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)

Immune responses result in a variety of metabolic adjustments that are mediated by cytokines of leukocytic origin. Of the dozens of cytokines released during an immune response, interleukin-1 (IL-1), tumor necrosis factor alpha (TNF alpha) and interleukin-6 (IL-6) are the major mediators of intermediary metabolism. These three cytokines act in concert to decrease food intake, increase resting energy expenditure, gluconeogenesis, glucose oxidation, and hepatic synthesis of fatty acids and acute phase proteins, decrease fatty acid uptake by adipocytes and alter the distribution of zinc, iron and copper. Most of these activities result from direct interactions between the cytokine and the responding cells. IL-1, TNF alpha and IL-6 also affect changes in metabolism by changing levels of circulating insulin, glucagon and corticosterone. The nutritional impact of these metabolic changes is dependent upon age. In growing animals, increases in energy expenditure and oxidation of amino acids are balanced by lower needs associated with growth. In adult animals, energy and amino acid requirements are increased by an amount similar to the increased basal metabolic rate and amino acid oxidation. Nutrition also influences the release of cytokines and consequently affects regulation of the immune response. For example, protein deficiency results in decreased IL-1 release and impaired tissue responses to IL-1.
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PMID:Nutritional aspects of leukocytic cytokines. 306 44

In order to study the effect of hyperglucagonaemia on nitrogen metabolism in diabetes, zinc protamine glucagon 60 micrograms was injected subcutaneously 3 times daily for 4 weeks into streptozotocin diabetic rats (n = 5), adequately treated with long acting insulin. This raised the plasma concentration of glucagon to 725 +/- 125 (mean +/- SEM), which is not different from that found in portal blood of uncontrolled diabetic rats: 400 +/- 75 ng/l. The controls were 5 diabetic rats treated with insulin alone and 5 non-diabetic rats. Compared with control rats the nitrogen balance was reduced (p less than 0.05) and the nitrogen contents of carcass, heart, intestines, and kidneys were reduced by 15-30% (p less than 0.05) in the glucagon treated rats. The hepatic capacity of urea synthesis and the alanine elimination rate were determined in the 3 above-mentioned groups, and confirmed in 3 identical groups followed for only 2 weeks; and in addition in a group of glucagon treated diabetic rats, where the long acting glucagon was substituted by neutral insulin the last two days before investigation.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Exogenous hyperglucagonaemia in insulin controlled diabetic rats increases urea excretion and nitrogen loss from organs. 306 29

The present study determines the effect of glucagon on the behavior of zinc, copper, calcium and magnesium ions in human plasma and urine. Five normal adults were submitted to intravenous infusion of 2.0 mg glucagon over a period of 120 min. A decrease in plasma magnesium and copper was observed with no significant change in urine ion concentrations. We related plasma magnesium mobilization to glucagon, and copper mobilization to plasma variation in free fatty acids and albumin.
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PMID:Metabolic effects of glucagon on plasma and urine zinc, copper, calcium and magnesium levels. 317 77

Glucagon administration is known to increase urinary inorganic phosphate (Pi) excretion. We have now confirmed that this effect also occurs in mice. While, at lower glucagon doses, phosphaturia was accompanied by a decrease in plasma Pi, at the highest dose of glucagon plasma Pi was not altered in spite of a massive increase in urinary Pi. This suggested that glucagon may additionally have another effect on phosphate homeostasis, i.e. of mobilizing Pi from body stores. In order to distinguish between the renal and extrarenal effects of glucagon, the animals were fed a low-phosphate diet, a procedure known to blunt the effect of several phosphaturic agents. Under these conditions, any Pi mobilized from body stores should be reflected by an increment of plasma Pi. Glucagon phosphaturia was indeed blunted under this condition. Furthermore, plasma Pi increased spontaneously by 0.82 +/- 0.14 mmol/l (mean +/- SEM) in an experimental period of 8 h during which the mice were fasted. In mice injected with zinc-protamine-glucagon subcutaneously at 4 and 16 micrograms/g of body weight, plasma Pi increased by 1.45 +/- 0.17 and 2.38 +/- 0.14 mmol/l during 8 h, respectively. Thus, it appears that exogenous glucagon is a strong Pi-mobilizing hormone. Furthermore, during the recovery phase following insulin-induced hypoglycemia, in which glucagon is thought to play a primordial role, a similar Pi mobilization to that obtained after glucagon administration was observed. Thus, since glucagon is released during fasting to maintain the homeostasis of blood glucose, it is conceivable that the mobilization of Pi induced by fasting might also have been caused by endogenous glucagon and that this hormone might be involved in Pi homeostasis.
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PMID:Effects of glucagon on renal and extrarenal handling of inorganic phosphate in mice: evidence for inorganic phosphate mobilizing activity. 329 8

Insulin from the principal islets of the teleost fish, Cottus scorpius (daddy sculpin), has been isolated and sequenced. Purification involved acid/alcohol extraction, gel filtration, and reverse-phase high-performance liquid chromatography to yield nearly 1 mg pure insulin/g wet weight islet tissue. Biological potency was estimated as 40% compared to porcine insulin. The sculpin insulin crystallised in the absence of zinc ions although zinc is known to be present in the islets in significant amounts. Two other hormones, glucagon and pancreatic polypeptide, were copurified with the insulin, and an N-terminal sequence for pancreatic polypeptide was determined. The primary structure of sculpin insulin shows a number of sequence changes unique so far amongst teleost fish. These changes occur at A14 (Arg), A15 (Val), and B2 (Asp). The B chain contains 29 amino acids and there is no N-terminal extension as seen with several other fish. Presumably as a result of the amino acid substitutions, sculpin insulin does not readily form crystals containing zinc-insulin hexamers, despite the presence of the coordinating B10 His.
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PMID:The isolation, purification and amino-acid sequence of insulin from the teleost fish Cottus scorpius (daddy sculpin). 352 55

The effect of zinc deficiency on glucose tolerance was investigated using intragastric force feeding to obviate decreased food intake and altered eating patterns. Three groups of weanling male Sprague-Dawley rats were fed a purified zinc-deficient diet: zinc-deficient, ad libitum-fed animals (ZDA) were offered powdered zinc-deficient diet; zinc-replete, force-fed controls (ZRF) were tube fed a diet blended with water containing 25 ppm of zinc; zinc-deficient, force-fed animals (ZDF) were similarly tube fed the zinc-deficient diet. The ZRF and ZDF groups received a diet of identical amount based on the intake of ad libitum-fed, zinc-replete rats. After 8 days of feeding, the ZDF group had impaired glucose tolerance curves, yet blood insulin and glucagon levels were normal. The ZDA group had normal glucose tolerance with low insulin levels compared with the ZRF group. The islet cell morphology among the three dietary groups were similar. These results suggest that the glucose intolerance observed in ZDF rats is not due to altered blood insulin and glucagon levels but rather to peripheral resistance to insulin action.
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PMID:Effect of pure zinc deficiency on glucose tolerance and insulin and glucagon levels. 352 81

Hepatocytes are in a dynamic equilibrium with the plasma zinc supply. Kinetic analysis of zinc uptake by isolated rat liver parenchymal cells defines two intracellular pools. In one pool zinc is bound relatively weakly and equilibrates rapidly with the medium at 37 degrees C. In the other pool zinc is bound tightly and interacts with the medium slowly at 37 degrees C. Of the two intracellular pools, the slower responding component represents an exchange process with the bulk of total cell zinc. The slow phase of uptake is saturable with albumin in the medium. The smaller pool is in rapid equilibrium with the medium and represents a labile zinc pool that accounts for net zinc accumulation. Both intracellular pools respond to hormonal stimuli. The factors that augment the uptake/exchange of zinc, namely glucocorticoids, glucagon, epinephrine, and dibutyryl cyclic AMP, are also those that stimulate metallothionein gene expression in hepatocytes. Changes in zinc flux into intracellular pools are directly related to the metallothionein content of hepatocytes. Characteristics of the labile zinc pool suggest that it may serve as an initial intermediate in zinc metabolism by hepatocytes as well as more general aspects of liver function related to zinc.
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PMID:Zinc uptake and metabolism by hepatocytes. 353 46

An endopeptidase (LEP-II), which has a unique substrate specificity, was purified to homogeneity by conventional chromatographic techniques from Streptococcus cremoris H61. The enzyme was a metalloendopeptidase since it was inhibited by EDTA and 1,10-phenanthroline; the metal-depleted enzyme could be fully reactivated by micromolar levels of Zn2+ and was not inhibited by specific inhibitors for serine or thiol protease. The molecular mass of the enzyme was estimated to be 80 kDa by Sephacryl S-300 gel filtration and high-performance liquid chromatography with a TSK-G3000SW column. The enzyme consisted of two identical subunits and the N-terminal sequence of LEP-II was determined up to the 19th residue. Although the enzyme had a broad substrate specificity it specifically hydrolyzed the peptide bonds involving the amino groups of hydrophobic amino acid residues. Various small polypeptides, such as alpha s1-CN(f1-23), alpha s1-CN(f91-100), oxidized insulin B chain, glucagon and some biologically active peptides were hydrolyzed. However, a variety of larger polypeptides or proteins, such as alpha s1-CN(f1-54), alpha s1-CN(f61-123), alpha s1-CN(f136-196), alpha s1-casein, beta-casein, and kappa-casein were not hydrolyzed. LEP-II recognized the size of its substrates, which were limited below a molecular mass of about 3.5 kDa.
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PMID:Purification and characterization of a novel metalloendopeptidase from Streptococcus cremoris H61. A metalloendopeptidase that recognizes the size of its substrate. 354 30

The effect of glucagon on the capacity of urea-N synthesis was examined in 24 rats as a function of time. First, the conditions for saturation of urea synthesis under glucagon influence were studied by the kinetics of urea-N synthesis rate in relation to arterial blood alpha-amino-N concentration between 5 and 17 mmol/l in 21 nephrectomized rats given zinc-glucagon (20 micrograms s.c. per day) for 14 days. Alanine was infused so that steady state concentrations of total alpha-amino-N was attained in each rat. The urea-N synthesis rate was calculated as accumulation in total body water corrected for intestinal hydrolysis. The relationship suggested a barrier limited substrate inhibition kinetics, as earlier found in control rats, and data were examined accordingly by non-linear regression analysis. The estimated kinetic constants were: Vmax = 71 mumol/(min X 100 g body wt), Km = 5.4 mmol/l, Ki = 2.4 mmol/l, and the barrier = 4.4 mmol/l. Vmax was increased three times compared with controls. The capacity of urea-N synthesis, i.e. the zenith of the relation, was attained in the concentration interval 7.5 to 12.0 mmol/l, as in controls. The capacity of urea-N synthesis was determined during i.v. infusion of zinc-glucagon (0.15 microgram per min) and after 2, 8, and 14 days of daily s.c. injections of 20 micrograms zinc-glucagon. Rats given zinc-protamine solution were controls.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Time dependent stimulating effect of glucagon on the capacity of urea-N synthesis in rats. 355 84

This report describes measurements of 50 variables in adult, female, reproductively inactive Vervet monkeys during prolonged nutrition realistic for westernized people. Dietary treatments consisted of an atherogenic Western diet (WD) and a prudent Western diet (PD). Ingredients were normal foods for man and no extra cholesterol was added. Fortification of both diets with vitamin C after cooking was necessary to prevent deficiency. Randomised groups of Vervet monkeys received either the PD or WD for 47 months, while a third group was fed WD for 20 months and then PD for 27 months (WD-PD). Before the dietary treatments nourishment was by a high carbohydrate diet (HCD) and baseline and reference values (RV) apply to this nutritional status. Plasma total cholesterol (mg/dl) was increased from 147 (HCD) to 174 (PD) and 376 (WD). Individual cholesterolaemio response ranged from mild to severe and was stable (PD and WD). Dietary reversal (WD-PD) reduced cholesterolaemia promptly. Statistically significant increases in calcium, zinc and vitamin E and decreased vitamin B6 were associated with the WD relative to the PD (in serum and plasma). Two cholesterol metabolising microsomal enzymes in liver were notably increased and one unchanged (WD). There were no dietary effects on triglycerides, vitamin A and glucose in plasma; insulin, glucagon, electrolytes, copper, magnesium or enzymes reflecting liver, muscle or brain cell damage in serum. Red blood cells, platelets and directly associated parameters increased (WD), haemoglobin was the same and haemoglobin per red cell decreased. Bleeding time was not affected. Bivariate correlations across the diets confirmed that Western nutrition promoted inherent individual susceptibility to cholesterolaemia. There were notable differences from RVs in total cholesterol, calcium, packed cell volume and haemoglobin, which emphasise excesses and deficiencies of the WD and PD.
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PMID:Diets realistic for westernized people significantly effect lipoproteins, calcium, zinc, vitamins C, E, B6 and haematology in vervet monkeys. 363 58


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