Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01275 (glucagon)
 26,492 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Pancreatic endocrine cells were stained immunocytochemically for insulin, glucagon, somatostatin and pancreatic polypeptide by the PAP technique or sequentially for two hormones by the PAP followed by an indirect immunogold procedure. Pancreatic endocrine cells of Chrysemys are found scattered as single cells or small aggregates throughout the exocrine parenchyma; only the splenic region shows islets consisting of a B cell core surrounded by a loose mantle of A cells and occasional D cells. PP cells were not found in this splenic portion but were found scattered throughout the remainder of the pancreas. In contrast to the typical vertebrate islet, Chrysemys pancreatic endocrine cells are characterized by a lack of preferential association of one cell type with another and suggests that paracrine regulatory mechanisms may not be operable in this species. Insulin secretion from pieces of Chrysemys pancreas has been measured in incubation and perifusion systems employing a heterologous radioimmunoassay. Insulin release by Chrysemys B cells is enhanced by elevated levels of glucose (300 mg/dl), however, response appears to be somewhat slower compared to other vertebrate B cells. Gastrin, secretin, neurotensin, motilin, serotonin, PYY, glucagon, gastric inhibitory polypeptide, somatostatin and insulin were demonstrated immunocytochemically in open-type GEP cells of the mucosal epithelium of the Chrysemys intestine. Of these cells, gastrin, neurotensin and insulin cells appear to be the most numerous while the other types appear less frequently. Cells containing PP, bombesin, cholecystokinin and substance P could not be demonstrated. The localization of insulin to GEP cells of the turtle intestine is an unusual finding but has been confirmed by radioimmunoassay of extracts of the intestinal mucosa.
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PMID:The gastro-entero-pancreatic system of the turtle, Chrysemys picta. 391 12

The effects of bombesin on gastric acid secretion from the Heidenhain pouch (HP), intraduodenal pH and gastroenteropancreatic (GEP) hormone levels were compared between 4 dogs with antrocolic transposition (ACT) and 4 non-ACT dogs. Bombesin, infused i.v. at a dose of 0.5 microgram/kg for one hr, produced a significant increase in gastric acid secretion from HP and a decrease in intraduodenal pH in both groups. However, these changes were more marked in ACT dogs. The intravenous infusion of bombesin also produced, in both groups, an increase in the plasma levels of gastrin, secretin, motilin, insulin, glucagon and pancreatic polypeptide (PP) with a different shape of curve for each hormone. Comparison between the two groups showed significantly greater plasma gastrin, secretin and insulin responses, and smaller plasma PP response in ACT dogs than in non-ACT dogs. These results demonstrate that the mechanism of GEP hormone release by bombesin may be complex and hormone responses to infusion of bombesin are influenced in a state of acid hypersecretion induced by ACT.
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PMID:Gastric acid secretion, intraduodenal pH and gastroenteropancreatic hormone release to bombesin in antrocolic transposition dogs. 398 57

There is evidence for involvement of gastrointestinal hormones in pathogenesis of obesity and reports on lipolytic activity in animals. The in vitro lipolytic activity of these hormones was tested in human adipocytes. Vasoactive intestinal polypeptide, glucagon, secretin, human gastrin I, gastrin releasing polypeptide, gastric inhibitory polypeptide, pancreatic polypeptide, motilin, bombesin, neurotensin, C-peptide, as well as cholecystokinin did not stimulate lipolysis significantly above basal. These results indicate that the involvement of these hormones in obesity in man might not be due to a direct lipolytic effect on the human adipocyte.
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PMID:Glycerol release from incubated human adipocytes is not affected by gastrointestinal peptides. 401 16

Concentrations of several gastrointestinal hormonal peptides were measured in lymph from the cisterna chyli and in arterial plasma; in healthy, conscious pigs during ingestion of a meal. Lymph concentrations of the pancreatic hormones insulin, glucagon and pancreatic polypeptide were small compared with plasma concentrations, although postprandial increments were significant. In contrast lymph concentrations of gastrin, cholecystokinin, motilin and gastric inhibitory peptide (GIP) from the foregut showed a more marked postprandial rise than the pancreatic hormones. Indeed the total integrated responses of these peptides in lymph reached about 50% of those seen in arterial plasma. It would appear unlikely that the lymphatics constitute an important transport mechanisms for these regulatory peptides. However, lymph concentrations of hormones may reflect levels in interstitial fluid better than plasma and may be of value in assessing putative physiological actions within a target tissue.
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PMID:Lymph, pancreatic and gastrointestinal hormones in response to feeding in the conscious pig. 405 90

The distribution and quantification of enteroendocrine cells exhibiting immunoreactivities to nine peptides and one amine were examined in the gastrointestinal mucosa of the adult opossum using specific immunocytochemical methods. In the stomach, 90% of the enteroendocrine cells are confined to the pyloric glands and this region contained 73% of the gastrin-containing cells, 60% of the somatostatin-containing cells and 9% of cells reactive for 5-HT. Enteroendocrine cells showing immunoreactivities to glucagon, pancreatic polypeptide, somatostatin and 5-HT were observed scattered within the oxyntic glands. Only somatostatin and 5-HT positive cells were found in the cardiac glands. Immunoreactivities to CCK, glucagon, gastrin, BPP, somatostatin, secretin, motilin, neurotensin, GIP and 5-HT were observed in the epithelium of the small intestine. Although considerable variation exists in the distribution of individual enteroendocrine cell types along the intestinal tract, nearly equal numbers of enteroendocrine cells were observed in each segment. The percentage of enteroendocrine cells increases distally in the colon. Of the three enteroendocrine cell types present, somatostatin- and 5-HT-immunoreactive cells are evenly distributed, whereas neurotensin-immunoreactive cells increase in numbers distally, resulting in an increase in total number.
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PMID:Quantitative distribution of enteroendocrine cells in the gastrointestinal tract of the adult opossum, Didelphis virginiana. 407 99

Historically, the enterochromaffin cell was the first endocrine cell type detected in avian gut; subsequently, a number of types of such cells were distinguished on the basis of the ultrastructural features of the secretory granules. More recently, immunocytochemical procedures have revealed somatostatin-, pancreatic polypeptide (PP)-, polypeptide YY-, glucagon-, secretin-, vasoactive intestinal peptide (VIP)-, gastrin-, cholecystokinin-, neurotensin-, bombesin-, substance P-, enkephalin-, motilin-, and FMRFamide-like immunoreactivity in avian gastrointestinal endocrine cells. Most endocrine cells are located in the antrum; there are a number in the proventriculus and small intestine but few in the gizzard, cecum, and rectum. Several avian gastroenteropancreatic hormones, including glucagon, VIP, secretin, bombesin, neurotensin, and PP, have been isolated and sequenced. They resemble the equivalent mammalian peptides in terms of molecular size but differ in amino acid composition and sequence; some (e.g., VIP) differ only in minor respects, others (e.g., secretin) more radically. Gastrointestinal endocrine cells appear late in development; available data indicate that few types are recognized by either immunocytochemistry or electron microscopy before 16 days of incubation. Experimental evidence has shown that at least the majority of gut endocrine cells are of endodermal origin and are not derived from the neural crest or neuroectoderm as earlier proposed. In early embryos, the progenitors of gastrointestinal endocrine cells are more widespread than are the differentiated cells in chicks at hatching. This, along with other observations, raises the question of factors that might influence the differentiation of gut endocrine cells.
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PMID:Gastrointestinal hormones in birds: morphological, chemical, and developmental aspects. 608 44

The 24 endocrine pancreatic tumors and 14 carcinoids were examined immunohistochemically for cholecystokinin, insulin, gastrin, GIP, glucagon, sercretin, VIP, motilin, neurotensin, pancreatic polypeptide (PP), somatostatin, and ACTH. In 12 tumors of the pancreas more than one peptide-containing cell type was observed. The clinical symptoms showed hypersecretion of only one of the hormones, however. The midgut carcinoids (jejunum, appendix) represented the classical view of the carcinoid as an argentaffin cell tumor secreting 5-hydroxytryptamine. Tumors originating in the foregut (bronchus, stomach, duodenum) and hindgut carcinoids (rectum) were nonargentaffine, containing and secreting various polypeptide hormones. We conclude that light microscopic immunohistochemical methods are useful in distinguishing endocrine from nonendocrine tumors and multihormonal syndromes (MEA) in the classification of predominant hormone-secreting tumors.
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PMID:[Endocrine tumors of the gastrointestinal and pancreatic systems. Multiple endocrine adenoma from another viewpoint]. 610 39

The effects of pirenzepine on the plasma concentrations of gut hormones in the fasting and postprandial states were studied in six healthy subjects. On separate days and in random order, 10 mg pirenzepine, in 2 ml of solvent, or 2 ml saline (0.15 mol/l) were given intravenously 30 min before a standard normal breakfast (2220 kJ). Pirenzepine was not found to affect basal or postprandial levels of insulin, glucagon, gastric inhibitory peptide (GIP), neurotensin, vasoactive intestinal peptide (VIP) or somatostatin. The basal concentration of pancreatic polypeptide (PP) was lowered (p less than 0.05) and the postprandial elevation reduced, though not significantly. While the basal concentration of motilin was also suppressed (p less than 0.05), the postprandial elevation remained unchanged following pirenzepine. The release of enteroglucagon was reduced significantly in the basal and postprandial states (p less than 0.05 and p less than 0.025 respectively). The postprandial gastrin response was prolonged slightly, but insignificantly, by pirenzepine. It is concluded that pirenzepine does not exert any major or unexpected actions on the hormonal control of digestion.
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PMID:The effect of pirenzepine on meal-stimulated gastrointestinal hormones. 611 82

1. The biochemical specificity and duration of action of a single 5 mg subcutaneous dose of des-AA1,2,4,5,12,13-D-Trp8-somatostatin were evaluated in eight patients with symptomatic pancreatic endocrine tumours. 2. There was a reduction by more than 50% for at least 10 h in plasma concentrations of growth hormone, glucagon, gastrin and motilin and for 4--5 h in plasma insulin, pancreatic polypeptide, gastric inhibitory polypeptide and enteroglucagon. 3. This study shows that this octapeptide analogue of somatostatin, like somatostatin itself, lacks specificity in the hormones it suppresses. However, its prolonged duration of action against several hormones when given subcutaneously suggests that it may be of therapeutic use in a number of disease states where excessive plasma concentrations of one or more of these hormones occur.
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PMID:Effect of a long-acting octapeptide analogue of somatostatin on growth hormone and pancreatic and gastrointestinal hormones in man. 611 53

The potency and specificity of somatostatin (SS) and four of its analogs were compared in seven patients with pancreatic endocrine tumors. The analogs tested were [D-Trp8]-SS, [D-Trp8, D-Cys14]-SS, Des-Asn5-[D-Trp8, D-Ser13]-SS, and Des (AA)1,2,4,5,12,13, [D-Trp8]-SS, and they did not show selective effects on the suppression of basal concentrations of GH, insulin, glucagon, pancreatic polypeptide, gastrin, gastric inhibitory peptide, motilin, enteroglucagon, or neurotensin. The observation that the potency of these analogs is similar to that of the parent molecule throws considerable light on the structure/activity relationship of the somatostatin molecule. Des-AA1,2,4,5,12,13, [D-Trp8]-Ss has been reported to have a prolonged action when administered sc. When administered iv, however, this octapeptide analog ws not long acting, suggesting that the prolonged action seen in the previous study was a result of delayed uptake from the injection site. An increment in plasma SS concentrations of 19 +/- 3 pmol/liter suppressed basal concentrations of GH, insulin, glucagon, and several gastrointestinal hormones by more than 50%, suggesting that even small changes in plasma SS levels may be physiologically important.
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PMID:The effect of somatostatin analogs on secretion of growth, pancreatic, and gastrointestinal hormones in man. 611 21


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