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)

Twenty to twenty-two days postcoitum mouse fetal pancreas organ bits were cultured on the dermal surface of irradiated pigskin as a substrate. The medium used for long term culture consisted of Eagle's Minimum Essential Medium with the addition of 10% bovine serum, 0.02 U/ml insulin, 0.025 microgram/ml glucagon, 3.63 microgram/ml hydrocortisone, 100 microgram/ml soybean trypsin inhibitor or 10(-8) M atropine. When the medium lacked trypsin inhibitor or atropine but contained the three hormones, the pigskin support began to be destroyed after 2 to 4 wk in culture. Thereafter, the cultured cells could not grow and survive on the digested pigskin. When 10(-6) M atropine was added to the medium, amylase secretion from cultured cells and destruction of pigskin were inhibited completely but pancreas cells could not grow or survive. In contrast, 100 microgram/ml soybean trypsin inhibitor or 10(-8) M atropine permitted cell growth, permitted amylase secretion from the cultured acinar cells, and prevented the destruction of pigskin. Under these conditions pancreas cells migrated or grew or both from the organ bits onto the surface of the pigskin dermis and organoid aggregations formed. Hydrocortisone was needed to permit growth for more than 2 wk. Glucagon and insulin had additive effects. Light and electron microscopic observations indicated the culture of at least five kinds of cells, i.e., duct, acinar, centroacinar, endocrine, and mesenchymal. The majority of cultured cells were duct cells and acinar cells. There were few mesenchymal cells. Mouse pancreas cells were cultured for at least 12 wk by this method.
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PMID:Duct, exocrine, and endocrine components of cultured fetal mouse pancreas. 618 9

The effects of dietary soybean trypsin inhibitor (SBTI, Kunitz type) or repeated i.p. injections of 95% pure cholecystokinin (CCK-39) on rat pancreas were investigated in a 10-day experiment. SBTI and CKK -39 induced similar increases in pancreatic weight, which led to both cellular hypertrophy and hyperplasia. Trypsin and chymotrypsin activity increased with an increase in pancreatic weight. Amylase activity increased only after CCK-39 injection, whereas lipase activity was not affected by either SBTI or CCK-39 treatment. After both treatments, insulin content showed only a slight tendency to increase, whereas glucagon content was not different from controls. The results indicate that SBTI and CCK-39 mainly exert their effects on the exocrine pancreas in a similar but not identical manner. It is therefore suggested that SBTI is not only a potent stimulator of the secretion of CCK activity but also of other unidentified gastrointestinal factor(s).
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PMID:The effect of feeding soybean trypsin inhibitor and repeated injections of cholecystokinin on rat pancreas. 620 62

An islet cell tumor, characterized by proinsulin level significantly elevated above normal human pancreas, has been found to contain insulin- and glucagon-degrading activity. Examination by chromatography on Sephadex G-75 of the degradation products formed from insulin showed A chain, and B chain rich-A chain aggregate as previously found with rat pancreatic islets. There was, however, little conversion of A chain to low molecular weight components indicating that insulinoma peptidase that has been found to degrade glucagon at about pH 6.8 degraded that A chain to a markedly lower rate. In contrast to the insulin-degrading activity, which was activated by glutathione in the presence of EDTA, the peptidase activity was not affected by the thiol compound. The activity of the peptidase was markedly inhibited by chelating agents, i.e., EDTA and o-phenanthroline, whereas chymotrypsin and trypsin inhibitors, i.e., TOS-PheCH2Cl, TOS-LysCH2Cl, soybean and pancreas trypsin inhibitor were found to have no effect.
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PMID:Thiol-protein disulfide oxidoreductase and peptidase activities in insulinoma tissue. 632 44

The conversion of proglucagon and proinsulin by secretory granules isolated from both prelabeled and unlabeled anglerfish islets was investigated. Either granules isolated from tissue labeled with [3H]tryptophan and [14C]isoleucine or [35S]cysteine, or lysed granules from unlabeled tissue to which exogenously labeled prohormones had been added were incubated under various conditions. Acetic acid extracts of these granule preparations were analyzed for prohormone and hormone content by gel filtration. Both prelabeled and lysed, unlabeled secretory granules converted radiolabeled precursor peptides (Mr 8,000-15,000) to labeled insulin and glucagon. The accuracy of the cleavage process was established by demonstrating comigration of products obtained from in vitro cleavage with insulin and glucagon extracted from intact islets using electrophoresis and high-pressure liquid chromatography (HPLC). The pH optimum for granule-mediated conversion was found to be in the range of pH 4.5-5.5. Conversion of both proglucagon and proinsulin by secretory granules was significantly inhibited in the presence of antipain, leupeptin, p-chloromercuribenzoate (PCMB) or dithiodipyridine (DDP) but not chloroquine, diisopropyl fluorophosphate, EDTA, p-nitrophenyl guanidinobenzoate, soybean trypsin inhibitor, or N-p-tosyl-L-lysine chloromethyl ketone HCl. The inhibitory action of PCMB and DDP was reversed in the presence of dithiothreitol. Both membranous and soluble components of the secretory granules possessed significant converting activity. HPLC and electrophoretic analysis of cleavage products demonstrated that the converting activities of the membranous and soluble components were indistinguishable. The amount of inhibition of proinsulin and proglucagon conversion caused by 600 micrograms/ml porcine proinsulin was significantly lower than that caused by the same concentration of unlabeled anglerfish precursor peptides. These results indicate that the proinsulin and proglucagon converting enzyme(s) in the anglerfish pancreatic islet is a unique intracellular thiol proteinase(s) that may be granule membrane-associated and may require the presence of prohormone sequences in addition to the dibasic residues at cleavage sites for substrate recognition and/or binding.
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PMID:Characterization of proinsulin- and proglucagon-converting activities in isolated islet secretory granules. 702 70

1. Inflammatory responses were induced by the injection of carrageenin into the rat paw and lymph was collected by cannulation of the thoracic duct. Cell-free lymph samples were intracutaneously injected into a second group of rats to measure vascular permeability activity by local exudation of Evans blue. 2. The vascular permeability activity in lymph samples draining inflamed tissue was consistently higher than in lymph from normal controls. Activity increased with the development of inflammation, attaining maximum values 2 to 2.5 h after the injection of carrageenin. 3. The activity was reduced by pretreatment of lymph donors with indomethacin or soybean trypsin inhibitor. Pretreatment of the animals used to measure vascular permeability activity with diphenhydramine or methysergide attenuated their responses to the permeability factors present in lymph. Thus prostaglandins, kinins, vasoactive amines or their generating systems may have contributed to the total activity detected. 4. Pretreatment of lymph donors with corticosterone or glucagon, whose anti-inflammatory action is mediated by the release of endogenous corticosteroids, did not alter the amount of activity in lymph. 5. These data suggest that the formation of the permeability factors present in lymph draining inflamed tissue was not affected by corticosteroids. We conclude that corticosteroids do not exert their anti-inflammatory activity at this level.
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PMID:Permeability factors in lymph draining inflamed tissues: effect of anti-inflammatory drugs. 730 23

Pancreatic trophism and pancreatic enzyme composition, and plasma levels of cholecystokinin, insulin, glucagon, and glucose in liver cirrhosis induced by chronic thioacetamide administration (0.02% in the drinking water for 12 mo) were studied in rats. Advanced liver cirrhosis was evident in all thioacetamide-treated rats. The weight of the pancreas and its contents of DNA, protein, trypsinogen, chymotrypsinogen, proelastase, secretory trypsin inhibitor, and amylase were significantly increased as compared to the controls. The pancreatic secretory enzyme content changes showed a nonparallelism, characteristic of a cholecystokinin effect. Light and electron microscopy revealed a normal pancreatic architecture. Bioassayed plasma cholecystokinin levels in both fed and 24-h-fasted cirrhotic rats were significantly higher than in the corresponding controls. The plasma glucose, insulin, and glucagon levels demonstrated hypoglycemic tendencies with a glucagon predominance. These findings indicate that advanced liver cirrhosis in the rat is accompanied by pancreatic hypertrophy and hyperplasia, which might be attributed, at least in part, to elevated circulating cholecystokinin levels.
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PMID:Pancreatic trophism in experimental liver cirrhosis. 828 79

A novel trypsin-like serine proteinase was purified to homogeneity from the bovine pancreas microsome fraction. The enzyme was solubilized with 3-[(3-cholamidopropyl)-dimethyl-ammonio]-1-propanesulfonate (CHAPS), and purified by a series of column chromatographic steps on Ultrogel AcA-34, trypsin inhibitor-Sepharose 4B, and arginine-Sepharose 4B. The molecular mass of this pancreas trypsin-like proteinase (bPTLP) was estimated to be 29.5 kDa by SDS-PAGE under reducing conditions. The NH2-terminal sequence of bPTLP is very homologous, but not identical to those of other serine proteinases, especially such as elastases IV, II, and III. Substrate specificity studies involving a synthetic substrate and glucagon indicated that the enzyme hydrolyzes Arg-X, Lys-X, and Leu-X bonds. The best synthetic substrate for bPTLP was t-butyloxycarbonyl Gln-Arg-Arg-4-methylcoumaryl 7-amide. The enzyme failed to hydrolyze the substrate for chymotrypsin and elastase. The enzyme activity was inhibited by diisopropyl fluorophosphate, p-amidinophenylmethane sulfonylfluoride, and leupeptin, indicating that it is a serine-proteinase. These findings show that bPTLP is a novel serine-proteinase which differs from all known proteinases. The physiological function of the enzyme has yet to be determined.
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PMID:Purification and characterization of a novel serine proteinase from the microsomal fraction of bovine pancreas. 890 82


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