M. Gestin

Kinetics of pancreatic exocrine secretion and plasma gut regulatory peptide release in response to feeding in preruminant and ruminant calves.

Pancreatic exocrine secretion and plasma cholecystokinin, gastrin, secretin, and somatostatin concentrations were examined in relation to feeding in 70- to 120-day-old preruminant and ruminant calves. The apparatus used was designed to immediately re-infuse the animals own pancreatic juice and to carry out accurate measurements of the juice flow in real time and to take samples. In the preruminants, pancreatic juice, protein, and trypsin flows increased from 45 min before and until 15 min after the meal and decreased sharply thereafter over a period of 30 min. while protein and trypsin concentrations peaked after feeding. A significant increase in plasma gastrin and cholecystokinin (CCK), a fall in secretin and no change in somatostatin were observed after milk ingestion. By contrast, in the ruminants, feeding had no effect on the pancreatic secretion and on the plasma concentrations of these peptides. Similar and simultaneous patterns of juice flow and secretin, as well as of protein and trypsin concentrations, CCK and gastrin, could support the hypothesis that these gut regulatory peptides play a significant role in the regulation of the pancreatic function. In preruminant calves, the existence of cephalic, gastric and intestinal phases is discussed. In the ruminants, that of the ruminal phase is questionable.

Exogenous CCK and gastrin stimulate pancreatic exocrine secretion via CCK-A but also via CCK-B/gastrin receptors in the calf

Abstract A predominance of the pancreatic cholecystokinin (CCK) receptor of the B/gastrin subtype (CCK-B/G) was reported in calves older than 1 month. Specific CCK-A and CCK-B/G receptor antagonists (SR 27897 and PD 135158, respectively) were used to identify the CCK receptor subtype involved in exogenous CCK- and gastrin-induced exocrine pancreatic responses. Conscious calves (2 months old) with catheterized pancreas, jugular vein and duodenum were used; the pancreatic juice was continuously reinfused. CCK (30 pmol kg–1 min–1, 40 min) evoked an increase in pancreatic juice flow and enzyme secretion, while the same dose of gastrin increased enzyme secretion alone. CCK-induced pancreatic secretion was abolished by SR 27897 (15 nmol kg–1 min–1, 55 min) and reduced by PD 135158 (0.15 nmol kg–1 min–1, 55 min). Gastrin-induced enzyme secretion was reduced by PD 135158 (50% to 90%) and to a lesser extent by SR 27897 (50% to 60%). These results demonstrate that CCK and gastrin in the physiological range stimulate pancreatic exocrine secretion in calves and that these effects are partly mediated by CCK-B/G receptors. Although CCK-A receptors are not predominantly expressed, they seem to play a major role in the response of pancreatic exocrine secretion to CCK.

Gut regulatory peptide levels in bovine fetuses and their dams between the 3rd and 9th months of gestation.

Several gut regulatory peptides were measured by radioimmunoassay between 3 and 9 months of gestation in the plasma of 91 bovine fetuses and their dams, in fetal gastric content and in amniotic fluid. During gestation, plasma peptide concentrations did not change in cows. Likewise, fetal plasma concentrations of cholecystokinin, somatostatin, secretin and vasoactive intestinal polypeptide showed no variation while those of gastrin, pancreatic polypeptide and gastric inhibitory polypeptide increased during the last 6 months. Peptide levels in the fetus were higher than or equal to maternal concentrations. At 8–9 months of gestation, gastrin, CCK, secretin and somatostatin concentrations in amniotic fluid were lower than those measured in fetal gastric content and in maternal and fetal plasma. Therefore, a substantial endogenous endocrine production of regulatory peptides by the fetus probably exists as early as the third month of gestation, accompanied by a release into the lumen of the gut.

Source of dietary protein influences kinetics of plasma gut regulatory peptide concentration in response to feeding in preruminant calves

The kinetics of the peripheral plasma concentrations of eight gut regulatory peptides were examined in response to feeding in preruminant calves. Two experiments were carried out in animals fed milk substitutes either based on milk protein (control diet) or in which casein had been replaced by hydrolyzed fish (fish diet in experiment 1) or whey (whey diet in experiment 2) protein concentrate. In contrast to the control diet, the latter two did not coagulate within the abomasum. No variation was observed in plasma concentrations of gut regulatory peptides during 1-1.4 hr before the morning meal regardless of the nature of the dietary protein. With the control diet, the meal was followed by an increase in cholecystokinin, gastrin and gastric inhibitory polypeptide and a fall in secretin, vasoactive intestinal polypeptide and motilin, whereas no significant change was observed for somatostatin and pancreatic polypeptide. The replacement of casein by protein substitutes did not greatly modify the pattern of plasma responses to feeding, but the prefeeding and postfeeding levels were highly affected. We conclude that the most important characteristic influencing plasma gut peptide concentrations is the ability of dietary protein to clot in the abomasum, consequently determining the pattern of gastric emptying, and that variations appear depending on the origin of protein substitutes in relation to the duodenal content and mainly to the digesta pH.

Method of Measurement of Pancreatic Elastase II Activity and Postnatal Development of Proteases in Human Duodenal Juice and Bovine and Porcine Pancreatic Tissue

A specific method for pancreatic elastase IIactivity analysis was developed. True elastase IIactivity could be discriminated from that of elastase Iand chymotrypsin. The postnatal development of four pancreatic proteases in the duodenal juice ofchildren and in the pancreatic homogenates of calves andpiglets was measured. The study was carried out onpatients without (14 children) and with (5 children) pancreatic insufficiency. Calves and pigletswere either milk-fed or weaned until slaughter atdifferent ages. Profiles of enzyme development wereglobally similar in milk-fed piglets and calves, while in children without pancreatic insufficiency,no significant change was observed between 4 and 168months. In children with pancreatic insufficiency,enzyme activity was low. In animals, elastase II and chymotrypsin activities were maximal at birth,decreased with age, and probably were associated withthe digestion of milk protein. In contrast, elastase Iand trypsin activities increased markedly after weaning in connection with the intake of solidfood.

Bovine Pancreatic Preproelastases I and II: Comparison of Nucleotide and Amino Acid Sequences and Tissue Specific Expression

Clones encoding bovine preproelastases I and II were isolated from a pancreatic cDNA library and were sequenced in order to define the structural characteristics of these enzymes. The bovine 947- and 884-nucleotide preproelastase I and II cDNAs encode proteins containing a signal peptide of the same length (16 amino acids), but with a slightly different number of amino acids for the activation peptide (10 and 12, respectively) and the mature enzyme (240 and 241, respectively). Considering amino acid sequences, each enzyme shares a high degree of identity (76-86%) within species. In contrast, only 55.3% identity is found between bovine elastases I and II. This difference could explain partly their own specificity. Analysis of the expression of the elastases in various bovine tissues demonstrated that they are specifically expressed in high levels in the pancreatic gland. These two approaches (structure and expression) allowed us to characterize the bovine pancreatic elastases I and II.