. The pancreatic acinar cells were isolated from newborn Holstein bull calves and cultured using the Dulbecco’s modified Eagle’s medium/nutrient mixture F12 Ham’s liquid (DMEM/F12). There were six treatments of leucine dosage including 0 (control), 0.23, 0.45, 1.35, 4.05, and 12.15 mM, respectively. After culture for 3 h, the samples were collected for subsequent analysis. As the leucine concentration increased from 0 to 1.35 mM, the α-amylase activity in media decreased significantly (P<0.05), while further increase in leucine concentration did not show any decrease in α-amylase activity. Addition of leucine inhibited (P<0.05) the expression of AF and CCKR, and decreased the activity of proteasome (P<0.05) by 76%, 63%, 24%, 7%, and 9%, respectively. Correlation analysis results showed α-amylase secretion was negatively correlated with leucine concentration (P<0.01), and positively correlated with proteasome activity (P<0.01) and the expression of CCK1R (P<0.01) and AF (P<0.05). The biggest regression coefficient was showed between α-amylase activity and proteasome (0.7699, P<0.001). After inhibition of proteasome by MG-132, low dosage leucine decreased (P<0.05) the activity of proteasome and α-amylase, as well as the expression of CCK1R. In conclusion, we demonstrated that the high-concentration leucine induced decrease in α-amylase release was mainly by decreasing proteasome activity.

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Section: Discussionsupporting

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Inhibitory effect of high leucine concentration on α-amylase secretion by pancreatic acinar cells: possible key factor of proteasome

et al. 2018

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“…The same phenomenon has previously been described by Harada et al ~4 They demonstrated that arginine dose-dependently inhibited stimulated protein release from the isolated perfused rat pancreas. Since exogenous hormones did not produce the same effect, Harada et al considered it unlikely that this inhibitory effect was mediated by pancreatic hormones, but they did not measure hormone secretion in their study 24. While we were able to confirm their finding that …”

Section: Discussionsupporting

confidence: 43%

The islet-acinar axis of the pancreas: Is there a role for glucagon or a glucagon-like peptide?

Schönfeld¹,

Müller

1994

Experientia

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Intravenous glucagon inhibits exocrine pancreatic secretion in vivo, but exogenous glucagon does not affect exocrine secretion in vitro. Recent work, however, suggested that endogenous glucagon may be involved in the regulation of exocrine secretion even in vitro. We therefore investigated the effects of exogenous and endogenous glucagon on exocrine secretion by the isolated perfused rat pancreas in the presence of 1.8 mM glucose. Exogenous glucagon did not affect CCK-stimulated amylase output. 20 mM arginine stimulated glucagon release, but did not affect basal enzyme secretion. CCK-stimulated amylase output, however, was significantly inhibited in the presence of arginine. This inhibitory effect of arginine on exocrine pancreatic secretion could be blocked by glucagon antibodies, but not by nonspecific gammaglobulins. Thus exogenous glucagon failed to affect exocrine pancreatic secretion in vitro, but endogenously released glucagon or a glucagon-like peptide inhibited amylase release in the isolated perfused pancreas. We conclude that glucagon or a glucagon-like peptide may be a mediator in the islet-acinar axis.

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Role of somatostatin in regulation of insular-acinar axis

1993

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Cysteamine is known to deplete somatostatin from pancreatic D cells. In the isolated perfused rat pancreas we investigated its effects on somatostatin and glucagon release as well as exocrine pancreatic secretion in the presence of 1.8 mM glucose. Cysteamine, 10 mM, released somatostatin, but had no effect on CCK-stimulated amylase secretion. Arginine-stimulated glucagon release, however, was significantly inhibited by cysteamine. Concomitantly we still observed stimulation of somatostatin secretion, but also a potentiation of CCK-stimulated amylase secretion. Our results are consistent with a role of somatostatin in the regulation of exocrine pancreatic secretion via its effect on pancreatic A and B cells.

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Inhibitory influence of amino acids on Secretagogues induced exocrine secretion in isolated perfused rat pancreas.

Cited by 12 publications

References 24 publications

Inhibitory effect of high leucine concentration on α-amylase secretion by pancreatic acinar cells: possible key factor of proteasome

Inhibitory effect of high leucine concentration on α-amylase secretion by pancreatic acinar cells: possible key factor of proteasome

The islet-acinar axis of the pancreas: Is there a role for glucagon or a glucagon-like peptide?

Role of somatostatin in regulation of insular-acinar axis

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