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Regulation of Digestive Reactions by the Pancreas

Stephen S. Rothman

10.1002/cphy.cp060323

Source: Supplement 18: Handbook of Physiology, The Gastrointestinal System, Salivary, Gastric, Pancreatic, and Hepatobiliary Secretion

Originally published: 1989

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Regulation Of Digestion As A Function of Bulk
2 Regulation of Specific Digestive Reactions
2.1 Effect of Diet on Digestive Enzyme Content of the Pancreas
2.2 Parallel Secretion
2.3 Adaptation Versus Regulation
2.4 Nonparallel Transport
3 Properties of Regulation
3.1 Sensory Input
3.2 Modes of Action
3.3 Regulatory Outcomes
4 Mechanism of Secretion
5 End Products and Zymogen Granules
6 Conclusion
Figure 1. Figure 1.

Secretion of amylase, trypsinogen, chymotrypsinogen, and total protein into cannulated duct of rabbit pancreas in situ as a function of time. Duodenum was perfused for all 6 20‐min periods (time on abscissa), either in absence (•; n = 9, where n = the number of rabbits; values are means ±; SE) or presence (○ n = 6) of glucose. When 5 mM glucose was added, it was added at 60 min (period 3) and removed at 100 min (period 5). For the glucose‐positive series only mean values are presented. None of the glucose‐positive points (○) for different times or measures was significantly different from time‐paired controls (•). [From Rothman 44.]
Figure 2. Figure 2.

Plot of secretion of chymotrypsinogen‐trypsinogen enzyme pair into cannulated duct of rabbit pancreas in situ before (X; periods 1 and 2 in Fig. 1 and after (○; periods 5 and 6) glucose was added to perfusion medium. Solid lines are calculated by linear regression analysis for both groups. Broken line shows that the glucose‐negative data fit a nonlinear function about as well as a linear function. (b.w., body weight; TAMe, p‐toluenesulfonyl‐l‐arginine methyl ester · HCl; ATEe, N‐acetyl‐l‐tyrosine ethyl ester · H2O.) [From Rothman 44.]
Figure 3. Figure 3.

Plot of secretion of amylase‐chymotrypsinogen enzyme pair into cannulated duct of rabbit pancreas in situ before (×; periods 1 and 2 in Fig. 1 and after (○; periods 5 and 6) glucose was added to perfusion medium. Lines are calculated linear regressions. The glucose‐positive intercept is significantly different from the origin. [From Rothman 44.]
Figure 4. Figure 4.

Regression lines calculated from scatter of individual pairs of enzyme measurements for all data points over a 50‐min period after intrapancreatic injection of cholecystokinin (CCK), CCK + Glucose (Glu), or CCK + Lysine (Lys). Each regression line is extended to upper limit of range of values observed for amylase output. In each case, best fit was using an equation y = axb. For CCK, y = 0.44 x0.66, n = 87, where n = the number of independent data points, r = 0.87, P < 0.01; for CCK + Glu, y = 0.66 x0.53, n = 97, r = 0.91, P < 0.01; and for CCK + Lys, y = 0.97 x0.53, n = 97, r = 0.70, P < 0.01. Differences among regressions were assessed by log‐log transformation to approximate linear functions. Each regression differed from the others at P < 0.001. Open circles and error bars represent average peak output (mean ±; SE) for condition indicated by adjacent regression line. [From Grendell et al. 25.]
Figure 5. Figure 5.

Idealized schema showing effect of insulin (I), glucagon (G), and glucose on relative rates of amylase and trypsinogen secretion by rat pancreas in presence of cholecystokinin (CCK). CCK augments output of both enzymes, increasingly favoring amylase secretion as overall enzyme output is increased. Both glucagon and insulin shift CCK curve (CCK alone) toward a more trypsinogen‐dominant function; however, glucagon points (G) tend to fall closer to origin, whereas insulin (I) points tend to be further away. Glucose shifts CCK curve toward a more amylase‐dominant function, and points are found further from the origin. [From Tseng et al. 58.]
Figure 6. Figure 6.

Percent release of α‐amylase (open circles, broken line) and trypsinogen (closed circles, solid line) in experiments with tissue homogenates, as related to concentration of l‐lysine. Both enzymes are measured in the same experiment. Points, means; error bars, SE; n = 3, where n = the number of tissue homogenates. [From Grendell and Rothman 24.]
Figure 7. Figure 7.

Percent release of α‐amylase, trypsinogen, and chymotrypsinogen (CHYMO) due to hexoses in experiments with tissue homogenates. Solid lines, experiments with glucose 1,6‐diphosphate; broken lines, experiments with glucose 1‐phosphate; and dotted broken lines, experiments with glucose 6‐phosphate. Data are means ±; SE (n = 8–18 values from 4–6 separate rat preparations). Glucose 1,6‐diphosphate and glucose 1‐phosphate produced substantial release of amylase (between 1.5 and 2 times control values at 10–20 mM) but only slight release of chymotrypsinogen and trypsinogen (up to ∼10% above control values). Glucose 6‐phosphate was ineffective in causing release of any of the enzymes. [From Niederau et al. 35.]


Figure 1.

Secretion of amylase, trypsinogen, chymotrypsinogen, and total protein into cannulated duct of rabbit pancreas in situ as a function of time. Duodenum was perfused for all 6 20‐min periods (time on abscissa), either in absence (•; n = 9, where n = the number of rabbits; values are means ±; SE) or presence (○ n = 6) of glucose. When 5 mM glucose was added, it was added at 60 min (period 3) and removed at 100 min (period 5). For the glucose‐positive series only mean values are presented. None of the glucose‐positive points (○) for different times or measures was significantly different from time‐paired controls (•). [From Rothman 44.]



Figure 2.

Plot of secretion of chymotrypsinogen‐trypsinogen enzyme pair into cannulated duct of rabbit pancreas in situ before (X; periods 1 and 2 in Fig. 1 and after (○; periods 5 and 6) glucose was added to perfusion medium. Solid lines are calculated by linear regression analysis for both groups. Broken line shows that the glucose‐negative data fit a nonlinear function about as well as a linear function. (b.w., body weight; TAMe, p‐toluenesulfonyl‐l‐arginine methyl ester · HCl; ATEe, N‐acetyl‐l‐tyrosine ethyl ester · H2O.) [From Rothman 44.]



Figure 3.

Plot of secretion of amylase‐chymotrypsinogen enzyme pair into cannulated duct of rabbit pancreas in situ before (×; periods 1 and 2 in Fig. 1 and after (○; periods 5 and 6) glucose was added to perfusion medium. Lines are calculated linear regressions. The glucose‐positive intercept is significantly different from the origin. [From Rothman 44.]



Figure 4.

Regression lines calculated from scatter of individual pairs of enzyme measurements for all data points over a 50‐min period after intrapancreatic injection of cholecystokinin (CCK), CCK + Glucose (Glu), or CCK + Lysine (Lys). Each regression line is extended to upper limit of range of values observed for amylase output. In each case, best fit was using an equation y = axb. For CCK, y = 0.44 x0.66, n = 87, where n = the number of independent data points, r = 0.87, P < 0.01; for CCK + Glu, y = 0.66 x0.53, n = 97, r = 0.91, P < 0.01; and for CCK + Lys, y = 0.97 x0.53, n = 97, r = 0.70, P < 0.01. Differences among regressions were assessed by log‐log transformation to approximate linear functions. Each regression differed from the others at P < 0.001. Open circles and error bars represent average peak output (mean ±; SE) for condition indicated by adjacent regression line. [From Grendell et al. 25.]



Figure 5.

Idealized schema showing effect of insulin (I), glucagon (G), and glucose on relative rates of amylase and trypsinogen secretion by rat pancreas in presence of cholecystokinin (CCK). CCK augments output of both enzymes, increasingly favoring amylase secretion as overall enzyme output is increased. Both glucagon and insulin shift CCK curve (CCK alone) toward a more trypsinogen‐dominant function; however, glucagon points (G) tend to fall closer to origin, whereas insulin (I) points tend to be further away. Glucose shifts CCK curve toward a more amylase‐dominant function, and points are found further from the origin. [From Tseng et al. 58.]



Figure 6.

Percent release of α‐amylase (open circles, broken line) and trypsinogen (closed circles, solid line) in experiments with tissue homogenates, as related to concentration of l‐lysine. Both enzymes are measured in the same experiment. Points, means; error bars, SE; n = 3, where n = the number of tissue homogenates. [From Grendell and Rothman 24.]



Figure 7.

Percent release of α‐amylase, trypsinogen, and chymotrypsinogen (CHYMO) due to hexoses in experiments with tissue homogenates. Solid lines, experiments with glucose 1,6‐diphosphate; broken lines, experiments with glucose 1‐phosphate; and dotted broken lines, experiments with glucose 6‐phosphate. Data are means ±; SE (n = 8–18 values from 4–6 separate rat preparations). Glucose 1,6‐diphosphate and glucose 1‐phosphate produced substantial release of amylase (between 1.5 and 2 times control values at 10–20 mM) but only slight release of chymotrypsinogen and trypsinogen (up to ∼10% above control values). Glucose 6‐phosphate was ineffective in causing release of any of the enzymes. [From Niederau et al. 35.]

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Article Title: Regulation of Digestive Reactions by the Pancreas
 

How to Cite

Stephen S. Rothman. Regulation of Digestive Reactions by the Pancreas. Compr Physiol 2011, Supplement 18: Handbook of Physiology, The Gastrointestinal System, Salivary, Gastric, Pancreatic, and Hepatobiliary Secretion: 465-476. First published in print 1989. doi: 10.1002/cphy.cp060323