trypsinogen and Body-Weight

The objectives were to evaluate the effects of standardized ileal digestible (SID) His:Lys ratio above the current NRC requirement on growth performance, intestinal health, and mobilization of His-containing proteins, including hemoglobin, carnosine, and trypsinogen, in nursery pigs from 7 to 11 kg body weight (BW). Forty pigs (26 d of age; initial BW of 7.1 ± 0.5 kg) were allotted to 5 dietary treatments based on a randomized complete block design with sex and initial BW as blocks. Dietary treatments were supplemented with varying SID His to Lys ratios of 26%, 32%, 38%, 43%, and 49% and fed to pigs for 14 d (SID Lys = 1.22%). Feed intake and BW were recorded at d 0, 7, and 14 to measure growth performance. Blood samples were collected on d 12. Pigs were euthanized on d 14 to collect pancreas, longissimus dorsi muscles, mid-jejunum, and jejunal mucosa. Data were analyzed using the Proc Mixed of SAS. Growth performance was not affected, whereas varying SID His to Lys ratio affected hemoglobin (P < 0.05, max: 12 g/dL at 36%), immunoglobulin A (IgA, P < 0.05, min: 1.25 μg/mg at 35%) in jejunal mucosa, villus height (P = 0.065, max: 536 μm at 40%) in jejunum, trypsinogen (P = 0.083, max: 242 pg/mg at 41%) in pancreas, and carnosine (P = 0.051, max: 4.7 ng/mg at 38%) in muscles. Varying SID His to Lys ratios linearly increased (P < 0.05, from 1.95 to 2.80 nmol/mg) protein carbonyl in muscles and decreased (P < 0.05, from 29.1% to 26.9%) enterocyte proliferation. In conclusion, SID His to Lys ratio between 35% and 41% in diets fed to nursery pigs at 7 to 11 kg enhanced intestinal health and maximized concentrations of His-containing proteins, indicating that His-containing proteins are effective response criteria when determining His requirement.. Histidine is an essential amino acid for protein synthesis, but it also plays a vital role in the metabolic system of pigs. An accurate assessment of His requirement provides pivotal information for efficient growth and health of pigs. Growth performance and plasma His concentration have been used to assess His requirement, but they may not be the effective parameters due to the contribution of His from mobilization of His-containing proteins, such as hemoglobin, carnosine, and pancreatic enzymes. Hemoglobin is a transport protein and the main component in red blood cells, enabling oxygen transport throughout the body. Most carnosine is stored in muscles at 3 to 4 g/kg wet weight and has antioxidative effects to prevent cells from oxidative damages. In addition, His has a critical role in serine peptidases as a part of the catalytic triad. In this study, growth performance did not respond to His deficiency due to the compensation of His from His-containing proteins and potentially due to a short experimental period. Standardized ileal digestible His to Lys ratio between 35% and 41% maximized concentrations of His-containing proteins and enhanced intestinal health in pigs at 7 to 11 kg body weight. This study indicated that hemoglobin, carnosine, and trypsinogen are effective response criteria when determining His requirement.

Topics: Animal Feed; Animal Nutritional Physiological Phenomena; Animals; Body Weight; Carnosine; Diet; Digestion; Histidine; Ileum; Lysine; Swine; Trypsinogen

Many patients with cystic fibrosis are malnourished at the time of diagnosis. Whether newborn screening and early treatment may prevent the development of a nutritional deficiency is not known.. We compared the nutritional status of patients with cystic fibrosis identified by neonatal screening or by standard diagnostic methods. A total of 650,341 newborn infants were screened by measuring immunoreactive trypsinogen on dried blood spots (from April 1985 through June 1991) or by combining the trypsinogen test with DNA analysis (from July 1991 through June 1994). Of 325,171 infants assigned to an early-diagnosis group, cystic fibrosis was diagnosed in 74 infants, including 5 with negative screening tests. Excluding infants with meconium ileus, we evaluated nutritional status for up to 10 years by anthropometric and biochemical methods in 56 of the infants who received an early diagnosis and in 40 of the infants in whom the diagnosis was made by standard methods (the control group). Pancreatic insufficiency was managed with nutritional interventions that included high-calorie diets, pancreatic-enzyme therapy, and fat-soluble vitamin supplements.. The diagnosis of cystic fibrosis was confirmed by a positive sweat test at a younger age in the early-diagnosis group than in the control group (mean age, 12 vs. 72 weeks). At the time of diagnosis, the early-diagnosis group had significantly higher height and weight percentiles and a higher head-circumference percentile (52nd, vs. 32nd in the control group; P=0.003). The early-diagnosis group also had significantly higher anthropometric indexes during the follow-up period, especially the children with pancreatic insufficiency and those who were homozygous for the deltaF508 mutation.. Neonatal screening provides the opportunity to prevent malnutrition in infants with cystic fibrosis.

Topics: Body Height; Body Weight; Cystic Fibrosis; Humans; Infant; Infant, Newborn; Neonatal Screening; Nutrition Disorders; Nutritional Status; Prospective Studies; Trypsinogen

The objective of this study was to evaluate effects of dietary crude protein (CP) intake on ileal amino acid digestibilities and expression of genes for digestive enzymes in growing and finishing pigs. In Experiment 1, 18 growing pigs (average initial BW = 36.5 kg) were assigned randomly into one of three treatments (n = 6/treatment group) representing normal (18 % CP), low (15 % CP), and very low (12 % CP) protein intake. In Experiment 2, 18 finishing pigs (average initial BW = 62.3 kg) were allotted randomly into one of three treatments (n = 6/treatment group), representing normal (16 % CP), low (13 % CP) and very low (10 % CP) protein intake. In both experiments, diets with low and very low CP were supplemented with crystalline amino acids to achieve equal content of standardized ileal digestible Lys, Met, Thr, and Trp, and were provided to pigs ad libitum. Daily feed intake, BW, and feed/gain ratios were determined. At the end of each experiment, all pigs were slaughtered to collect pancreas, small-intestine samples, and terminal ileal chymes. Samples were used for determining expression of genes for digestive enzymes and ileal amino acid digestibilities. Growing pigs fed the 12 % CP and 15 % CP diets had lower final body weight (P < 0.01) and ADG (P < 0.0001) when compared with pigs fed the 18 % dietary CP diet. Growing pigs fed with the 12 % CP diet showed higher digestibilities for CP (P < 0.05), DM (P < 0.05), Lys (P < 0.0001), Met (P < 0.01), Cys (P < 0.01), Thr (P < 0.01), Trp (P < 0.05), Val (P < 0.05), Phe (P < 0.05), Ala (P < 0.05), Cys (P < 0.01), and Gly (P < 0.05) than those fed the 18 % CP diet. Finishing pigs fed the 16 % CP diet had a higher (P < 0.01) final body weight than those fed the 10 % CP diet. mRNA levels for digestive enzymes (trypsinogen, chymotrypsin B, and dipeptidases-II and III) differed among the three groups of pigs (P < 0.05), and no difference was noted in the genes expression between control group and lower CP group. These results indicated that a reduction of dietary CP by a six-percentage value limited the growth performance of growing-finishing pigs and that a low-protein diet supplemented with deficient amino acids could reduce the excretion of nitrogen into the environment without affecting weight gain.

Topics: Amino Acids; Animal Feed; Animals; Body Weight; Chymotrypsin; Diet, Protein-Restricted; Dietary Proteins; Digestion; Female; Ileum; Male; Swine; Trypsinogen

In this study, we cloned two trypsinogens of the orange-spotted grouper, Epinephelus coioides, and analyzed their structure, expression, and activity. Full-length trypsinogen complementary (c)DNAs, named T1 and T2, were 900 and 875 nucleotides, and translated 242 and 244 deduced amino acid peptides, respectively. Both trypsinogens contained highly conserved residues essential for serine protease catalytic and conformational maintenance. Results from isoelectric and phylogenetic analyses suggested that both trypsinogens were grouped into trypsinogen group I. Both trypsinogens had similar expression patterns of negative relationship with body weight; expression was first detected at 1 day post-hatching (DPH) and exhibited steady-state expression during early development at 1-25 DPH. Both expression and activity levels significantly increased after 30 DPH due to metamorphosis. Grouper larval development is very slow with insignificant changes in total length and body weight before 8 DPH. The contribution of live food to an increase in the trypsin activity profile may explain their importance in food digestion and survival of larvae during early larval development.

Topics: Age Factors; Amino Acid Sequence; Analysis of Variance; Animals; Base Sequence; Body Weight; Cloning, Molecular; Cluster Analysis; Conserved Sequence; DNA Primers; DNA, Complementary; Larva; Molecular Sequence Data; Perciformes; Phylogeny; Real-Time Polymerase Chain Reaction; Reverse Transcriptase Polymerase Chain Reaction; Sequence Analysis, DNA; Trypsinogen

To characterize the time course and physiologic significance of decline in serum immunoreactive trypsinogen (IRT) levels in infants with cystic fibrosis (CF) by mode of diagnosis and genotype, and to examine IRT heritability.. We studied longitudinal IRT measurements in 317 children with CF. We developed statistical models to describe IRT decline. Pancreatic disease severity (Mild or Severe) was assigned using CF genotype and was confirmed in 47 infants through fat malabsorption studies.. Infants with severe disease exhibited IRT decline with non-detectable levels typically seen by 5 years of age. Infants with mild disease exhibited a decline in the first 2 years, asymptomatically approaching a level greater than published norms. IRT and fecal fat were inversely correlated. IRT values in infants with meconium ileus (MI) were significantly lower than newborn-screened infants at birth. The high proportion of shared variation in predicted IRT values among sibling pairs with severe disease suggests that IRT is heritable.. IRT declines characteristically in infants with CF. Lower IRT values in newborns with MI suggest increased pancreatic injury. Furthermore, IRT is heritable among patients with severe disease suggesting genetic modifiers of early CF pancreatic injury. This study demonstrates heritability of a statistically modeled quantitative phenotype.

Topics: Biomarkers; Body Height; Body Weight; Chlorides; Cystic Fibrosis; DNA Mutational Analysis; Fats; Feces; Female; Follow-Up Studies; Genetic Predisposition to Disease; Genotype; Humans; Ileus; Infant, Newborn; Longitudinal Studies; Malabsorption Syndromes; Male; Neonatal Screening; Predictive Value of Tests; Severity of Illness Index; Sweat; Trypsinogen; Vitamins

Type 2 and type 3 inositol 1,4,5-trisphosphate receptors (IP3R2 and IP3R3) are intracellular calcium-release channels whose physiological roles are unknown. We show exocrine dysfunction in IP3R2 and IP3R3 double knock-out mice, which caused difficulties in nutrient digestion. Severely impaired calcium signaling in acinar cells of the salivary glands and the pancreas in the double mutants ascribed the secretion deficits to a lack of intracellular calcium release. Despite a normal caloric intake, the double mutants were hypoglycemic and lean. These results reveal IP3R2 and IP3R3 as key molecules in exocrine physiology underlying energy metabolism and animal growth.

Topics: Amylases; Animals; Body Weight; Calcium; Calcium Channels; Calcium Signaling; Carbachol; Digestion; Eating; Energy Intake; Energy Metabolism; Inositol 1,4,5-Trisphosphate Receptors; Lipase; Mice; Mice, Knockout; Pancreas, Exocrine; Receptors, Cytoplasmic and Nuclear; Saliva; Salivation; Submandibular Gland; Trypsinogen

Heat shock proteins (HSPs) are necessary in the synthesis, degradation, folding, transport, and translocation of different proteins. It is well known that the increased expression of HSPs may have a protective effect against cerulein-induced pancreatitis in rats or against choline-deficient ethionine-supplemented diet model pancreatitis in mice. The aim of this study was to investigate the potential effects of HSP preinduction by cold or hot water immersion on trypsin-induced acute pancreatitis in rats. Trypsin was injected into the interlobular tissue of the duodenal part of the pancreas at the peak level of HSP synthesis, as determined by Western blot analysis. The rats were sacrificed by exsanguination through the abdominal aorta 6 h after the trypsin injection. The serum amylase activity, the tumor necrosis factor-alpha, interleukin-1, and interleukin-6 levels, the pancreatic weight/body weight ratio, and the pancreatic contents of DNA, protein, amylase, lipase, and trypsinogen were measured. A biopsy for histology was taken. Hot water immersion significantly elevated the HSP72 expression, while cold water immersion significantly increased the HSP60 expression. Cold water immersion pretreatment ameliorated the pancreatic edema in trypsin-induced pancreatitis, however this was not due to the HSP60. Hot water immersion pretreatment did not have any effect on the measured parameters in trypsin-induced pancreatitis. The findings suggest that the induction of HSP60 or HSP72 are not enough to protect rats against the early phase of this localized necrohemorrhagic pancreatitis model.

Topics: Amylases; Animals; Antibodies; Antibody Specificity; Blotting, Western; Body Weight; Chaperonin 60; Cold Temperature; Cytokines; Disease Models, Animal; DNA; Heat-Shock Proteins; Hot Temperature; HSP72 Heat-Shock Proteins; Immersion; Lipase; Male; Organ Size; Pancreas; Pancreatitis; Proteins; Rats; Rats, Wistar; Stress, Physiological; Trypsin; Trypsinogen

Heat shock proteins (HSPs) have indispensable functions in the synthesis, degradation, folding, transport, and translocation of intracellular proteins. HSPs are proteins that help cells to survive stress conditions by repairing damaged proteins.. To investigate the potential effects of HSP preinduction by cold-water (CWI) or hot-water immersion (HWI) on sodium taurocholate (TC)-induced acute pancreatitis in rats.. TC was injected into the common biliopancreatic duct of the animals at the peak level of HSP synthesis, as determined by Western blot analysis. The rats were killed by exsanguination through the abdominal aorta 6 hours after the TC injection. The serum amylase activity, the IL-1, IL-6 and TNF-alpha levels, the pancreatic weight/body weight ratio, and the pancreatic contents of DNA, protein, amylase, lipase, and trypsinogen were measured, and a biopsy for histology was taken.. HWI significantly elevated HSP72 expression, whereas CWI significantly increased HSP60 expression. It was demonstrated that CWI pretreatment ameliorated the pancreatic edema and the serum amylase level increase, whereas the morphologic damage was more severe in this form of acute pancreatitis. HWI pretreatment did not have any effects on the measured parameters in TC-induced pancreatitis.. The findings suggest a possible role of HSP60, but not HSP72, in the slight protection in the early phase of this necrohemorrhagic pancreatitis model.

Topics: Amylases; Animals; Body Weight; Chaperonin 60; Cytokines; Disease Models, Animal; DNA; Fever; Heat-Shock Proteins; HSP72 Heat-Shock Proteins; Hypothermia; Lipase; Male; Organ Size; Pancreas; Pancreatitis; Rats; Rats, Wistar; Taurocholic Acid; Trypsinogen

Cells respond to stress by upregulating the synthesis of cytoprotective heat shock proteins (HSPs) and antioxidant enzymes. The aim of this study was to compare the effects of cold (CWI) or hot water immersion (HWI) stress on three different acute pancreatitis models (cholecystokinin octapeptide (CCK), sodium taurocholate (TC), and L-arginine (Arg)). We examined the levels of pancreatic HSP60, HSP72, and antioxidants after the water immersion stress. Male Wistar rats were injected with CCK, TC, or Arg at the peak level of pancreatic HSP synthesis, as determined by Western blot analysis. HWI significantly elevated HSP72 expression and CWI significantly increased HSP60 expression in the pancreas. Water immersion stress decreased the levels of pancreatic antioxidants. CWI and-HWI pretreatment ameliorated most of the examined laboratory and morphological parameters of CCK-induced pancreatitis. CWI pretreatment decreased pancreatic edema and the serum amylase level; however, the morphological damage was more severe in TC-induced acute pancreatitis. Overall, CWI and HWI pretreatment only decreased the serum cytokine concentrations in Arg-induced pancreatitis. CWI and HWI resulted in differential induction of pancreatic HSP60 and HSP72 and the depletion of antioxidants. The findings suggest the possible roles of HSP60 and (or) HSP72 (but not that of the antioxidant enzymes) in the protection against CCK- and TC-induced acute pancreatitis. Unexpectedly, CWI pretreatment was detrimental to the morphological parameters of TC-induced pancreatitis. It was demonstrated that CWI and HWI pretreatment only influenced cytokine synthesis in Arg-induced pancreatitis.

Topics: Acute Disease; Amylases; Animals; Antioxidants; Blotting, Western; Body Weight; Chaperonin 60; Cytokines; Disease Models, Animal; Heat-Shock Proteins; HSP72 Heat-Shock Proteins; Immersion; Lipase; Male; Microscopy, Electron; Organ Size; Pancreas; Pancreatitis; Rats; Rats, Wistar; Sincalide; Stress, Physiological; Trypsinogen

Thyroxine has been shown to play a role in the development of exocrine pancreatic enzymes in neonatal rats.. To further evaluate the regulatory mechanisms for thyroxine in pancreatic development, we examined the changes in the expression of pancreatic enzymes (amylase and trypsinogen) and ornithine decarboxylase (ODC) genes following daily injection of thyroxine for 5 and 10 days to neonatal rats (5 days old).. Total pancreatic proteins and DNA contents as well as the activity of ODC and exocrine enzymes were significantly increased after 5 and 10 days of thyroxine treatment. These increases were associated with parallel alterations (to three to fourfold rise) in steady-state mRNA levels of both amylase and trypsinogen. In contrast, thyroxine only produced a 57-68% increase in steady-state ODC mRNA levels.. These data suggest that thyroxine stimulated the express of amylase and trypsinogen genes partly due to increased transcriptional rate and/ or decreased mRNA turnover. Thyroxine also stimulated ODC gene expression. However, the stimulatory mechanisms may involve transnational or posttranslational regulation of ODC and are independent of thyroxine effects.

Topics: Amylases; Animals; Animals, Newborn; Body Weight; Female; Gene Expression; Ornithine Decarboxylase; Pancreas; Pregnancy; Rats; Rats, Sprague-Dawley; RNA, Messenger; Thyroxine; Trypsinogen

The present study was performed to examine the effect of ageing on pancreatic hyperplasia observed after proximal small bowel resection (PSBR). Young and old Wistar rats were randomly assigned to two groups, which underwent either an approximate 90% PSBR or a jejunal and ileal transection (TRC). One week after the operation, the pancreatic wet weight and the protein, DNA and RNA content of the pancreas were all significantly higher in young PSBR rats than in young TRC rats. However, no differences were seen in the old rat groups. Plasma enteroglucagon levels were elevated in both young and old PSBR rats, but the ratio of increase between the PSBR and TRC groups was significantly higher in young rats. Plasma cholecystokinin and gastrin levels did not increase after PSBR in either the young or old rats. These findings suggest that pancreatic hyperplasia observed after PSBR is attenuated by ageing, probably due to an insufficient increase in plasma enteroglucagon levels.

Topics: Aging; Amylases; Animals; Body Weight; Cholecystokinin; DNA; Eating; Gastrins; Glucagon-Like Peptides; Hyperplasia; Intestine, Small; Lipase; Male; Organ Size; Pancreas; Radioimmunoassay; Rats; Rats, Wistar; RNA; Trypsinogen

The pancreas has been reported as a possible target for FK506 toxicity. This study was conducted to examine the effects of FK506 on the structure and function of pancreatic acinar cells.. Male Sprague-Dawley rats received an intramuscular injection of saline or FK506, and pancreatic acini were isolated on the day of sacrifice.. FK506 caused a time-dependent suppression in amylase secretory response to cholecystokinin or carbachol at days 3-14, and increases in amylase and trypsinogen content at days 7-14. The properties of cholecystokinin and scopolamine binding sites in acini were not altered by FK506. Amylase release by A23187 and secretin were decreased by FK506, but those by phorbol ester 12-O-tetradecanoylphorbol-13-acetate, forskolin, 5'-cyclic adenosine monophosphate and vasoactive intestinal peptide were not changed. Increases in cytosolic free calcium concentration induced by cholecystokinin were not changed by FK506. Histologically, a significant increase in cytoplasmic zymogen granules was observed in pancreas from FK506-treated rats.. These data suggest that FK506 induced changes in function and metabolism in pancreatic acinar cells, and these changes might be caused by altering postreceptor loci in stimulus-secretion coupling.

Topics: Amylases; Analysis of Variance; Animals; Atropine; Body Weight; Calcimycin; Calcium; Carbachol; Cholecystokinin; Colforsin; Cytosol; Dose-Response Relationship, Drug; Feeding Behavior; Kinetics; Male; N-Methylscopolamine; Pancreas; Rats; Rats, Sprague-Dawley; Receptors, Cholecystokinin; Reference Values; Scopolamine; Scopolamine Derivatives; Secretin; Sincalide; Tacrolimus; Tetradecanoylphorbol Acetate; Time Factors; Trypsinogen; Vasoactive Intestinal Peptide

The effects of body size and feed intake on N digestibility, pancreas and liver weight, and digestive enzyme activities in male broiler chicks were compared with those induced by dietary tannins. Four groups (SSM, ad lib., pair-fed and young) of sixteen birds each (2 weeks old) were used as experimental animals. They were fed on experimental diets for 4 weeks, except the young group which were fed from age 15 d to 24 d only. Two isonitrogenous and isoenergetic diets with (SSM) or without salseed (Shorea robusta) meal (CONTROL) were used. SSM diet was fed ad lib. to SSM group and control diet was fed ad lib. to ad lib. and young birds and to pair-fed birds at same intake level as SSM birds. Birds fed ad lib. utilized their diet more efficiently than the SSM and pair-fed birds. Digestibility of N, both apparent and ileal, was substantially lower with SSM diet than with the control diet. Each of the treatments induced enlargement of the pancreas (g pancreas/kg live weight) when compared with ad lib. birds. There was no difference between the relative liver weights of SSM and ad lib. birds; however, pair-fed and young birds had comparatively bigger livers. In pair-fed birds the trypsinogen activity of pancreatic tissue (U/g pancreatic tissue) was significantly depressed but there was a significant elevation in trypsinogen (U/kg live weight) activity in SSM birds; again pair-fed birds exhibited the lowest value for this variable.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: alpha-Amylases; alpha-Glucosidases; Animals; Body Weight; Chickens; Diet; Digestion; Dipeptidases; Energy Intake; Enteropeptidase; Intestinal Mucosa; Liver; Male; Nitrogen; Pancreas; Sucrase; Tannins; Trypsin; Trypsinogen

Outputs and turnover times of trypsinogen 2, chymotrypsinogen 1, lipase and amylase were determined in pancreatic juice of growing male Wistar rats at various times during protein restriction (5% protein) followed by balanced refeeding (20% protein). In control rats fed a 20% protein diet, trypsinogen 2, chymotrypsinogen 1 and amylase outputs increased progressively with age, those of lipase remained constant and the turnover times of the four hydrolases were shortened. With time, protein restriction induced the most rapid decrease in trypsinogen 2 output, followed by that of amylase, then by those of trypsinogen 1 and lipase. Compared with controls, protein restriction enhanced specific radioactivity in total proteins and each hydrolase and diminished the enzyme turnover times at the beginning of the experiment. Refeeding returned each hydrolase output to control values, but the turnover times remained shortened to the end of experiment. Pancreatic lobules were isolated from control and protein-depleted rat pancreata after 23 d of dietary treatment. After a pulse of [3H]leucine, lobules were incubated in Krebs-Ringer-bicarbonate-HEPES. Basal and stimulated (50 pmol cholecystokinin/L) secretions of total proteins, amylase and radioactive proteins were measured. Protein restriction resulted in a lower response of acinar cells to cholecystokinin. The reduced ability of cholecystokinin to stimulate secretion may be attributable to a lower number and/or to the reduced affinity of cholecystokinin receptors in acinar cells. Therefore, the observed output and turnover changes during protein restriction could be partly due to an impairment of cholecystokinin efficiency.

Topics: Aging; Amylases; Animals; Body Weight; Dietary Proteins; Food; Food Deprivation; Isoelectric Focusing; Lipase; Male; Pancreas; Rats; Rats, Inbred Strains; Trypsinogen

Adult, male Sprague-Dawley rats weighing initially 185-225 g, were treated with 5, 15, or 50 mg nicotine or placebo 3-week-release pellets by sc implantation, for 1.5, 3, 6 and 12 weeks. These doses of nicotine correspond to infusion rates of 9.9, 29.8, and 99.2 micrograms/h, respectively. At the highest nicotine dose trypsin and chymotrypsin activities were markedly higher in pancreas from 12-week nicotine-treated rats compared with controls. This was associated with a fourfold increase in steady-state amylase mRNA levels in comparison to placebo controls. In addition, secretagogue-stimulated enzyme release from pancreatic acini isolated from rats treated with 50 mg nicotine pellets was significantly higher than controls at 1.5 and 3 weeks and declined below control levels after 12 weeks of treatment. In rats treated with 15-mg nicotine pellets, maximal secretagogue-stimulated enzyme release from isolated acini occurred at 1.5 weeks, declining thereafter to control levels. Electron microscopy of pancreas from rats treated with the 50 mg nicotine dose revealed intracytoplasmic vaculoes appearing after 3 weeks of treatment, and persisting throughout the remaining experimental period. It is concluded that 12-week nicotine treatment results in increased pancreatic enzyme biosynthesis and accumulation of digestive enzymes within the pancreas. This is associated with altered responsiveness to secretagogues and evidence of morphological damage.

Topics: Amylases; Animals; Blotting, Northern; Body Weight; Chymotrypsin; DNA; Dose-Response Relationship, Drug; Male; Nicotine; Organ Size; Pancreas; Proteins; Rats; Rats, Inbred Strains; RNA; Sincalide; Trypsin; Trypsinogen; Vacuoles

Earlier histological studies have demonstrated that copper deficiency results in a selective and progressive atrophy of pancreatic acinar tissue. The present study examined both biochemical and morphological changes of the exocrine pancreas in nutritional copper deficiency. Groups of mature female rats were fed a purified diet either deficient (less than 0.5 micrograms/g) or sufficient (6.2 micrograms/g) in copper for 6 wk. Copper deficiency resulted in distinct ultrastructural changes in acinar cells, including marked variability in zymogen granule content, autophagic vacuoles and dilation of acinar lumen. Pancreatic weight and total DNA, RNA and protein content of the pancreas were similar in both groups of rats, whereas pancreatic amylase, trypsin and chymotrypsin activity was significantly lower in the copper-deficient group. In addition, secretagogue-induced release of these enzymes from dispersed acini isolated from copper-deficient rats was significantly reduced in comparison to enzyme secretion from normal controls. Pancreatic Cu-Zn and Mn superoxide dismutase activity was also found to be significantly lower in the copper-deficient rats than in normal controls. We conclude that nutritional copper deficiency in adult female rats reduces the responsiveness of the pancreas to secretagogues and may increase the susceptibility of the pancreas to oxidative damage.

Topics: Animals; Body Weight; Copper; DNA; Female; L-Lactate Dehydrogenase; Organ Size; Pancreas; Protease Inhibitors; Radioimmunoassay; Rats; Rats, Inbred Strains; RNA; Superoxide Dismutase; Trypsinogen

The activation of zymogen proteases and lysosomal enzyme cathepsin B in the pancreas was investigated in cerulein-induced pancreatitis in rats. Acute pancreatitis was induced by two intraperitoneal injections of 40 micrograms/kg of body weight of cerulein at intervals of 1 h. After the first cerulein injection, the active trypsin and elastase contents in the pancreas tissues significantly increased, and reached the highest level at 3 h after the first injection, followed by peaks at 5 h in the serum amylase and lipase levels and the pancreas wet weight. Cathepsin B contents in pancreas tissues showed a parallel increase with active zymogen enzymes during the first 3 h of pancreatitis. These findings may suggest that the intracellular activation of trypsinogen is an important step in the development of cerulein-induced acute pancreatitis and that cathepsin B plays a role in the activation of trypsinogen in pancreatic acinar cells.

Topics: Amylases; Animals; Body Weight; Cathepsin B; Ceruletide; Enzyme Precursors; Lipase; Lysosomes; Male; Pancreas; Pancreatic Elastase; Pancreatitis; Peptide Hydrolases; Rats; Rats, Inbred Strains; Trypsin; Trypsinogen

To determine the effect of riboflavin deficiency on the rat pancreas, one-third of a group of rats was fed a purified riboflavin-sufficient diet ad libitum and two-thirds were fed isocaloric amounts of riboflavin-deficient diet for 13 wk; one-half of the latter group was replenished with daily intraperitoneal injections of riboflavin for the last 3 wk. Body weight, pancreas weight, DNA, protein, amylase, chymotrypsinogen, and trypsinogen decreased in riboflavin-deficient animals. In vitro basal secretion of chymotrypsinogen decreased and basal and bethanechol-stimulated secretions of trypsinogen increased in riboflavin-deficient rats. These changes were considered to be caused by relative inanition resulting from decreased food consumption. On replenishment of riboflavin, amylase content reverted to that of animals fed ad libitum whereas increases in body weight, pancreas weight, DNA, protein, chymotrypsinogen, and trypsinogen were not statistically significant. Both basal- and bethanechol-stimulated secretions of chymotrypsinogen increased. These data indicate that riboflavin deficiency, which commonly accompanies chronic alcoholism, may contribute to the pancreatic injury in chronic alcoholism.

Topics: Amylases; Animals; Bethanechol; Bethanechol Compounds; Body Weight; Chymotrypsin; DNA; Male; Organ Size; Pancreas; Proteins; Rats; Rats, Inbred Strains; Riboflavin Deficiency; Trypsinogen

Starving of rat pups at the 5th or 10th day of life for three days led to lower body and pancreatic weights compared to age-matched controls. When compared to the weights before fasting, only the 5-day-old pups showed increases in pancreatic protein and DNA contents despite food deprivation. Pancreatic acinar responsiveness to carbachol stimulation was not affected. Accumulations of amylase and lipase in the pancreas of the rat pups were increased by fasting, with an accompanied surge in the level of serum corticosterone. In 10-day-old rat pups, injection with aminoglutethimide (AG), a drug which suppresses steroidogenesis, prevented the enzymatic increases and concomitantly suppressed the serum total corticosterone levels at 12 and 24 hr after the onset of fasting. These results strongly support the role of corticosterone in the modulation of the pancreatic adaptation to food deprivation in the suckling rat.

Topics: Aminoglutethimide; Amylases; Animals; Animals, Newborn; Body Weight; Carbachol; Cells, Cultured; Corticosterone; DNA; Lipase; Microbial Collagenase; Organ Size; Pancreas; Proteins; Rats; Rats, Inbred Strains; Starvation; Trypsinogen

The effects of aging upon pancreatic digestive enzymes were studied in 27- and 3-month-old Fischer 344 rats. Mean pancreatic weight, protein and DNA concentration and content, and protein-DNA ratios did not differ in the two groups of animals. Pancreatic amylase concentration was reduced by 41% and lipase concentration was increased by 29% in the aging animals, whereas, trypsinogen concentrations did not differ. Young and aging rats were fed diets enriched with fat (72%) or sucrose (75%) for seven days to define whether the different enzyme contents were intrinsic to the aging process or adaptable. In young, but not in aging rats, lipase concentration increased 25% during high fat compared to high sucrose diet feeding. High starch diet feeding induced a 26% increase in amylase in young rats but not in the old. Trypsinogen concentration was unaffected by dietary manipulation. Jejunal enteropeptidase concentration was modestly reduced in the aging rat. Postprandial luminal concentrations of trypsin and amylase did not differ in the two groups. Thus, aging may induce modest changes in pancreatic digestive enzymes and in jejunal enteropeptidase which are unlikely to be physiologically important. However, the pancreas of aging rats does not adapt to changes in dietary intake as well as young rats.

Topics: Aging; Amylases; Animals; Body Weight; Dietary Fats; Enteropeptidase; Jejunum; Lipase; Male; Pancreas; Rats; Rats, Inbred F344; Sucrose; Trypsinogen

To determine the effect of niacin deficiency on pancreas, rats were fed a standard rat chow ad libitum or an equal amount of a niacin-deficient or niacin-sufficient diet in the first experiment, or of a niacin-tryptophan-deficient or niacin-tryptophan-sufficient diet in the second experiment. Niacin deficiency decreased tissue chymotrypsinogen and trypsinogen content; amylase, chymotrypsinogen, and trypsinogen concentration; and basal secretion of total protein. Niacin-tryptophan deficiency decreased body weight, pancrease weight, and content of DNA, protein, amylase, lipase, chymotrypsinogen, and trypsinogen. Secretion of amylase and trypsinogen was increased. These studies indicate that niacin and niacin-tryptophan deficiency alter digestive-enzyme content and secretion, probably due to metabolic aberrations that result in an altered redox state of the acinar cell.

Topics: Amylases; Animals; Body Weight; Chymotrypsinogen; DNA; Lipase; Male; Niacin; Organ Size; Pancreas; Proteins; Rats; Rats, Inbred Strains; Trypsinogen; Tryptophan

Chronic reserpine treatment of adult rats results in the accumulation of pancreatic enzymes and reduction of their discharge. These changes are reminiscent of those in cystic fibrosis. Since the majority of cystic fibrosis patients have their pancreatic dysfunction manifested in childhood, we studied chronic reserpine treatment in rat pups. Four-day-old rat pups were given reserpine (50 micrograms/kg intraperitoneally) or vehicle daily until sacrifice. The reserpine group showed significant decreases in body weights at 14 and 21 days of age. Pancreatic weights were also decreased but were of normal weight or increased when normalized against body weights. At 14 and 21 days of age, pancreatic concentrations of amylase, lipase, and trypsinogen showed no difference between reserpine and control pups. At both ages, pancreatic contents of all three enzymes were generally less in the treated pups, but were found to be similar when corrected for body weights. Hydrocortisone treatment of 14-day-old pups caused precocious accumulation of pancreatic enzymes in both reserpine and control groups. Intestinal contents of lipase, trypsin, and amylase were decreased in the reserpine pups at 14 days of age and reached a more significant level at 21 days of age; these data suggest a decrease in the secretion of pancreatic enzymes. Dispersed acini from 14-day-old pups showed a reduced capacity to release amylase as stimulated by carbachol or the octapeptide of cholecystokinin. The results suggested that chronic reserpine treatment of pups in the suckling period did not cause significant disturbance of the developmental accumulation of pancreatic enzymes. A definite inhibition of exocrine secretion was found with reserpine treatment.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Amylases; Animal Population Groups; Animals; Animals, Suckling; Body Weight; Carbachol; Female; Hydrocortisone; Lipase; Pancreas; Rats; Rats, Inbred Strains; Reserpine; Sincalide; Trypsinogen

Pancreatic development was studied in rats 17-28 days of age. Control pups, weaned naturally at 21-24 days showed a gradual increase in body weight, pancreatic weight, total DNA and protein content with age. Pups weaned at 17 days showed a transient increase in pancreatic weight and protein content only at day 22; at no time did they show a difference in either DNA content or body weight. Pups nursed up to 25 days of age had a smaller body weight, but had DNA and protein content similar to control rats. Control pups showed gradual increases in lipase and trypsinogen with a sharp increase in amylase between days 22 and 25. Pups weaned at 17 days showed a precocious increase in trypsinogen and a sharp increase in amylase between days 19-22, but an immediate decrease in lipase which eventually returned to the control level at day 28. Pups nursed beyond the weaning stage showed an increase in lipase and trypsinogen but no sharp increase in amylase. A significant increase in all pancreatic enzymes, pancreatic mass, pancreatic DNA and protein content was seen in all groups of rats irrespective of their diet. The results suggest an inherent biological program as a basic control of pancreatic ontogeny with diet playing a modifying role.

Topics: Aging; Amylases; Animals; Body Weight; Lipase; Organ Size; Pancreas; Rats; Rats, Inbred Strains; Trypsinogen; Weaning

Pancreatic secretion has been studied in dogs in basal and postprandial conditions, as nearly physiological as possible. When pancreatic juice was excluded from the duodenum pancreatic secretion was not raised, compared with secretion during the return of juice to the duodenum. In fact, in seven mongrels, returning pancreatic juice led a transient rise in pancreatic secretion. This was not seen in five beagles. These results indicate that dogs do not manifest the feedback control of pancreatic secretion by pancreatic juice observed in other species. Pancreatic secretory activity was determined in 10 dogs after stimulation by food. The highest secretion rates occurred during the initial 60 min. The maximal secretion of protein occurred before the maximal secretion of fluid and bicarbonate. The effect of the meal diminished slowly during the subsequent minutes but did not reach basal levels after 2 h. In physiological conditions, maximal pancreatic secretion of fluid and bicarbonate was about one-fifth and of protein was almost one-seventh of the maximal secretory capacity obtained with secretin and cholecystokinin, respectively. Potential specific activity of trypsinogen was unchanged during the different experimental conditions. Trypsinogen output represented a constant average of 20% of protein output. The interindividual variability of pancreatic secretion rates was reduced when outputs were expressed per kilogram of body weight. In general, a significant positive correlation was found between body weight and the secretory outputs. No differences were observed in the response of mongrel and beagle dogs to a meal.

Topics: Animals; Bicarbonates; Body Weight; Dogs; Feedback; Female; Food; Male; Pancreas; Pancreatic Juice; Proteins; Trypsinogen

Rats were intoxicated over a 32-day period by continuous exposure to an ethanol-enriched atmosphere. Under these conditions, body weights increased up to day 26 and blood ethanol levels increased to approximately 2 g/liter. Pancreatic and hepatic histologies were normal. Amylase levels and total pancreatic protein decreased, while lipase levels rose. These changes appear to be independent of the caloric balance of the diet.

Topics: Alcoholic Intoxication; Amylases; Animals; Body Weight; Chymotrypsinogen; Diet; Ethanol; Humans; Lipase; Liver; Male; Pancreas; Rats; Trypsinogen

Topics: Administration, Oral; Amylases; Animals; Aprotinin; Blood Glucose; Body Weight; Depression, Chemical; Glucose; Injections, Intraperitoneal; Injections, Intravenous; Insulin; Insulin Secretion; Lipase; Male; Organ Size; Pancreas; Radioimmunoassay; Rats; Secretory Rate; Stimulation, Chemical; Time Factors; Trypsinogen

Topics: Amylases; Animals; Blood Glucose; Body Weight; Cattle; Glucose Tolerance Test; Insulin; Intubation, Gastrointestinal; Iodine Radioisotopes; Islets of Langerhans; Lipase; Male; Organ Size; Pancreas; Rats; Stimulation, Chemical; Time Factors; Trypsin Inhibitors; Trypsinogen

Topics: Amino Acids; Amylases; Animal Nutritional Physiological Phenomena; Animals; Blood Glucose; Blood Proteins; Body Weight; Caseins; Cholesterol; Chymotrypsinogen; Deficiency Diseases; Dietary Proteins; Fish Products; Glycine max; Growth; Hemoglobins; Lipase; Pancreas; Plant Proteins; Protein Deficiency; Serum Albumin; Swine; Trypsinogen; Urea

Topics: Amylases; Animals; Animals, Newborn; Body Weight; Chymotrypsinogen; Dietary Carbohydrates; Dietary Fats; DNA; Lipase; Organ Size; Pancreas; Rats; RNA; Trypsinogen; Weaning

Topics: Adaptation, Physiological; Amylases; Animals; Body Weight; Chymotrypsinogen; Diabetes Mellitus, Experimental; Dietary Carbohydrates; Dietary Fats; Dietary Proteins; Fasting; Fatty Acids; Hydrolases; Intestine, Small; Lipase; Male; Nutritional Requirements; Pancreas; Rats; Trypsinogen

Topics: Aging; Amylases; Animals; Animals, Newborn; Body Weight; Chymotrypsin; Diet; Dietary Carbohydrates; Dietary Fats; Dietary Proteins; Hydrolases; Intestine, Large; Intestine, Small; Lipase; Pancreas; Proteins; Rats; Trypsin; Trypsinogen; Weaning

Topics: Amidines; Amylases; Animals; Body Weight; Diet; Growth; Organ Size; Pancreas; Peptide Hydrolases; Rats; Trypsin Inhibitors; Trypsinogen

Topics: Amylases; Animals; Body Weight; Caseins; Chymotrypsin; Dietary Proteins; DNA; Eating; Enzyme Precursors; Male; Nucleic Acids; Pancreas; Peptide Hydrolases; Rats; RNA; Statistics as Topic; Trypsinogen

Topics: Amylases; Animals; Body Weight; Cholecystokinin; Enzyme Precursors; Female; Male; Methacholine Compounds; Organ Size; Pancreas; Parotid Gland; Rats; Secretin; Submandibular Gland; Trypsinogen