• Asian-Australasian Journal of Animal Sciences
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• v.24 no.4
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• pp.500-508
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• 2011

Forty-four Gansu Alpine Fine-wool lambs were used to study changes in the activities of three gastric and five pancreatic enzymes under grazing conditions between 0 and 56 days of age. The lambs were slaughtered on days 0, 3, 7, 14, 21, 28, 42 and 56, the abomasal contents, mucosa and pancreas were immediately removed and placed into liquid nitrogen and enzyme activities were determined. Gastric enzyme (chymosin, pepsin and pregastrc esterase) activities were relatively high at birth, especially chymosin, but decreased quickly between day 0 and 21. The activity of pepsin changed insignificantly with increasing age. There was no significant change in the pancreatic enzyme activities (trypsin, chymotrypsin, ${\alpha}$-amylase, lipase and lactase). The activity of trypsin was relatively higher than that of the other pancreatic enzymes, and lactase activity was low. These ontogenic patterns might be under the control of many gut regulatory peptides, the plasma concentrations of which changed simultaneously. Some gastric and pancreatic enzymes were correlated with plasma concentrations of these gut regulatory peptides.

• The Korean Journal of Pharmacology
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• v.16 no.2 s.27
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• pp.15-24
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• 1980

[${\alpha}$]-Amylase catalyses the hydrolysis of starch, glycogen, and related poly- and oligosac-charide by random cleavage of ${\alpha}$-D-(l-4) glucan linkage. In man large amounts of amylase are secreted into the digestive tract by the salivary and exocrine pancreatic gland, minimal amount being produced also in other tissues. It has been known that ${\alpha}$-amylase exists in multiple molecular forms, isoenzyme which can be separated from each other because of difference in their physicochemical properties. By using various methods, several groups of investigator have separated the many isoenzyme in serum, saliva and pancreatic juice. Furthermore, changes of the normal serum isoenzyme pattern is diagnostically useful even when the total serum enzyme activity is noninformative, such as the clinical use of isoenzyme of serum lactate dehydrogenase. Procarboxypeptidase-A which is one of the pancreatic enzymes is also present as isoenzymes. Four forms of procarboxypeptidase-A haye been found in the bovine enzyme and three forms of the porcine enzyme. In human pancreatic juice four forms of procarboxypeptidase-A isoenzyme were found by isoelectric focusing method. Recently, the so-called isoamylase analysis was developed for the diagnostic use of amylase in pancreatic diseases. In alcohotic patients, the serum concentration of pancreatic isoamylase is subnormal and this lowered activity provides strong evidence for pancreatic exocrine insufficiency. The purpose of this study was to elucidate the variations of the isoenzyme of amylase and procarboxypeptidase-A in serum, saliva and pancreatic juice of the experimental animals. The results are as follow. 1) Three main forms of isoenzyme of amylase by isoelectric focusing were found in pancreatic juice of normal rabbit. However, many new bands were appeared in the pancreatic juice of cholic acid administered animal intravenously while the infusion of cholic acid or elastase into pancreatic duct produced the decrease of number of the fractions on the isoelectric focusing. In the case of serum isoenzyme from normal animal, two major and a few minor isoamylases were observed. By injecting alcohol intravenousely the fractions of serum isoamylase were significantly decreased and in contrary to the pattern in the pancreatic juice the infusion of cholic acid or elastase into pancreatic duct exhitited a significant decrease of the isoenzyme of amylase fractions. In saliva from normal animal three main isoamylase were produced of the administration of alcohol. 2) In the case of procarboxypeptidase-A isoenzyme, two major fractions which have isoelectric point at 6.2 and 6.4 and other two minor bands were observed in the pancreatic juice of normal rabbit. By the treatment of the juice with trypsin, only one band was produced on the isoelectric focusing. No procarboxypeptidase was appeared on the electrofocusing by the infusion of cholic acid or phospholipase A into the pancreatic duct of rabbit. However, a single major fraction of procarboxypeptidase-A was appeared at 3 hr after simple ligation of the pancreatic duct. No significant changes were observed in the juice of the alcohol or cholic acid administered group.

• Archives of Pharmacal Research
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• v.19 no.3
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• pp.201-206
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• 1996

Nitric oxide (NO) is thought to be a second messenger involved in secretion. Upon stimulating pancreatic acinar cells with cholecystokinin-pancreozymin (CCK-PZ), NO formation has been shown to be associated with increased levels of cGMP (Seo et al., 1995). To elucidate the signaling pathway of VIP-induced enzyme secretion, we investigated the NO and cGMP synthesis steps as potential steps where two signal pathways triggered by CCK-PZ and VIP interact. The results obtained in this work provide evidence that increase in pancreatic enzyme secretion by treatment with VIP has no relationship with NOS activity and cGMP level. This conclusion was derived from the following findings that VIP treatment of rat pancreatic tissue increased amylase release as well as protein output in a dose- and time-dependent manner, whereas NOS activity and cGMP synthesis were not affected by VIP treatment as monitored by NOS activity assay and determining cGMP level, which was further confirmed by a NOS-inhibitor study. Consequently, CCK-PZ or VIP increases enzyme secretion in rat pancreatic tissue, but the two hormones are different in their mode of action. Together the results suggest that signaling pathway of VIP-induced enzyme secretion might either bypass the NO and cGMP synthesis steps or lie on a distinct pathway from CCK-PZ-induced pathway.

• YAKHAK HOEJI
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• v.12 no.1_2
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• pp.1-15
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• 1968

The levels of activities of amylase, lipase and trypsin in both the pancreatic tissue and serum of 18 species of vertebrate animals were measured and enzymologically compared with each other. 1) The value of amylase in the pancreas of experimental mammalia has been found decreasing in the order pig, rat, dog, cat, rabbit and cow; that of pancreatic lipase has been found decreasing in the order of pig, dog, cat, rat, rabbit and cow; and that of trypsin has been found decreasing in the order of pig, cow, dog, rat, rabbit. Thus the value of all the above three kinds of enzymes were observed highest in pig, but in cow amylase and lipase were observed lowest while trypsin were observed considerably high. 2) In view of diets, the comparatively high values of pancreatic enzyme were observed in the ommivorous animals such as pig, rat, dog, while the values observed low in the herbivorous animals, such as cow and rabbit. 3) In the bovine, the values were observed moderately high except lipase which were found comparatively low. 4) In the Reptilia and Amphibia such a mud turttle and frog, the values were shown in similar measure with each other, that is, the pancreatic amylase and trypsin were observed considerably high while the lipase was found low. 5) In the species of Reptilia such as a viper and snake, the activities of pancreatic enzymes were not detected. But in the tissue of liver, stomach, activities of the enzymes were found considerably high. Lacertilia animals such as lizard the values of pancreatic enzymes were little observed. 6) In the fish in which the pancreatic tissue is scattered in the liver, the pancreatic enzymes were found in the liver tissue considerably higher than in the other tissues but lower than in the warm-blooded animals, especially the lipase was lower. 7) In generally the values of serum amylase and lipase were observed higher than those of man; and even in the cold-blooded animals in which the values of pancreatic enzymes were shown low or none, the values were also observed high. 8) The above three kinds of pancreatic enzyme values of those experimental animals have shown a tendency of higher degree in higher taxa than in lower taxa according to taxonomical order. 9) In view of tissue, the pancreatic cell was observed large in the mammalian animals such as rat and pig and cytoplasm was also abundantly contained in the acinous cell; and the bovine and the snake haave the pancreatic cells of the similar rosette form the comparatively large acinous cells of long rhombic form in the comparatively large acinous cells of long rhombic form in which the spindle shaped neucleus and the abundant cytoplasm were contained. In the fish the pancreatic cell were found scattered in the liver in which the very large pancreatic islet were found.

• Korean Journal of Poultry Science
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• v.16 no.4
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• pp.219-232
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• 1989

The present study was done to investigate the mechanism of Pancreatic digestive enzyme secretion in response to dietary components in chicks. A simplefied pancreatic juice collection method, useful for a short-term experiment, was developed. By wing vein injection, it was shown that the increased trypsinogen and chymotrypsinogen, while neither other single amino acids nor glucose affected the secretion of enzymes, amylase, trypsinogen and chymotrypsinogen. Cholecystokinin (CCK) had an immediate effect on pancreatic enzyme secretion and this response was in a dose dependent fashion. The injection of CCK seemed to have selective stimulation favoring the secretion of chymotrypsinosen followed by amylase and trypsinogen. Simultaneous injection of single amino acid with CCK increased digestive enzyme secretion to various extents depending on the kind of amino acids whereas the injection of glucose with CCK did not affect when compared with that of CCK'alone. By varying doses, synergetic action of CCK plus amino acid on the secretion of pancreatic digestive enzymes was observed at 0.5mM for Val and 5mM for Arg. A further attempt was made to examine the effect of combined administration of amino acids with CCK on pancreatic enzyme secretion. The injected substances were an AAs mixture and combination of selected amino acids, i.e. Thr＋Phe＋Ile, Thr＋Phe. Thr＋Ile or Phe＋Ile. When increases in enzyme outputs for the first 30 min were compared , it was shown that the responses of three enzymes, amylase, trypsinogen and chymotrypsinogen, brought about by the administration of the AAs mixture was almost entirely accounted for by the combined injection of Thr＋Phe. Thus, it was well demonstrated that CCK and amino acids had a synergetic action on the secretion of a specific pancreatic digestive enzyme depending on a kind of amino acid injected.

• The Korean Journal of Pharmacology
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• v.13 no.2
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• pp.41-48
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• 1977

In 1968, Case et al. first studied the importance of cyclic AMP as an intermediate in the action of secretin and cholecystokinin-pancreozymin and they suggested that the action of secretin, not that of cholecystokinin-pancreozymin, may be mediated through cyclic AMP. Recently Albano et al. reported that in the exocrine pancreas each of the two major physiological functions is modulated a specific cyclic nucleotide, enzyme secretion by cyclic GMP, and fluid and ionic secretion by cyclic AMP. But in pancreas still conflicting results have been reported on the role of cyclic nucleotides in enzyme and electrolyte secretion. In these study, the role of cyclic nucleotides in the exocrine pancreatic secretion was examined. The results are as follows. 1) Very strong stimulation on amylase release from guinea pig pancreatic slice was produced by 1 unit of cholecystokinin-pancreozymin but as compared to that of cholecystokinin-pancreozymin very weak response was observed by 1 unit of secretion or $1\;{\mu}g$ of VIP. 2) Both cholecystokinin-pancreozymin and acetylcholine produced a rapid and marked rise in cyclic GMP as well as cyclic AMP in isolated pancreatic tissue. However, both secretin and VIP failed to alter significantly the basal level of cyclic GMP in pancreatic fragments. 3) Atropine inhibited acetylcholine mediated amylase release, but did not affect the cholecystokinin-pancreozymin response. Furthermore, atropine pretreatment produced a marked inhibitory effect on the increase of tissue cyclic nucleotides induced by cholecystokinin-pancreozymin and acetylcholine. In summary, these results suggest that whereas the pancreatic secretion produced by secretin and VIP is modulated by the formation of cyclic AMP, the pancreatic enzyme secretion in response to cholecystokinin-pancreozymin and acetylcholine is triggered by both cyclic AMP and cyclic GMP.

• Asian-Australasian Journal of Animal Sciences
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• v.21 no.1
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• pp.97-102
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• 2008

Four hundred and forty 1-day-old Arbor Acre broilers were fed commercial starter diets with 0, 250, 750 and 2,250 mg/kg of an alpha-amylase preparation from 1 to 21 days of age to investigate the effects of an exogenous enzyme on growth performance, activities of digestive enzymes in the pancreas and anterior intestinal contents and pancreatic amylase mRNA expression. Body weight gain (BWG) and average daily gain (ADG) increased linearly (p<0.01) with increasing levels of supplementary amylase but feed conversion ratio (FCR) was not affected. There was a negative quadratic change of protease and amylase in the small intestinal contents with the increase of supplementary amylase level. The activity of intestinal trypsin was also increased (p<0.05). Lipase was unaffected by amylase supplementation (p>0.05). The pancreatic protease, trypsin, and lipase were not affected by exogenous amylase levels. Consistent with the tendency for a linear depression of amylase activity, pancreatic ${\alpha}$-amylase mRNA was down-regulated by dietary amylase supplementation. The present study suggested that oral administration of exogenous amylase affected activities of intestinal enzymes and the production of pancreatic digestive enzymes in a dose-dependent manner.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.2
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• pp.117-123
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• 1992

The present study was undertaken in order to elucidate the effects of pretreatment with nicotinamide on changes in serum glucose level, body weight, water consumption, serum insulin concentration, and the activity of pancreatic enzyme in rats treated with streptozotocin (STZ). Histological studies were also carried out to evaluate the effects on pancreatic tissues and Langerhans's islet cells. Nicotinamide pretreatment in STZ diabetic rats inhibited the rise of fasting serum glucose concentration and water consumption. Pretreatment with nicotinamide significantly increased the concentration of serum insulin and body weight changes compared to the STZ-treated group. Pancreatic lipase and trypsin activities were increased, but amylase activity was decreased and pancreatic $\beta$ -cell was destroyed by STZ. Pvetreatment with nicotinamide prevented these STZ-induced changes. These results suggest that nicotinamide pretreatment supresses STZ-induced changes in pancreatic enzymes by preventing $\beta$-cell destruction and therefore maintaining a normal serum insulin revel.

• The Korean Journal of Physiology and Pharmacology
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• v.16 no.6
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• pp.463-468
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• 2012

Type 1 diabetes (T1D) is caused by dysregulation of the immune system in the pancreatic islets, which eventually leads to insulin-producing pancreatic ${\beta}$-cell death and destabilization of glucose homeostasis. One of the major characteristics of T1D pathogenesis is the production of inflammatory mediators by macrophages that result in destruction or damage of pancreatic ${\beta}$-cells. In this study the inflammatory microenvironment of T1D was simulated with RAW264.7 cells and MIN6 cells, acting as macrophages and pancreatic ${\beta}$-cells respectably. In this setting, peroxiredoxin-1, an anti-oxidant enzyme was knocked down to observe its functions in the pathogenesis of T1D. RAW264.7 cells were primed with lipopolysaccharide and co-cultured with MIN6 cells while PRX-1 was knocked down in one or both cell types. Our results suggest that hindrance of PRX-1 activity or the deficiency of this enzyme in inflammatory conditions negatively affects pancreatic ${\beta}$-cell survival. The observed decrease in viability of MIN6 cells seems to be caused by nitric oxide production. Additionally, it seems that PRX-1 affects previously reported protective activity of IL-6 in pancreatic ${\beta}$ cells as well. These results signify new, undiscovered roles for PRX-1 in inflammatory conditions and may contribute toward our understanding of autoimmunity.

• Natural Product Sciences
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• v.18 no.2
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• pp.116-120
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• 2012

Pancreatic lipase digests dietary fats by hydrolysis, which is a key enzyme for lipid absorption. Therefore, reduction of fat absorption by the inhibition of pancreatic lipase is suggested to be a therapeutic strategy for obesity. We previously reported coumarins and secoiridoids of Fraxinus rhynchophylla as inhibitory constituents on adipocyte differentiation. Further investigation on F. rhynchophylla led to the isolation of lignan derivatives such as lignans (1 - 10), sesquilignans (11 - 14) and coumarinolignans (15 - 17). Among them, coumarinolignans and sesquilignans were first reported from Fraxinus species. Among the constituents isolated, sesquilignans showed the significant inhibition on pancreatic lipase, whereas lignans and coumarinolignans exerted weak effects.