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)

Immunoassay of gut extracts showed the presence of glucagon-like immunoreactivity (GLI) from the stomach to the colon of the cat with maximal concentrations in the ileum and colon. Twenty percent glucose perfused through the lumen of the jejunum, ileum, or colon produced an increase in GLI concentration in the venous effluent of the segment only in the case of the colon. The amount of GLI released was not sufficient to alter peripheral plasma concentrations.
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PMID:Regional release of glucagon-like immunoreactivity from the intestine of the cat. 86 76

A protein from porcine gut with 100 amino acid residues (porcine gut GLI-1) and having glucagon-like immunoreactivity has been characterized by partial sequences. The sequence of the C-terminal amino acid residues is -Met-Asn-Thr-Lys-Arg-Asn-Lys-Asn-Asn-Ile-Ala and includes the C-terminal amino acid residue sequence (-Met-Asn-Thr) of porcine glucagon. Evidence is presented that the glucagon sequence -Thr-Ser-Asp-Tyr-Ser-Lys-Tyr- is found in the gut GLI-1 as well. The data support the theory that gut GLI-1 contains the full glucagon sequence and that gut GLI-1 and glucagon are formed from a common precursor.
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PMID:Sequence analysis of porcine gut GLI-1. 88 77

To produce a carboxy-terminal specific antiserum against pancreatic glucagon, glucagon was coupled mainly via its amino-terminal histidine to thyroglobulin, using the amino group reactive pentandial at pH 7.0 for the conjugation procedure. After repeated immunization of rabbits, one high titer antiserum was obtained with a combining site recognizing a part of the carboxy-terminal portion of glucagon as judged from the cross-reaction curves with glucagon fragments, duck pancreatic glucagon and gut glucagon-like immunoreactive substances. There was no cross-reaction with secretin, vasoactive intestinal peptide, and gastric inhibitory peptide. In spite of strong immunoreactive similarities with the antiserum 30K (Unger) this antiserum results in determinations of a somewhat higher amount of plasma immunoreactive glucagon (IRG). The difference was found to depend on a higher content of IRG with a molecular size close to immunoglobulin IgG. A patient with agamma-globulinemia had no measurable IRG of molecular size close to that of IgG, indicating a possible competitive binding of some immunoglobulins to the antiserum.
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PMID:Production and characterization of an antiserum against pancreatic glucagon. 91 16

Gut glucagon-like immunoreactivity (GLI) was extracted from the mucosa of the canine intestine and was separated into two peaks by gel filtration; Peak I (7,000 daltons) and Peak II (3,500 daltons). These two peaks were purified by means of affinity chromatography using an anti-glucagon antibody as a ligand substance. These purified gut GLIs were not composed of single component, when applied to ion exchange chromatography. These partially purified Peak I and Peak II showed lipolytic activities, though very weak in potency, in vitro on the rat fat tissue at pharmacologically high concentration (5 ng eq/ml in final). It was concluded that gut GLI, even though purified, showed heterogeneity and that gut GLI revealed lipolytic activity although weak in potency compared with pancreatic glucagon.
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PMID:Heterogeneity of extractable gut glucagon-like immunoreactivity (GLI) and its lipolytic activity. 92 46

In order to clarify the nature of the biological action of gut glucagon-like immunoreactivity (GLI), GLI was extracted from the mucosa of the canine intestine and purified by gel filtration and affinity chromatography. 1500 gm of the mucosa yielded approximately 7 gm of crude extract of GLI. This crude extract was applied to a column packed with Sephadex G-50 or Bio-Gel P-10 and two peaks were obtained, Peak I and II. Each peak was purified with affinity chromatography, bound to gamma-globulin of anti-glucagon rabbit-serum. In this step, the GLI was purified approximately 80 times in comparison with the crude extract. Peak I or Peak II, as well as pancreatic glucagon, was infused successively into the pancreaticoduodenal artery of the anesthetized dogs. When buffer solution or the Peak I GLI was infused, the plasma immunoreactive insulin in the pancreatic vein did not change significantly. In contrast, both the Peak II and pancreatic glucagon promoted insulin secretion from the pancreas. The results obtained in this experiment demonstrate the promotion of insulin release from the pancreas and suggest an important role of gut GLI in the absorption and metabolic processing of nutrients.
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PMID:Purification of canine gut glucagon-like immunoreactivity (GLI) and its insulin releasing activity. 93 62

Radioimmunoassay of acid ethanol extracts of the rat intestinal tract showed the presence of glucagon-like immunoreactivity (GLI) from the duodenum to the colon with maximal concentrations in the ileum and colon. Twenty percent glucose instilled in the duodenum at a dose of 2g/kg body weight stimulated a twofold increase in peripheral plasma GLI concentration. When the instilled glucose load was restricted to only the duodenum and jejunum, or to only the ileum and colon, the increase in peripheral plasma GLI was approximately half that seen when the entire gut was exposed to the glucose. It is concluded that the distal gut as well as the proximal gut releases GLI in the rat.
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PMID:The contribution of the distal gastrointestinal tract to glucagon-like immunoreactivity secretion in the rat. 96 99

Numerous epithelial cells in the oxyntic gland area of the stomach of cat and dog appear to store pancreatic-type glucagon, as evidenced by immunohistochemistry and--in the case of the dog--also by radioimmunoanalysis. No glucagon immunoreactive cells are found in the antropyloric mucosa. Disseminated cells in the intestinal mucosa store gut-type glucagon. In all species studied, these cells predominate in ileum and colon.
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PMID:Distribution and properties of glucagon immunoreactivity in the digestive tract of various mammals: an immunohistochemical and immunochemical study. 110 1

Gut glucagon-like immunoreactivity (GLI) was extracted from plasma of dogs and was compared for its molecular size and insulin releasing activity with GLI present in the intestine. Plasma was obtained from the portal vein of dogs, of which the pancreas was removed as rapidly as possible during the glucose administration into the intestine. Plasma GLI of intestinal origin was extracted by a modification of Kenny's method. The amount of GLI extractable from plasma in each dog ranged from 4.30 to 25.74 ng. The extract of plasma during glucose absorption was observed to have two peaks on gel filtration, corresponding to Peak I and Peak II of GLI extracted from the gastrointestinal tract. The intrapancreatic infusion of the Peak II GLI extractable from plasma promoted remarkable insulin release in dogs, like pancreatic glucagon. In contrast, the Peak I GLI from plasma caused an equivocal rise of insulin in the pancreatic vein. It is concluded from the experiment that gut GLI extracted from plasma shows the same elution pattern on gel filtration and the same insulin releasing activity as GLI extractable from the gut.
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PMID:Plasma glucagon-like immunoreactivity (GLI) in dogs. 114 15

Duck intestinal extracts were separated into three main peaks of proteins by chromatography on P6 BioGel columns. The first, which crossreacted with glucagon antibodies, gut "GLI", did not stimulate lipolysis in isolated chicken adipocytes. Both second and third peaks, corresponding to smaller molecular-size peptides were even more lipolytic than pancreatic glucagon.
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PMID:The contribution of the pancreas and the intestine to the regulation of lipolysis in birds. I. Existence of highly potent lipolytic factors in ileum extracts. 115 Jan 30

The effects of repeated injections of 75 U crude cholecystolinin-pancreozymin (CCK-PZ) at increasing plateau glucose concentrations achieved by glucose infusion were studied in 15 controls, 8 chronic pancreatitics and 8 mild maturity onset diabetics. In control subjects CCK-PZ alone caused minor insulin release but proportinally greater secretion with increasing blood glucose concentrations. Chronic pancreatitis patients who had normal responses to intravenous glucose responded normally to the CCK-PZ but at significantly higher plateau glucose levels. Diabetics had no response to IV glucose boluses of 5 g or 10 g, but with glucose infusions of 250-500 mg/min had almost normal insulin responses to CCK-PZ. The responses to CCK-PZ plus glucose were greater than either stimulus alone, indicating an interaction between these and the beta cell. These studies suggest that the gut homone-receptor in the beta cell is intact in maturity onset diabetes and chronic pancreatitis, whether the glucose receptor is normal or defective. The peptide-responsible in the crude CCK-PZ is not secretin, glucagon or gut glucagon, but may be gastric inhibitory polypeptide (GIP) since pure CCK-PZ has no insuli releasing properties.
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PMID:Insulin responses to crude cholecystokinin-pancreozymin in normal subjects, in patients with chronic pancreatitis and patients with mild maturity onset diabetes. 115 Aug 59


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