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At least 19 recordsLinked to original sources
PubMed1977

Estimation of cholecystokinin-pancreozymin (CCK) in human plasma and tissue by a specific radioimmunoassay and the immunohistochemical identification of pancreozymin-producing cells in the duodenum of humans.

A reliable, sensitive, reproducible and specific radioimmunoassay for cholecystokinin-pancreozymin (CCK) has been developed, using rabbit antisera to highly purified porcine hormone. The natural occurring variant of CCK (39-CCK), in which the ordinary CCK is lengthened from its N-terminus by a hexapeptide, labelled with 125J, and repurified by column chromatography on Sephadex G-10 and on SP-Sephadex C-25, was used as tracer. Separation from antibody-bound labelled 39-CCK was carried out using a double antibody procedure. Non-specific interference with the assay system was abolished by ethanol extractions. Highly purified porcine CCK was used as standard. No significant crossreaction was found with gastrin, motilin, vasoactive polypeptide (VIP), gastric inhibitory polypeptide (GIP), natural and synthetic secretin, pancreatic glucagon or insulin. The sensitivity of the assay is approximately 40 pg/ml of test solution. The mean immunoreactive CCK concentration in 45 fasting normal subjects was 222 pg/ml increasing after food ingestion to 480 pg/ml. Somatostatin was able to abolish the stimulated CCK release. Elevated CCK concentrations were found in chronic pancreatitis. Immunohistochemical identification of pancreozymin cells was carried out either in surgical samples or in biopsy material. Approximately 1650 CCK cells per cross-section in the duodenum of humans have been found. The CCK cells usually appeared elongated, oval or pyramidal in shape and were observed to reach the lumen with their apical cell pole.

Animals↗
PubMed1981

[Cholecystokinin-pancreozymin synthesis. Synthesis of [28-threonine,31-norleucine]- and [28-threonine,31-leucine]cholecystokinin-pancreozymin-(25-33)-nonapeptide].

The syntheses of two analogues related to the C-terminal nonapeptide amide sequence 25-33 of cholecystokinin-pankreozymin are described. Based on the primary structure of the CCK-PZ-active caerulein and the experiences gained from the methionine replacement with leucine or norleucine in human little gastrin I, the analogues were designed by substituting methionine 28 with threonine, and methionine 31 with leucine and norleucine, respectively. Using a new method for the synthesis of tyrosine-O-sulfate-containing peptides, developed in our laboratory, and applying acid-labile side-chain protection in combination with the benzyloxycarbonyl group, the fully protected nonapeptide amide derivatives Z-Arg(Z2)-Asp(OBut)-Tyr-(SO3Ba1/2)-Thr(But)-Gly-Trp-Leu-Asp(OBut)-Phe-NH2 and Z-Arg(Z2)-Asp(OBut)-Tyr(SO3-Ba1/2)-Thr(But)-Gly-Trp-Nle-Asp(OBut)-Phe-NH2, were obtained. Upon hydrogenolytic and subsequent acidolytic removal of the protecting groups, followed by purification via chromatographic procedures the nonapeptide amides were isolated in satisfactory yields at a high degree of purity. In vivo and in vitro assays showed that a substitution of methionine 31 by norleucine with concomitant replacement of methionine 28 by threonine produced a fully active analogue, whereas for the threonine 28, leucine 31 analogue the pankreozymin-activity was lowered by a factor 10.

Amino Acid Sequence↗
PubMed1980

Rat pancreas adenylate cyclase: VII. Effect of extracellular calcium on pancreozymin-induced cyclic AMP formation.

1. The effect of stimulation of adenylate cyclase by pancreozymin-C-octapeptide on the cyclic AMP level of rat pancreatic fragments has been investigated. 2. In normal Krebs-Ringer bicarbonate medium pancreozymin-C-octapeptide causes a slight increase in pancreatic cyclic AMP level; this increase can be considerably enhanced by incubation in a calcium-free incubation medium. 3. The dose-response curve for pancreozymin-C-octapeptide in calcium-free medium is shifted to lower peptide concentrations, compared to the curve in normal Krebs-Ringer bicarbonate medium. 4. The maximal stimulatory effect of pancreozymin-C-octapeptide is obtained at a 1-methyl-3-isobutylxanthine concentration of 10 mM. 5. It suffices to lower the Ca2+-concentration of the medium from 2.5 to 1.5 mM to get the maximal increase in cyclic AMP content under influence of pancreozymin-C-octapeptide. 6. It is concluded that extracellular calcium antagonizes the stimulation of adenylate cyclase by pancreozymin-C-octapeptide. This suggests that a low cytoplasmic Ca2+-concentration is required for the maximal response of acinar cell adenylate cyclase to pancreozymin.

Adenylyl Cyclases↗
PubMed1969

Effects of secretin, pancreozymin, or gastrin on the response of the endocrine pancreas to administration of glucose or arginine in man.

Intravenous administration of porcine secretin or pancreozymin or synthetic human gastrin II resulted in raised increments in serum immunoreactive insulin during intravenous infusion of glucose in normal man. Enhancement of serum immunoreactive insulin by each hormone was associated with accelerated disposal of glucose. In response to prolonged intravenous infusion of arginine with pancreozymin there was a maintained rise in immunoreactive insulin and glucagon-like immunoreactivity in the blood. These effects of pancreozymin and arginine were not reproduced with secretin and arginine, and may have been due to the stimulation of glucagon secretion together with insulin by pancreozymin. Enteric infusion of hydrochloric acid, or stimulation of gastric acid secretion by betazole, presumed to cause release of endogenous secretin, led to enhancement of insulin secretion during intravenous infusion of glucose. Enteric infusion of arginine, presumed to cause release of endogenous pancreozymin, led to a rise in serum immunoreactive insulin not attributable to effects of circulating glucose and amino acids. It is concluded that secretin and pancreozymin released in response to physiological stimuli contribute to stimulation of the endocrine pancreas after ingestion of food.

Adolescent↗
PubMed1978

Visualization of the cystic artery after injection of Pancreozymin.

In 84 patients selective angiography of the common hepatic artery before and after injection Pancreozymin was performed. The results prove that: 1. Pancreozymin produces visualization of the cystic artery and its branches and of the gall-bladder wall in the majority of these normal gall-bladders that are not visualized during angiography without Pancreozymin. 2. Pancreozymin improves visualization of many normal and pathological gall-bladders seen only faintly on angiography without Pancreozymin. 3. In a patient with an angiographically normal liver the non-visualization of the branches of the cystic artery or of the gall-bladder wall after injection of Pancreozymin is a reliable sign of organic gall-bladder disease, or of a collapsed gall-bladder seen sometimes in patients with bile duct or pancreatic tumour.

Cholecystokinin↗
PubMed1960

A test of pancreatic function in man based on the analysis of duodenal contents after administration of secretin and pancreozymin.

Pancreozymin in man as in animals appears to act as a specific enzyme stimulant. The preparations of pancreozymin used in these experiments also contain cholecystokinin, which causes the gall bladder to contract, and a smooth muscle stimulant, possibly substance P. The duodenal contents obtained in response to a standard dose of secretin and pancreozymin have been collected quantitatively in man and the volume and amount of bicarbonate, amylase, trypsin, and lipase measured in order to study pancreatic function. The results of 105 tests undertaken on a normal group, in pancreatic and biliary disease, and in non-pancreatic steatorrhoea have been analysed. In localized pancreatic lesions and after recovery from acute pancreatitis, normal function is often retained. Mild functional impairment may be demonstrated only by a poor enzyme output in the post-pancreozymin fractions, while at a later stage bicarbonate output is affected and finally the volume of the duodenal contents is reduced. The secretin-pancreozymin test is most valuable, therefore, in the more chronic and advanced forms of pancreatic disease in which it gives a good assessment of residual pancreatic function. In diagnosis care must be taken in interpreting a functional test in terms of anatomical pathology. The test has proved useful not only in diagnosis but also as a guide to treatment and an index of prognosis.

Amylases↗
PubMed1967

The effects of secretin, pancreozymin, and gastrin on insulin and glucagon secretion in anesthetized dogs.

The effects upon islet hormone secretion of highly purified preparations of secretin and of pancreozymin-cholecystokinin and of a crude gastrin-containing extract of hog antrum have been studied in acutely operated dogs. All three preparations were shown to cause a striking increase in insulin concentration in the pancreaticoduodenal venous plasma after their rapid endoportal injection in anesthetized dogs. With each hormone preparation, the peak in insulin secretion occurred 1 minute after injection, and a rapid decline was observed immediately thereafter. Whereas secretin and gastrin failed to alter significantly the pancreaticoduodenal venous glucagon or arterial glucose concentration, pancreozymin caused a dramatic rise in pancreaticoduodenal venous glucagon concentration, which reached a peak 3 minutes after injection, and hyperglycemia was noted to occur soon thereafter. Endoportal infusion of secretin and pancreozymin for 20 minutes caused responses that were sustained but qualitatively identical to the responses noted after rapid injection of the hormones. The beta-cytotropic effect of secretin was abolished by the infusion of epinephrine. These results could not be attributed to the small degree of contamination of the enteric hormone preparations with insulin or glucagon, and it would appear that secretin, pancreozymin, and probably gastrin have insulin-releasing activity and that pancreozymin has, in addition, glucagon-releasing activity.The demonstration that these three hormones possess insulin-releasing activity suggests that there is in the gastrointestinal tract a chain of betacytotropic hormones from antrum to ileum that is capable of augmenting insulin secretion as required for disposal of substrate loads. It is suggested that the existence of this "entero-insular axis" prevents high substrate concentrations that would otherwise follow ingestion of large meals were the insular response entirely a function of arterial substrate concentration.

Adrenocorticotropic Hormone↗
PubMed1982

Pancreozymin and secretin enhance duodenal fluid antibody levels to cow's milk proteins.

Duodenal fluid was collected from normal volunteers before and after stimulation with pancreozymin-cholecystokinin and secretin. Protein content, proteolytic enzyme activities, and antibody activities against cow's milk proteins, alpha-casein, and beta-lactoglobulin B, were measured in the duodenal fluid. After pancreozymin-cholecystokinin stimulation, immunoglobulin A and immunoglobulin M antibody activities rose to peak levels in 5-10 min. The increase in protein content and proteolytic enzyme activities after pancreozymin-cholecystokinin stimulation paralleled the increase in antibody activity against the two cow's milk proteins. Secretin, in spite of its known dilutional effect on duodenal fluid enzyme concentration, also produced a rise in immunoglobulin M and immunoglobulin A antibody activities. Only a slight increase in immunoglobulin G antibody activity was noted after both pancreozymin-cholecystokinin and secretin. It is suggested that, pancreozymin-cholecystokinin and secretin, in addition to their well-established effects on the release of digestive enzymes, also stimulate release of specific antibodies against food proteins. Release of antibody coincident with food intake may act in preventing the inadvertent absorption of antigenic food proteins.

Adult↗
PubMed1980

Tissue distribution and metabolism of drugs V: effect of secretin and pancreozymin on drug transport in rabbit pancreas.

The effect of secretin and pancreozymin on the tissue distribution and penetration of drugs in the rabbit pancreas was studied to clarify hormonally regulated drug distribution. Drugs with high liquid solubility were distributed easily within the pancreas even during secretin or pancreozymin treatment, and these hormones had little effect on drug distribution from the blood to the pancreas. However, secretin increased the concentration ratio of dimethadione in the pancreatic juice (J) to plasma unbound dimethadione (Pf), probably because the pancreatic juice during secretin infusion is alkaline relative to the control. Secretin had no effect on the J/Pf of isonicotinamide and sulfanilamide. Secretin decreased the J/Pf of drugs with low lipophilicity or large molecular weight because the penetration rates of these drugs from cell water to pancreatic juice were not rapid enough to reach equilibrium. Pancreozymin was unable to change the J/Pf of any drug tested. These results suggest that the barrier between the blood and the pancreas or the barrier between the pancreas and the pancreatic juice is unchanged by secretin or pancreozymin.

Animals↗
PubMed1975

Radioselenium pancreozymin-secretin test as a clinical test for pancreatic exocrine function.

The appearance of radioselenium in the protein fraction of duodenal aspirates has been studied after an intravenous injection of 75-Se-selenomethionine. The continuous flow of pancreatic juice was stimulated by pancreozymin at 120 minutes and by secretin at 140 minutes. A good distinction between normal subjects and patients with pancreatic disease was obtained by measuring 75-Se-radioactivity in the protein fraction of duodenal aspirates; either cumulative radioactivity during the combined 80-minute post-pancreozymin-secretin period, or maximum 75-Se-specific activity during the postsecretin period was used as an index. The test presented here might be a useful and sufficiently reliable method for detecting abnormal pancreatic exocrine function. This test can be performed along with the conventional pancreozymin-secretin test, serum enzyme response to pancreozymin and secretin, and pancreatic scintiscanning.

Amylases↗
PubMedDate not supplied

Effects of calcitonin on the secretion of pancreatic juice induced by dopamine, secretin and pancreozymin.

1. Effects of calcitonin on dopamine-, secretin- and pancreozymin-induced pancreatic secretion were investigated in the isolated blood-perfused canine pancreas. 2. The volume of pancreatic secretion induced by pancreozymin given intra-arterially (i.a.) was decreased by an i.a. infusion of 1 u/min of calcitonin, but that induced by dopamine or secretin given i.a. was not affected by calcitonin treatment. 3. Amylase concentration in pancreatic juice either in spontaneous secretion in the resting state or in that of stimulated secretion by pancreozymin was decreased approximately 30% by calcitonin treatment, but amylase concentration in pancreatic juice induced by dopamine or secretin was not affected by calcitonin treatment. 4. Calcitonin had no effect on bicarbonate concentration in pancreatic juice stimulated by these secretagogues. 5. Calcium concentration in pancreatic juice in the resting state was reduced about 36% by calcitonin treatment. Calcitonin caused a decrease in a calcium concentration in the pancreozymin-induced secretion, but did not cause any change in the dopamine- or secretin-induced one. 6. These results suggest that calcitonin may affect the secretory mechanism of the acinar cells but not that of the ductular cells, and that the acinar cells are active even in the resting state.

Amylases↗
PubMed1981

[Central action of cholecystokinin-pancreozymin and secretin on pancreatic enzyme secretion].

In chronic experiments on dogs with fistulae of pancreas, administration of pancreozymin into the cerebral ventricles activated the lipase activity of pancreatic juice whereas secretin inhibited the trypsin activity. The pancreozymin administration into the anterior hypothalamus activated the pancreatic lipase whereas administration of this hormone into the RF exerts no effect on the basal secretion of juice and enzymes. The secretin administration into the hypothalamus or RF leaves the pancreatic secretion intact. Administration of CSF from dogs-donors with pancreozymin in their cisterna magna activated the lipase activity of the juice. Central action of cholecystokinin-pancreozymin on the pancreatic secretion of enzymes seems to be actualized through the hypothalamic structures.

Amylases↗
PubMedDate not supplied

[Evaluation of the vegetable oil taken up into the duodenum as a factor in pancreozymin liberation in healthy persons and in digestive organ diseases].

Investigations carried out in 14 healthy volunteers, 29 patients with chronic pancreatitis and 15 patients with chronic hepatitis showed that infusion into the duodenum of an optimally tolerable quantity (25 ml) of vegetable oil makes for a release of an amount of pancreozymin, which, by the criterion for stimulating secretion of pancreatic amylase, is equivalent to 0.5 Un/kg of pure preparation of pancreozymin and, as to the degree of stimulating the secretion of lipase and trypsin, it exceeds the effect of 0.5 Un/kg, but is less than that of 1.5 Un/kg of pure pancreozymin. These data should be taken into account in evaluating the ability of some alimentary fats to stimulate the release of endogenous pancreozymin.

Cholecystokinin↗
PubMed1981

[Can cerulein replace pancreozymin in the diagnosis of exocrine pancreatic function? (author's transl)].

The effect of the decapeptide cerulein on exocrine pancreatic function was compared with pancreozymin by means of intraindividual double stimulation. 100 ng/kg bw/45 min of synthetic cerulein led to a greater enzyme excretion than 2 U/kg bw pancreozymin. This increase in enzyme secretion was independent of whether the pancreas function was normal or disordered. In the selected experimental procedure, cerulein increased the excretion of enzymes (chymotrypsin, trypsin, lipase, amylase) whether it was infused in connection with or before an injection of pancreozymin. Cerulein can therefore completely replace pancreozymin in the diagnosis of pancreatic function.

Ceruletide↗