alpha-chymotrypsin and Hypertrophy

Topics: Animals; Arachis; Chymotrypsin; Digestion; Drug Stability; Fabaceae; Glycine max; Growth; Hot Temperature; Humans; Hypertrophy; Lectins; Pancreas; Plant Lectins; Plant Proteins; Plant Proteins, Dietary; Plants, Medicinal; Protease Inhibitors; Trypsin Inhibitors

The role of exogenous and endogenous cholecystokinin has been studied in the process of pancreatic regeneration after acute pancreatitis. A mild form of pancreatitis was induced in rats by subcutaneous cerulein at 12 micrograms.kg-1, three times a day for 2 days. After 3 days of rest, the cerulein-treated rats were divided into four groups: rats with acute pancreatitis fed 20% casein, who received no treatment; rats fed 50% casein; rats fed 20% casein supplemented with 1% soybean trypsin inhibitor (SBTI); and rats fed 20% casein who received 1 microgram.kg-1 of subcutaneous cerulein, three times a day. Controls were fed 20% casein plus saline subcutaneously. Rats were killed after 5, 10, or 20 days of treatment. Pancreatitis resulted in significant decreases in pancreatic weight and contents of protein, amylase, chymotrypsin, RNA and DNA. During the regenerative process, 1 microgram.kg-1 of cerulein increased all parameters to control values within 5 days and induced pancreatic growth thereafter. SBTI restored the pancreas to normal after 10 days with cellular hypertrophy; the 50% casein diet gave a response similar to SBTI without hypertrophy. It can be concluded that cerulein and SBTI can accelerate pancreatic regeneration after an attack of acute pancreatitis.

Topics: Acute Disease; Amylases; Animals; Body Weight; Ceruletide; Cholecystokinin; Chymotrypsin; Drug Therapy, Combination; Glycine max; Hypertrophy; Male; Nucleic Acids; Organ Size; Pancreas; Pancreatitis; Proteins; Rats; Rats, Inbred Strains; Regeneration; Trypsin Inhibitors

This study was an investigation of the role of cholecystokinin (CCK) in the stimulatory action of cholestyramine on rat exocrine pancreas. Postprandial CCK release was significantly enhanced by acute administration of cholestyramine (12.7 +/- 1.8 vs 3.7 +/- 0.5 pmol/L in controls). Over four weeks, rats were fed either regular diet or diet containing 6% cholestyramine, and were treated with the specific CCK receptor antagonist L-364,718 (2 x 0.5 mg/kg body weight/day s.c.) or DMSO (vehicle for the antagonist). Cholestyramine significantly increased pancreatic weight and trypsin and chymotrypsin contents. L-364,718 abolished these effects. Concomitant administration of antagonist and cholestyramine elevated amylase content, compared to controls. CCK levels in fasted animals did not differ between the four groups. The effect of the same dose of L-364,718 on pancreatic enzyme depletion, induced by the protease inhibitor camostate, was studied in a control experiment. A single dose of camostate (200 mg/kg) caused a 44-68% decrease in enzyme content. L-364,718 reversed this effect for all enzymes. We conclude that CCK is the mediator of cholestyramine-induced pancreatic hypertrophy and increase in content of proteases. After long-term administration, the CCK receptor antagonist, in combination with cholestyramine revealed an agonistic effect on individual, pancreatic enzyme content.

Topics: Administration, Oral; Animals; Benzodiazepinones; Cholecystokinin; Cholestyramine Resin; Chymotrypsin; Devazepide; Dimethyl Sulfoxide; DNA; Dose-Response Relationship, Drug; Esters; Gabexate; Guanidines; Hypertrophy; Male; Organ Size; Pancreas; Rats; Rats, Inbred Strains; Receptors, Cholecystokinin; Time Factors; Trypsin; Trypsin Inhibitors

The in vivo effects of epidermal growth factor (EGF) on pancreatic growth and digestive enzyme concentrations were compared with the actions of the pancreatic secretagogue caerulein in the adult rat. EGF (10 micrograms/kg BW) did not alter pancreatic weight or protein content. However, this concentration of EGF inhibited [3H]thymidine incorporation into DNA by 44%, decreased DNA content by 20%, and increased the concentrations of amylase, chymotrypsinogen, and protein by 106%, 232%, and 42%, respectively. Pancreatic acini prepared from EGF-treated rats exhibited a characteristic secretory response to caerulein that was superimposable to that obtained in acini from saline-treated rats. In both groups of acini half-maximal and maximal stimulation of amylase release occurred at approximately 5 pM and 50 pM caerulein, respectively. In contrast to EGF, caerulein (1 microgram/kg BW) increased pancreatic weight by 29% and protein content by 59%, and enhanced [3H]thymidine incorporation into DNA by 70%. Although caerulein increased the concentrations of pancreatic amylase and chymotrypsinogen by 38% and 297%, respectively, pancreatic acini prepared from caerulein-treated rats were less sensitive to the actions of caerulein in vitro when compared with acini from control rats. Indeed, the EC50 was shift from 4.8 pM to 9.8 pM after 4 days of treatment. EGF potentiated the actions of caerulein on pancreatic weight, protein content, and chymotrypsinogen concentration, and prevented the caerulein-induced alteration in the secretory responsiveness of the acinar cell. Conversely, caerulein reversed the inhibitory effect of EGF on thymidine incorporation. These findings suggest that EGF may modulate the trophic effects of certain gastrointestinal hormones, and may participate in the regulation of pancreatic exocrine function in vivo.

Topics: Amylases; Animals; Cell Division; Ceruletide; Chymotrypsin; DNA Replication; Epidermal Growth Factor; Hyperplasia; Hypertrophy; Male; Organ Size; Pancreas; Rats; Rats, Inbred Strains; Reference Values

1. The Bowman-Birk soya-bean trypsin inhibitor (BBTI) begins to cause pancreatic enlargement and increased enzymic activity in the pancreas of chicks after a minimum of 7 d of feeding. 2. The active inhibitory site of BBTI against trypsin is the factor involved in the pancreatic enlargement and increase of pancreatic enzyme activity in chicks.

Topics: Animals; Chickens; Chymotrypsin; Hypertrophy; Kinetics; Male; Pancreas; Trypsin Inhibitor, Bowman-Birk Soybean; Trypsin Inhibitors

Topics: Aging; Amylases; Animals; Body Weight; Cholecystokinin; Chymotrypsin; DNA; Hyperplasia; Hypertrophy; Lipase; Organ Size; Pancreas; Proteins; Rats; RNA; Stimulation, Chemical

Topics: Amylases; Animals; Cell Membrane; Chymotrypsin; Enzyme Precursors; Hypertrophy; Male; Nucleic Acids; Pancreas; Pancreatic Diseases; Proteins; Rats; Trypsin Inhibitors; Trypsinogen

Topics: Animals; Chymotrypsin; Ethanol; Glycine max; Growth; Hot Temperature; Hypertrophy; Intestine, Small; Male; Methionine; Pancreatic Diseases; Poultry; Proteins; Rats; Trypsin Inhibitors

Topics: Chymotrypsin; Glossopharyngeal Nerve; Hypertrophy; Neurophysiology; Papain; Parasympathetic Nervous System; Peptide Hydrolases; Pharmacology; Rats; Reflex; Research; Submandibular Gland; Sympathectomy; Taste; Taste Buds; Trypsin

Topics: Body Weight; Body Weights and Measures; Chymotrypsin; Diet; Hematologic Tests; Hyperplasia; Hypertrophy; Pancreatic Extracts; Pancreatin; Peptide Hydrolases; Pharmacology; Rats; Research; Submandibular Gland; Trypsin

Topics: Autonomic Nervous System; Body Weight; Chymotrypsin; Ganglia; Ganglia, Autonomic; Hypertrophy; Pancreatic Extracts; Pancreatin; Physiology; Rats; Research; Salivary Gland Diseases; Submandibular Gland; Trypsin