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Results for “Pancreatic Polypeptide”

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At least 19 recordsLinked to original sources
PubMed1982

Influence of glucagon, gastric inhibitory polypeptide, pancreatic polypeptide and somatostatin on beta-adrenergically induced insulin secretion in the mouse.

The effect of four polypeptides, glucagon, Gastric Inhibitory Polypeptide (GIP), Pancreatic Polypeptide (PP) and somatostatin on beta-adrenoceptor stimulated insulin secretion in vivo in the mouse was investigated. The beta-adrenoceptor stimulation was induced by isoprenaline (IPNA). It was found that at dose levels without influence on basal insulin secretion the polypeptides produced the following pattern of interaction with IPNA. Insulin secretion induced by IPNA was increased by glucagon and inhibited by somatostatin. GIP and PP did not change IPNA-induced insulin release. It is concluded from this and earlier published studies that glucagon, but not always GIP, serves as a positive modulator of basal and stimulated insulin secretion, and that somatostatin is a general inhibitor of insulin release. beta-Adrenoceptor-induced insulin secretion however, seems to be less sensitive to somatostatin than insulin release induced by glucose.

Animals↗
PubMed1986

Pancreatic polypeptide, pancreatic glucagon and enteroglucagon in morbid obesity and following gastric bypass operation.

The influence of morbid obesity and gastric bypass operation on pancreatic polypeptide (PP), pancreatic glucagon and enteroglucagon was studied in six morbidly obese patients before and 6-9 months after surgery. Hormone plasma levels were determined in the fasting state and after a standardized test meal. Fasting levels of PP, pancreatic glucagon and enteroglucagon were not significantly different between the pre- and post-operative state as well as compared to normal controls. The postprandial response showed a significant reduction of PP, a significant increase of enteroglucagon and no change of pancreatic glucagon after surgery compared with the preoperative values.

Adult↗
PubMed1983

Diurnal profile of pancreatic polypeptide, pancreatic glucagon, gut glucagon and insulin in human morbid obesity.

The diurnal profiles of pancreatic glucagon, insulin, pancreatic polypeptide (PP), and enteroglucagon were studied in five obese non-diabetic subjects (195 +/- 11 per cent of ideal body weight) and in six age matched controls. All the subjects were served with ordinary mixed meals five times during the day. The obese subjects were normoglycemic but hyperinsulinemic. Both groups showed rapid increases in PP to all meals, but the PP-response was significantly impaired in the obese group during the first part of the day. Normal subjects showed significant enteroglucagon responses to all meals, and had elevated levels throughout the day. In obese subjects, levels and responses were much lower at all times. Pancreatic glucagon profiles were similar. It is concluded that the possible role of abnormalities of PP and enteroglucagon secretion in the pathogenesis of human obesity deserves further study.

Adult↗
PubMed1987

Purification and primary structure of ostrich pancreatic polypeptide.

Pancreatic polypeptide has been isolated from ostrich pancreas by gel filtration, ion exchange chromatography and high pressure liquid chromatography. The ostrich peptide contains 36 amino acids and has an amino acid composition similar to pancreatic polypeptide of other avian species. The primary structure of ostrich pancreatic polypeptide differs from that of the chicken peptide only at residues 3 and 18 where the ostrich peptide contains an alanine and a valine residue compared to the serine and isoleucine residues found in those positions in the chicken peptide.

Amino Acid Sequence↗
PubMed1982

Effect of cephalic-vagal stimulation on insulin, gastric inhibitory polypeptide, and pancreatic polypeptide release in humans.

The purpose of the present study was to determine whether there is a cephalic phase of insulin or gastric inhibitory polypeptide release in man. Seven healthy, normal weight volunteers were sham fed an appetizing steak meal, and serum insulin, gastric inhibitory polypeptide, and pancreatic polypeptide concentrations were measured. A pancreatic polypeptide response to sham feeding was employed as marker of adequate cephalic-vagal stimulation. Although serum pancreatic polypeptide concentrations increased significantly (P less than 0.05) in response to sham feeding, sham feeding had no significant effect on serum insulin and gastric inhibitory polypeptide levels. In addition, sham feeding did not affect insulin or gastric inhibitory polypeptide responses to intragastric glucose, although sham feeding did augment the pancreatic polypeptide response to this meal. These experiments were, therefore, unable to demonstrate insulin or gastric inhibitory polypeptide release in response to cephalic-vagal stimulation in humans.

Adult↗
PubMed1982

Effects of synthetic human pancreatic polypeptide, synthetic bovine pancreatic polypeptide, and the C-terminal hexapeptide on pancreatic somatostatin and glucagon secretion in the rat.

Synthetic human pancreatic polypeptide stimulated pancreatic somatostatin secretion by isolated rat islets and by the isolated perfused rat pancreas. In contrast, synthetic bovine pancreatic polypeptide and the C-terminal hexapeptide had no effect on somatostatin secretion. Synthetic human pancreatic polypeptide had only a mild stimulatory effect on glucagon secretion at the highest concentration of the peptide used (2.2 x 10(-6) M0 and in the presence of 16.7 mM glucose.

Animals↗
PubMed1994

Isolation and structural characterisation of herring gull (Larus argentatus) pancreatic polypeptide.

Pancreatic polypeptide (PP) has been isolated from pancreatic extracts of the herring gull (Larus argentatus) using a radioimmunoassay employing an antiserum (PP 221), generated to the conserved C-terminal hexapeptide amide of mammalian PP. Gel permeation and reverse-phase HPLC fractionation of crude pancreatic extracts resolved a single molecular form of gull PP in each case. Purification of gull PP to homogeneity indicated that the mammalian PP antiserum employed was only 4% cross-reactive with this peptide. When radioimmunoassay data were corrected for this, the herring gull pancreas was found to contain 5 nmol PP/g wet wt. The molecular mass of gull PP was determined as 4237 +/- 2 Da by 252Cf plasma desorption mass spectroscopy (PDMS). Gas-phase sequencing established unequivocally the entire primary structure of a 36-amino-acid residue peptide as Gly-Pro-Val-Gln-Pro-Thr-Tyr-Pro-Gly-Asp-Asp-Ala-Pro-Val-Glu-Asp-Leu-Val- Arg-Phe - Try-Asn-Asp-Leu-Gln-Gln-Tyr-Leu-Asn-Val-Val-Thr-Arg-His-Arg-Tyr. The computed molecular mass of this peptide (4235.6 Da) was in close agreement with that derived by PDMS. The primary structure of herring gull PP differs from that of the chicken in four residues at positions 3 (Val/Ser), 18 (Val/IIe), 22 (Asn/Asp), and 23 (Asp/Asn). Avian PP thus appears to be a highly conserved regulatory peptide.

Amino Acid Sequence↗
PubMed1991

Intraluminal ileal recovery of pancreatic polypeptide.

Pancreatic polypeptide (PP) is a normal constituent of pancreatic islet cells. Enterocytes containing PP have been identified but incompletely characterized. We previously demonstrated independent intravascular and intraluminal release of two related peptides, peptide YY and neuropeptide Y. In this study, using ileal segments in conscious dogs, we evaluated the intravascular and ileal intraluminal presence of PP to test meals. Fasted plasma and recoverable ileal PP concentrations averaged 139 +/- 2 and 65 +/- 4 pg/mL, respectively. A mixed protein meal resulted in a sustained rise of circulating PP levels associated with a brief evaluation of ileal luminal PP levels. Fat meals were followed by elevations in plasma PP levels without luminal changes. Glucose ingestion altered neither plasma nor luminal PP levels. Our data support the existence of ileal PP-containing cells that respond independently of circulatory PP-releasing cells to different ingested stimuli.

Animals↗
PubMed1987

Cellular peptide processing after a single arginyl residue. Studies on the common precursor for pancreatic polypeptide and pancreatic icosapeptide.

The processing of the common precursor for pancreatic polypeptide and pancreatic icosapeptide was studied in primary cultures of endocrine cells isolated from the duodenal part of the canine pancreas. Biosynthetically labeled peptides were characterized by enzymatic digestion and radiosequencing and compared to a COOH-terminally extended form of the icosapeptide which was isolated from canine pancreas and also sequenced. It was substantiated that, in these cell cultures, processing can be studied at a classical dibasic site between the pancreatic polypeptide and the icosapeptide, and at a monobasic processing site between the icosapeptide and its COOH-terminal extension. Pulse-chase experiments showed that the monobasic cleavage occurs later than the dibasic one in the biosynthetic process; the monobasic site was apparently not cleaved before the prohormone had been processed at the dibasic site. The monobasic processing could also be distinguished from the dibasic cleavage mechanism as, in time, the cells gradually lost the ability to cleave at the monobasic site while the dibasic processing was unaffected. It is concluded that monobasic conversion, which is important in the activation of a series of hormones, neuropeptides, and growth factors, is a distinct cellular processing mechanism.

Amino Acid Sequence↗
PubMed1984

Serum immunoreactive trypsin, pancreatic polypeptide, and pancreatic isoamylase as diagnostic tests for chronic pancreatitis.

The efficiency of immunoreactive trypsin (IRT), pancreatic polypeptide (PP), and pancreatic isoamylase (PI) in the diagnosis of chronic pancreatitis was studied in 80 consecutive patients clinically suspected of having chronic pancreatitis. Twenty-five patients had chronic pancreatitis, and of these, 17 had pancreatic insufficiency. IRT, PP, and PI were of no value in the diagnosis of chronic pancreatitis without insufficiency. The three tests were of equal but limited value in diagnosing pancreatic insufficiency (nosographic sensitivities, 0.53 to 0.59, and predictive values of a negative test, 0.88 to 0.90). The combination of IRT, PP, and PI did not increase the diagnostic efficiency compared with each of the three tests alone. We conclude that IRT, PP, and PI are of similar but limited value as diagnostic tests for pancreatic insufficiency.

Adult↗
PubMed1984

A cDNA encoding a small common precursor for human pancreatic polypeptide and pancreatic icosapeptide.

A cDNA for the hormone, human pancreatic polypeptide (PP), was isolated by oligodeoxynucleotide screening from a cDNA library constructed from normal human pancreatic mRNA. The primary structure of the precursor protein as deduced from the cDNA sequence is 95 amino acids long and is composed of a typical, but rather long signal peptide of 29 residues, followed by the sequence of the 36 amino acid human pancreatic polypeptide, which again is separated from the human pancreatic icosapeptide sequence by a classic cleavage and amidation site, Gly-Lys-Arg. The precursor terminates in a heptapeptide which is cleaved from the icosapeptide at a monobasic processing site. Both the size and the structure of the PP precursor was supported by the results of peptide analysis of biosynthetically labeled pro-PP isolated from canine PP cells in which processing was prevented by the arginine analogue canavanine. It is concluded that the precursor for mammalian PP gives rise to two peptide products, the well preserved, carboxyamidated PP and an icosapeptide which is preserved only in its COOH-terminal end, plus a small highly variable COOH-terminal oligopeptide.

Amino Acid Sequence↗
PubMed2002

Pancreatic polypeptide in pancreatitis.

Pancreatitis is a disease with increasing incidence which can be divided into an acute and a chronic form. In both acute and chronic pancreatitis, changes in plasma concentration of pancreatic polypeptide (PP) and its regulation have been reported. In daily clinical work a serologic test for the precise diagnosis and staging of acute and chronic pancreatitis is still desirable. Therefore, many studies have investigated plasma concentrations of PP in acute and chronic pancreatitis as a diagnostic marker and as a therapeutic option to treat pancreatogenic diabetes mellitus. Although the study results are presently inconclusive and potentially contradictory, the findings are nevertheless encouraging, and indicate that PP might have a role in diagnosis, grading and estimation of the prognosis of pancreatitis. Further data and prospective controlled studies are needed to judge whether PP is of clinical value for diagnosing, staging and predicting long-term outcome in acute and chronic pancreatitis.

Acute Disease↗
PubMed1984

Effects of a gastric partitioning operation for morbid obesity on the secretion of gastric inhibitory polypeptide and pancreatic polypeptide.

Nine morbidly obese subjects were studied with a test meal before and 3 months after a gastric partitioning operation. After the operation the postprandial release of plasma gastric inhibitory polypeptide was significantly increased, the plasma pancreatic polypeptide release was similar, and the serum insulin release significantly reduced as compared with the preoperative values.

Adult↗
PubMed1987

Immunoneutralization of circulating pancreatic polypeptide and pancreatic secretion.

To determine the role of endogenous pancreatic polypeptide (PP) as a physiological inhibitor of pancreatic secretion, normal rabbit serum (control) or rabbit PP-antiserum was administered intravenously to dogs with chronic esophageal, gastric, and pancreatic fistulas. In all dogs tested, sham-feeding and ordinary feed with a meat meal resulted in a marked rise in the plasma level of immunoreactive PP that coincided with an increase in the exocrine pancreatic secretion of HCO3- and protein. After intravenous administration of PP antiserum, endogenous plasma PP was almost completely bound by infused antibodies to PP, whereas no such binding was detected after infusion of normal rabbit serum. In contrast, plasma gastrin remained unchanged both under basal and stimulated conditions. Immunoneutralization of PP, released endogenously, failed significantly to affect gastric acid and pancreatic protein responses to sham-feeding and the pancreatic HCO3- and protein responses to feeding a meat meal in chronic pancreatic fistula dogs. However, the PP antiserum abolished, in part, the inhibitory effect of exogenous PP on pancreatic secretion stimulated by exogenous hormones. We conclude that endogenous PP is not a physiological inhibitor of exocrine pancreatic secretion, as has been suggested previously.

Animals↗
PubMed1992

Glucose, insulin, gastric inhibitory polypeptide, and pancreatic polypeptide responses to polycose during pregnancy.

Polycose, a glucose polymer produced by controlled acid enzyme hydrolysis of starch, has been proposed as an effective substitute for glucose solution in antepartum screening for glucose intolerance. The purposes of this study were to examine the glucose and hormonal responses to 50 g of glucose polymer (polycose) solution in pregnant and nonpregnant women and to compare these with the standard 50-g oral glucose challenge test. In addition, the subject's acceptance of the glucose polymer solution was evaluated. Subjects were examined after an overnight fast following a 3-day dietary preparation. There was no difference in glucose or insulin responses to glucose or polycose in either pregnant or nonpregnant women. In contrast, the gastric inhibitory polypeptide response to polycose was significantly higher than to glucose. No differences were observed in plasma pancreatic polypeptide responses to glucose and polycose. In the pregnant subjects, even though the plasma insulin response to carbohydrate challenge was higher than in the nonpregnant subjects, gastric inhibitory polypeptide levels were significantly lower. Patient satisfaction was similar with both carbohydrate solutions. These data suggest that polycose can be used as a substitute for glucose in antepartum testing, although the differences in the hormonal responses should be recognized. Further studies in a subject population with carbohydrate intolerance will be required before polycose use can be recommended in abnormal states.

Adult↗
PubMed1982

Dose-dependent increase in concentrations of gastric inhibitory polypeptide and pancreatic polypeptide after small amounts of glucose intraduodenally in man.

Nine healthy volunteers were infused intraduodenally with 100 ml isotonic solutions of 1, 2.5, and 5 g glucose for 15 min at 1-h intervals. The gastric inhibitory polypeptide (GIP) concentration in plasma did not increase after 1 g of glucose, whereas after 2.5 g of glucose the GIP concentration increased from 32.1 (23.3-68.4) to 53.9 (30.0-63.0) pM and after 5 g from 36.8 (18.0-54.7) to 78.5 (46.9-163) pM. The serum concentration of pancreatic polypeptide (PP) increased only after 5 g, from 19.3 (14.8-29.1) to 28.8 (15.3-45.3) pM. This shows that the plasma concentration of GIP increases dose-dependently after small doses of duodenal glucose and that glucose really is a duodenal stimulus for an increase i serum PP concentration.

Adult↗
PubMed1994

In vitro release of vasoactive intestinal polypeptide and pancreatic polypeptide from human VIPoma cells and its inhibition by somatostatin analogue (SMS 201-995).

BACKGROUND: The purpose of the present study was to determine whether vasoactive intestinal polypeptide (VIP) is released from the tumor cells of VIPoma and if so then to attempt to show how its release is regulated by cultured human VIPoma cells. METHODS: A resected specimen of a pancreatic tumor from a patient with watery diarrhea, hypokalemia, and achrohydria syndrome was examined. The dissociated cells were obtained by collagenase digestion of the tumor tissue and were cultured in vitro. RESULTS: The extraction of tumor cells disclosed that the cells contained VIP and pancreatic polypeptide (PP). Neither insulin, glucagon, somatostatin nor pancreastatin was detected. Immunohistochemically, 40% to 60% of the cells in the tumor stained positively for VIP and 1% to 5% stained positively for PP. The dissociated cells became reaggregated in the culture (50 to 300 microns) and could be maintained in vitro. Incubation experiments revealed a simultaneous in vitro release of VIP and PP with a significant increase by either carbachol or phorbol myristate acetate but not by theophylline or caerulein. Atropine completely abolished the stimulatory effects of carbachol on VIP and PP release. Octreotide (somatostatin analogue [SMS 201-995]) significantly inhibited the carbachol and phorbol myristate acetate-stimulated VIP and PP release. CONCLUSIONS: These findings show the in vitro release of VIP and PP from the VIPoma cells and also provide evidence for the direct inhibitory effect of somatostatin analogue on both the VIP and PP release from the tumor cells.

Adult↗
PubMed1988

Influence of avian pancreatic polypeptide on pancreatic and biliary secretion in laying hens.

White Leghorn hens, 14 to 29 wk of age, were surgically prepared with cannulae for collecting secretions from the cystic duct and the duct draining the ventral pancreatic lobe and for infusing the jugular vein with avian pancreatic polypeptide (aPP) or saline. A plasma infusion rate that produced a plasma level of 15 ng of aPP/mL was used. A comparison of values obtained during saline infusion with those obtained during aPP infusion indicated that pancreatic and biliary secretory volumes and pancreatic total protein concentration were significantly depressed by aPP. The pH of pancreatic and biliary secretions were not significantly affected by aPP. Because aPP also depresses gastric secretion and motility in hens, it is proposed that its physiological role may be to oppose or modulate the actions of other, stimulatory gastrointestinal hormones.

Animals↗