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)

Among 88 unselected patients with chronic pancreatitis 35% (95% confidence limits 25 to 46) had insulin-dependent diabetes, 31% (21% to 41%) had non-insulin-dependent diabetes or impaired glucose tolerance (by intravenous glucose tolerance test), and 34% (24% to 45%) had normal glucose tolerance. B cell function measured by C-peptide concentration after 1 mg glucagon IV correlated with the pancreatic enzyme secretion (meal stimulated duodenal lipase content). B cell function was preserved to a greater extent (P less than .01), and glycosylated hemoglobin and fasting level of glucose were lower (P less than .01 to .05) in the 31 patients with pancreatogenic diabetes than than in 35 otherwise comparable patients with type I (insulin-dependent) diabetes, yet daily insulin dose was similar in the two groups. Glucagon stimulated C-peptide was inversely correlated to glycosylated hemoglobin in insulin-dependent patients with pancreatogenic diabetes and in type I diabetes. Since body mass indices were identical in the two groups, better glucoregulation was not due to reduced food intake or malabsorption in pancreatogenic diabetes. Rather residual B cell function and/or different secretion of other pancreatic hormones in pancreatogenic diabetes may account for different metabolic control in type I IDDM compared with insulin-dependent pancreatogenic diabetes.
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PMID:Metabolic control and B cell function in patients with insulin-dependent diabetes mellitus secondary to chronic pancreatitis. 330 47

Glucagon is structurally related to secretin but inhibits the effects of secretin and cholecystokinin (CCK) on pancreatic secretion in vivo. Because secretin is a weak stimulant of pancreatic growth and potentiates the trophic effects of CCK, we hypothesized that glucagon might inhibit CCK-induced pancreatic growth. Four groups of 10 rats were injected with saline, glucagon (30 micrograms/kg, equimolar to a known trophic dose of secretin), cerulein (0.67 microgram/kg), or glucagon plus cerulein every 8 h for 5 days. The pancreas was excised, weighed, and assayed for total content of DNA, protein, amylase, chymotrypsinogen, and lipase. In control and glucagon-alone groups, the small intestine was also removed, weighed, and assayed for DNA, protein, and disaccharidase content. Glucagon alone decreased pancreatic DNA and increased lipase content. Compared with cerulein-treated animals, animals treated with glucagon and cerulein showed significant decreases in pancreatic weight and content of protein, amylase, and chymotrypsinogen. Although glucagon had significant effects on intestinal protein, maltase, and sucrase contents in certain segments, there was no clear pattern of response. The data suggest that glucagon may be an inhibitory regulator of pancreatic growth, acting to block the effects of CCK on pancreatic hypertrophy.
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PMID:Glucagon inhibition of cerulein-induced hypertrophy of the exocrine pancreas. 336 38

Rat hearts were depleted in vivo from both the heparin-releasable lipoprotein lipase and heparin-resistant tissue neutral triacylglycerol lipase activity by treatment of the animals with cycloheximide (2 mg/kg body weight), intraperitoneally injected 2.5 and 5 h prior to perfusion. The tissue acid lipase, mono- and diacylglycerol lipase activities were not affected by cycloheximide-induced inhibition of protein synthesis. Myocardial basal and glucagon-stimulated lipolysis, determined by the rate of glycerol production and release from the isolated hearts, was not significantly different in control and cycloheximide-treated rats. Tissue triacylglycerols were recovered with the highest relative specific distribution in the lysosomal fraction isolated from heart homogenates. Upon prolongation of the perfusion-duration the relative specific distribution of triacylglycerols in the lysosomal fraction decreased. In addition, the specific lysosomal triacylglycerol content (micrograms/mg protein) dropped significantly, indicating an important role of lysosomes in myocardial triacylglycerol turnover. Our data strongly suggest that the heparin-resistant neutral triacylglycerol lipase activity may not be the only determinant of endogenous lipolysis in the isolated rat heart and indicate that lipolysis may additionally be mediated by the lysosomal, acid lipase in concert with the microsomal mono-and diacylglycerol lipase.
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PMID:Studies on the involvement of lipolytic enzymes in endogenous lipolysis of the isolated rat heart. 394 May 39

Evidence is presented that all lipase activities present in the vascular and myocardial tissue from rat heart are regulated by product inhibition. Lipoprotein lipase activity, which plays a role in the uptake of circulating triglycerides, is determined by its reaction products, e.g. fatty acids and, predominantly, monoglycerides. Tissue acid and neutral lipase activities are regulated by product fatty acids and their coenzyme A (CoA) and carnitine ester derivatives. The order of potency is palmitoyl CoA approximately palmitoyl carnitine greater than palmitate for neutral lipase and palmitoyl carnitine greater than palmitoyl CoA palmitate for acid lipase activity. Product inhibition of extracellular and intracellular lipolytic processes warrants a close coupling between the supply of substrate fatty acids and the rate of fatty acid oxidation as determined by cardiac contractile activity. None of the lipases studied was directly affected by catabolic hormones (norepinephrine, glucagon) or their intracellular second messengers (cyclic AMP, protein kinase, Ca2+, calmodulin).
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PMID:Regulation of lipases involved in the supply of substrate fatty acids for the heart. 400 68

The effect of glucagon on human exocrine pancreatic secretion was evaluated in ten patients by analysis of pure pancreatic juice. Pancreatic juice was obtained by endoscopic cannulation of the pancreatic duct at 2-min intervals during constant intravenous infusion of secretin (1 U per kg of body weight per hr) plus caerulein (0.04 micrograms per kg of body weight per hr). Since steady secretion was established 20 minutes after the start of juice collection, a further five 2-min fractions were collected as controls, then constant intravenous infusion of glucagon (15 micrograms per kg of body weight per hr) was commenced. Pancreatic juice was collected for a further 20 minutes. The control fractions and post-glucagon fractions were compared in each patient using Student's test. Glucagon depressed secretin-caerulein-stimulated pancreatic secretions. More uniform reductions were observed in the concentration and output of protein and enzymes. Individual variations were observed in the secretory volume and bicarbonate concentration and output. Amylase and lipase were depressed in a parallel fashion in seven patients and in the remaining three, amylase was more depressed than lipase. The post-glucagon reduction in pancreatic secretion was not proportional to the rise in plasma glucagon and blood glucose.
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PMID:Studies on the effect of glucagon on human pancreatic secretion by analysis of endoscopically obtained pure pancreatic juice. 401 95

Rat adipose tissue was homogenized in 0.154 m KCl, and the supernatant fluid, obtained after centrifugation at 15,000 g, was extracted with benzene to remove triglycerides. Most of the lipase activity in the extracted fluid was precipitated with ammonium sulfate between 15 and 40% saturation. The specific activity of the lipase in this fraction was about three times that in the benzene-extracted supernatant fluid. The specific activity of the monoglyceride esterase was increased to a lesser extent. Lipase activity in the benzene-extracted fluid and in the ammonium sulfate fraction was increased 15-45% by incubation with 0.3 mm ATP, 10 mm MgCl(2), and 0.03 mm cyclic AMP for 10 min before assay. None of these compounds alone or in combinations of two was as effective as all three together. The specific activity of the 15-40% ammonium sulfate fraction prepared from fat cells exposed to epinephrine and glucagon was greater than that from portions of the same cell pool not exposed to hormones. In addition, the already elevated lipase activity in preparations from hormone-treated cells was not enhanced by incubation with ATP, MgCl(2), and cyclic AMP. Thus, it seems probable that the lipase activity in the ammonium sulfate fractions represents, at least in part, hormone-sensitive lipase.
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PMID:Activation of hormone-sensitive lipase in extracts of adipose tissue. 432 64

Hormone-sensitive lipase partially purified from adipose tissue of laying hens was markedly activated by cyclic AMP-dependent protein kinase. Activation was approximately 4-fold (ranging up to as great as 10-fold) compared with the much lower degree of activation obtained with analogous preparations from rat and human adipose tissues (59 and 86%, respectively). The partially purified preparations contained adequate endogenous protein kinase activity to effect complete activation with addition of cyclic AMP, ATP, and Mg(2+). Activation was blocked by protein kinase inhibitor (from rabbit skeletal muscle) but could be restored fully by addition of excess exogenous protein kinase (from bovine skeletal muscle). The fully activated lipase was slowly deactivated by dialysis at 4 degrees C and then rapidly and almost fully reactivated by addition of cyclic AMP and ATP-Mg(2+). Reactivation was blocked by protein kinase inhibitor. This deactivation-reactivation cycle was rapid at 23 degrees C with dialysis against charcoal and could be demonstrated repeatedly using a single preparation. The reversible deactivation of protein kinase-activated enzyme is presumed to reflect the action of a lipase phosphatase. Lipase prepared from tissue previously exposed to glucagon yielded a much smaller degree of activation than lipase prepared from tissue not exposed to the lipolytic hormone, indicating that the physiological hormone-induced activation is probably similar to or identical with the protein kinase activation demonstrated in the cell-free preparations. Under the conditions of assay used, the partially purified lipase fraction contained diglyceride, monoglyceride, and lipoprotein lipase activities. However, treatment with cyclic AMP-dependent protein kinase had virtually no effect on these lipase activities.
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PMID:Reversible protein kinase activation of hormone-sensitive lipase from chicken adipose tissue. 437 88

Hypertriglyceridaemia is often observed in patients (1) with chronic renal insufficiency, (2) on haemodialysis and (3) after successful renal transplantation. HDL cholesterol is reduced in all three groups of patients and plasma cholesterol is elevated after renal transplantation. In these three patient groups type IV hyperlipoproteinaemia is found most frequently and after renal transplantation there is a relative increase in the incidence of type II hyperlipoproteinaemia. The role of glucagon resistance and carnitine deficiency in the alteration of fat metabolism seen in patients with chronic renal failure and patients on haemodialysis is discussed. Other factors which may influence fat metabolism in uraemia include calcium and vitamin D status as well as beta adrenergic receptor blocking agents and diuretics. Steroid therapy may be one cause of the hypercholesterolaemia and hypertriglyceridaemia seen after renal transplantation. PHLP lipase activity is reduced in all three groups of patients. In nephrotic syndrome, if hypercholesterolaemia occurs, the HDL cholesterol fraction is increased and thus the cardiovascular risk may be lower than in the three patient group mentioned above.
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PMID:[Alterations of fat metabolism in renal disease - pathogenetic mechanisms (author's transl)]. 612 54

The effects of different adrenergic agents on high density lipoprotein (HDL) cholesterol concentration and on the neutral NaCl-resistant triacylglycerol hydrolase (liver lipase) activity of the liver were studied in rats. Treatment of rats with the beta-blockers metoprolol, atenolol or propranolol led to a lowering of the HDL-cholesterol (esterified and non-esterified) content. The alpha 1-antagonist prazosin had no effect. Administration of norepinephrine for 10 days resulted in an increase of HDL non-esterified cholesterol. This effect of norepinephrine was largely abolished by prazosin, but not by propranolol. In normal rats the liver lipase activity was not influenced by alpha- or beta-blockade. Adrenergic stimulation, either short-term (by diethyl ether stress) or long-term (by norepinephrine treatment), led to a lowered liver lipase activity. The lipase activity was restored by prazosin but not by propranolol. The apparent involvement of the alpha 1-receptor in the regulation of liver lipase activity was further studied in vitro. Blockade of alpha- or beta-receptors with prazosin or propranolol did not affect the secretion of the liver lipase activity by isolated parenchymal liver cells. Stimulation of alpha- or beta-receptors by epinephrine led to a lower secreted lipase activity. Selective stimulation by isoprenaline had no effect. The effect of epinephrine could be abolished by prazosin but not by propranolol. Vasopressin and the calcium ionophore A23187 also lowered the secretion of liver lipase activity in vitro. Glucagon and/or the phosphodiesterase inhibitor Ro 20-1724 had no effect. These results indicate an involvement of the alpha 1-receptor in the regulation of liver lipase activity at the level of synthesis or secretion of the lipase. The effect of the alpha 1-receptor is presumably mediated through changes in the intracellular free calcium concentration. The effect of adrenergic modulation on HDL-cholesterol concentrations can partly be explained through modification of the liver lipase activity.
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PMID:Regulation of liver lipase. II. Involvement of the alpha 1-receptor. 614 7

The effect of salmon calcitonin (SMC) on pancreatic enzymes and hormones was investigated following retrograde choledocho-pancreatography (ERCP). 40 patients were randomly divided in two groups and 2.5 micrograms/h SMC or sodium chloride was infused intravenously for 28 hours. Infusion was started 4 hours before endoscopic procedure and amylase, lipase, glucose, insulin, glucagon and gastrin plasma concentrations were measured before and 2, 12 and 24 hours after the end of the ERCP. According to the radiological findings of pancreatography two additional groups were formed: group 1 with visualization of the main duct and its branches and group 2 with additional visualization of the pancreatic parenchyma. No change in glucose, insulin, glucagon and gastrin was found in any of the groups analyzed. Amylase and lipase showed a significant increase after 2 hours and 24 hours later, values were reached which were not significantly different to baseline levels. The time course of the plasma concentrations was identical in the patients treated by SMC or sodium chloride and showed no significant difference at the various time intervals. Therefore, inhibition of the known increase in pancreatic enzymes following ERCP was not found with SMC treatment.
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PMID:[The effect of salmon calcitonin on pancreatic enzymes and hormones before and after retrograde cholangiopancreatography]. 616 82


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