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)

In rats, total gastrectomy (TG) has been shown to induce pancreatic hyperplasia and increased tissue concentrations of pancreatic trypsin and amylase, whereas lipase concentration was decreased. We performed total gastrectomy with the additional insertion of a duodenal tube in 17 rats. A central venous catheter was placed after 3 wk. The control groups consisted of sham-operated rats with a gastrotomy plus duodenal tube and a group of rats with only a duodenal tube. The rats received meal stimulation with a 6 mL liquid diet (3 mL oil, 2 mL amino acid solution, and 1 mL glucose) via duodenal tube upon recuperation. Blood samples were taken before as well as 5, 15, 30, and 60 minutes after the meal and analyzed for insulin, pancreatic glucagon, gastrin, and CCK by specific RIA techniques. Glucose tolerance was found to be impaired after total gastrectomy. Though insulin release was delayed compared to the controls, the integrated postprandial output was unchanged. The pancreatic glucagon release after the meal increased 83% in TG rats, compared to control rats. The baseline and postprandial gastrin values diminished 70% compared to control animals. Neither group exhibited a postprandial increase in gastrin levels. TG led to an increased postprandial CCK output of 72% compared to controls. The trophic changes of rat exocrine pancreas following total gastrectomy, therefore, could be based on an elevated postprandial release of CCK.
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PMID:Cholecystokinin influences pancreatic trophism following total gastrectomy in rats. 266 36

We studied the effects of intravenous infusion of synthetic oxyntomodulin (proglucagon 33-69), a potential hormone from the ileal mucosa, on fasting and postprandial gastric acid secretion, gastric emptying, gastroduodenal motility, and pancreatic secretion of trypsin and lipase measured simultaneously in six normal volunteers using multilumen tubes for infusion of markers, manometry, and aspiration of gastric and duodenal contents. The infusion resulted in plasma concentrations of 203 +/- 21 pmol/liter (mean +/- SEM) of oxyntomodulin, regarded as high but not unphysiological concentrations of the peptide. Oxyntomodulin almost abolished basal acid secretion and inhibited postprandial acid secretion by 35 +/- 10%. Gastric emptying decreased significantly; the time for 50% to leave the stomach increased from 17.3 +/- 2.2 min to 34.7 +/- 8.0 min. The postprandial gastroduodenal motility was massively inhibited by oxyntomodulin. Postprandial trypsin and lipase output was significantly inhibited by 56 +/- 12% and 42 +/- 11%, respectively, during oxyntomodulin infusion. However, pancreatic enzyme output was linearly related to gastric emptying and oxyntomodulin did not influence this relationship, suggesting that oxyntomodulins effect was due to its effect on gastric emptying. Oxyntomodulin seems to play an important role in the small intestinal inhibitory control of gastropancreatic functions.
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PMID:Oxyntomodulin from distal gut. Role in regulation of gastric and pancreatic functions. 267 Apr 87

We report further characterisation of the hepatocyte growth factor 'hepatotropin' which is found in rat serum 24 h after partial hepatectomy. Hepatotropin enhances DNA synthesis in primary cultures of adult rat hepatocytes, and is of high molecular weight. Serum fractions were separated by gel filtration, heparin-sepharose affinity chromatography and ion-exchange chromatography. Sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) identified a band of apparent subunit relative molecular weight (Mr) 100,000 associated with biological activity, although purification to homogeneity has not been achieved. The activity is heat-labile, trypsin-sensitive, and stable to lyophilisation, but loses activity after dilution and reconcentration. In combination with known peptide hepatocyte growth modulators, hepatotropin acted synergistically with insulin and epidermal growth factor (EGF) but its action was not enhanced by glucagon. Studies on isolated rat hepatocyte membranes showed no evidence of enhanced phosphorylation of the EGF receptor by hepatotropin. The relationship of hepatotropin to previously described serum and platelet-derived growth factors is discussed.
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PMID:Further characterisation of 'hepatotropin', a high molecular weight hepatotrophic factor in rat serum. 268 95

Extralobular islet of Langerhans cells were isolated from the pancreas of an infant with intractable neonatal hypoglycemia (nesidioblastosis) by digestion with a mixture of trypsin and collagenase, and subsequent purification on a gradient of fetal calf serum. These islet cells cultured in Eagle's medium containing 20% fetal calf serum formed confluent endocrine cell monolayers within 15 days. These endocrine cells were studied immunocytochemically, and their secretion products were assayed by radioimmunological methods. The large numbers of beta, alpha and delta cells present in the islets before explanation remained functional in the cultures for 30 days. The beta cells secreted large amounts of insulin throughout this period, and secretion was stimulated by raising the glucose concentration in the medium from 5.6 to 16.8 mM. Initially there was little secretion of glucagon, but this increased during the subsequent 10 days in culture. It was not inhibited when the glucose concentration was raised from 5.6 to 16.8 mM. Somastostatin secretion remained stable throughout the period of culture, but tended to rise when the glucose concentration was increased. These results show that the culture of pancreatic cells from infants with nesidioblastosis provides an interesting in vitro system for studying the biological and biochemical characteristics of endocrine cells in the human pancreas.
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PMID:Culture of islets of Langerhans from an infant with intractable neonatal hypoglycemia: cytochemical and radioimmunological studies. 269 67

The intravenous administration of glucagon to anesthetized rats resulted within 5 min in a 20% drop in the hepatic phosphorylase phosphatase activity, as measured in a post-mitochondrial supernatant at low dilution, but it did not affect the activity of glycogensynthase phosphatase. On the other hand, the injection of insulin plus glucose caused increases by about 35% in both phosphatase activities. Upon subcellular fractionation these effects were recovered in the cytosol, but not in the glycogen/microsomal fraction. However, activity changes in the latter fraction were observed after recombination with the liver cytosol from a hormone-treated animal. Preincubation of the liver cytosol with modulator protein (a specific inhibitor of type-1 protein phosphatases) cancelled the activity changes induced by insulin plus glucose. No hormonal effects on hepatic protein phosphatase activities were observed when the fractions were either diluted an additional 10-fold or pretreated with trypsin. An acute hormonal regulation of protein phosphatases could also be demonstrated in the perfused liver. When added to the perfusion medium, glucose as well as insulin increased the cytosolic protein phosphatase activities by about 25%. Their effect was additive, irrespective of the order of addition. On the other hand, the addition of glucagon and/or vasopressin resulted in a 20% drop in the phosphorylase phosphatase activity. The presence of glucagon did not interfere with the effectiveness of insulin, and vice versa. The changes in the phosphorylase phosphatase activities induced by glucagon, insulin, and glucose represented changes in the Vmax only. We propose that the acute control of the hepatic glycogen synthase phosphatase and phosphorylase phosphatase activities is mediated by transferable, cytosolic effector(s).
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PMID:Acute regulation of hepatic protein phosphatases by glucagon, insulin, and glucose. 284 53

Angiotensin II (ANG II) was conjugated to polystyrene Latex fluorescent microspheres (0.5 or 0.05 micron diam) with carbodiimide. Biological activity of the ANG II-conjugated microspheres (ANG II microspheres) was assessed in dispersed hepatocytes. The 0.05 micron ANG II microspheres inhibited glucagon-stimulated adenosine 3',5'-cyclic monophosphate accumulation and stimulated phosphorylase activity in hepatocytes, whereas the 0.5 micron ANG II microspheres only stimulated phosphorylase activity. The biological activity of the ANG II microspheres was caused by the conjugated ANG II and not by "free" ANG II associated with the spheres or by trypsin-like activity of hepatocytes causing release of ANG II from the microspheres. Binding of 0.05 micron ANG II to hepatocytes was readily observed with fluorescence microscopy. Little, if any, binding was observed with microspheres without conjugated ANG II. This fluorescent preparation of ANG II may have great utility in the study of receptor behavior after binding in individual cells.
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PMID:Development of a new fluorescent angiotensin II probe. 284 96

Glucagon/PP-related peptides were detected immunohistochemically in 18 out of 22 cases of rectal tumors investigated. The reactive tumors showed prevalence of trabecular or mixed trabecular-acinar structure and moderate staining with Grimelius' silver and lead-hematoxylin. Three of the remaining 4 cases were characterized by reactivity for 5-hydroxytryptamine only, prevalence of a solid nest structural component and intense staining with Grimelius' silver technique and lead-hematoxylin. Fifteen of the 18 glucagon/PP-reactive cases were investigated immunohistochemically with a series of 6 sera directed against different sequences of glucagon, glicentin and proglucagon, and of 7 sera directed against PP, PYY and proPP-icosapeptide. A large spectrum of glucagon-related immunoreactivities, including C-terminus and mid-portion glucagon-immunoreactivity, N- and C-terminus glicentin-immunoreactivity, GLP1- and GLP2-immunoreactivity, were detected in human rectal L cells and most rectal carcinoids. With the exception of a few scattered cells in the rectal mucosa and in 3 tumors, C-terminus glucagon-immunoreactivity was obtained only after trypsin or subtilisin treatment of tissue sections. Both PYY and PP/proPP-like peptide(s) were detected in rectal L cells and carcinoids, with prevalence of PYY in normal cells and PP/proPP-like peptides in tumor cells. It is concluded that the same or closely related hormone/prohormone sequences are synthesized and stored in rectal endocrine cells and carcinoid tumors although differences of quantitative expression, post-translational cleavage or reactivity to antibodies may occur. The usefulness of protease treatments of tissue sections to unmask immunoreactivities of uncleaved propeptides or fixative-denatured peptides is outlined.
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PMID:Glucagon, glicentin, proglucagon, PYY, PP and proPP-icosapeptide immunoreactivities of rectal carcinoid tumors and related non-tumor cells. 288 65

A saponin fraction was isolated from Momordica charantia seeds by delipidation, saline extraction, ammonium sulfate precipitation, and extraction of the resulting supernatant with n-butanol. Thin-layer chromatography, in the upper phase of the n-butanol--ethyl acetate--water (4:1:5, by volume) system on plastic sheets coated with silica gel 60 F254, revealed the presence of a single spot after spraying with 10% sulfuric acid. The lack of contamination of the saponin preparation with proteins was judged by the absence of protein bands in sodium dodecyl sulfate--polyacrylamide gel electrophoresis, agarose electrophoresis and agarose diffusion, and by the absence of an absorption maximum around 278 nm. The saponin acted as a noncompetitive inhibitor of corticotropin, glucagon, and epinephrine in lipolysis in isolated rat adipocytes, and it also antagonized dibutyryl cAMP induced lipolysis. The antilipolytic activity was resistant to heat, trypsin, chymotrypsin, pronase, and glutathione, in keeping with the chemical nature of saponin. Incorporation of [3-3H]glucose into lipid was inhibited. Adipocyte viability and ATP content were not affected by the saponin, suggesting that its inhibitory effects on lipolysis and lipogenesis were not due to an adverse effect on cell viability.
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PMID:A steryl glycoside fraction from Momordica charantia seeds with an inhibitory action on lipid metabolism in vitro. 302 Nov 85

Calcitonin gene-related peptide (CGRP) has recently been identified in central and peripheral nerve fibres, including those of blood vessels supplying the exocrine pancreas, and in pancreatic islet cells. Moreover, receptors have been characterised in the same tissue. The present study examined the effects of human CGRP and of calcitonin on exocrine pancreatic secretion and on islet cell function in nine healthy volunteers. CGRP (300 ng/kg/h) caused, respectively, a 25% and 31% inhibition of caerulein stimulated trypsin and amylase output which was similar to that seen with calcitonin (300 ng/kg/h). Arginine stimulated insulin and glucagon release was unaffected by either CGRP, or calcitonin. Calcitonin gene-related peptide caused cutaneous flushing, but did not affect the pulse rate or arterial blood pressure in the doses tested. Calcitonin gene-related peptide inhibits exocrine pancreatic secretion in vivo in man, but does not affect islet cell hormone release.
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PMID:Effect of calcitonin and calcitonin gene-related peptide on pancreatic functions in man. 327 54

The effects of micelles of nonionic, zwitterionic, anionic and cationic surfactants and lipids on the conformation of glucagon and insulin have been investigated by circular dichroism and intrinsic protein fluorescence. The influence of these amphipathic compounds on the hydrolysis, monitored by HPLC, of glucagon and insulin by trypsin and chymotrypsin has also been studied. The alpha-helix content of glucagon was increased to a similar extent by all the micelles, irrespective of their charge and of whether they were synthetic surfactants or phospholipids. The amphipathic compounds always induced a blue-shift in the wavelength of maximum emission of fluorescence of glucagon of about 9 nm, whereas the fluorescence intensity was increased in some cases and decreased in others. The circular dichroism of insulin was also modified in some cases. Some amphipathic compounds protected glucagon against proteolysis by trypsin and chymotrypsin very markedly, whereas others did not protect at all or only slightly protected the hormone. Two hypotheses have been formulated to explain the different results. Hydrolysis of insulin was generally not influenced by surfactants and lipids.
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PMID:Conformation and proteolysis of glucagon and insulin in surfactant and lipid solutions. 328 14


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