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)

Protamines are cationic fish chromosomal proteins that retard absorption of isophane (NPH) insulins. Protamines are also administered in large doses for heparin neutralization in cardiac procedures. This study used a rapid enzyme-linked immunosorbent assay to examine frequency of protamine antibodies in diabetic and control populations. Antigen specificity of the IgG binding to protamine-coated plates was verified by competitive inhibition with other protamines, histone, glucagon, thyroid-stimulating hormone, arginine, and lysine. All antibodies tested cross-reacted completely with all protamines. Only 4 of 18 had any cross-reactivity with histones. None cross-reacted with the other inhibitors. In population surveys, 122 (38%) of 319 NPH insulin-treated diabetic subjects, 3 (8%) of 39 diabetic subjects treated with protamine-free lente insulins, and 5 (2.5%) of 202 normal control subjects had protamine antibody. No correlation was found between insulin and protamine antibodies. Because more than one-third of insulin-treated diabetic subjects have circulating IgG specific for protamine, they are potentially at risk for acute immunologic or anaphylactoid reactions when protamine is administered for heparin neutralization.
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PMID:Frequency and specificity of protamine antibodies in diabetic and control subjects. 329 13

Glycyl-histidyl-lysine (GHL) has been shown to have growth stimulatory effects on a number of different cell types including hepatocytes and hepatoma cells. In this study, the effects of GHL on Morris hepatoma 7777 cells were investigated. The greatest stimulatory effects on 3H-thymidine and 3H-leucine incorporation were observed at a GHL concentration of 2 ng/ml. In randomly proliferating cells, the incorporation of 3H-thymidine into DNA increased by 50% and that of 3H-leucine into protein by 29%. In addition, synergistic effects were observed when insulin and glucagon were included with GHL in the incubation mixture. Experiments with cells rendered quiescent by serum starvation indicated that cells in the G1 phase of the cell cycle are more sensitive to GHL stimulation. In these experiments, 3H-thymidine incorporation increased earlier and peaked at a higher value than in the control cells. This finding suggests that GHL may play a role in stimulating quiescent cells to re-enter the cell cycle.
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PMID:Effects of glycyl-histidyl-lysine on Morris hepatoma 7777 cells. 331 36

1. Lysine and alanine uptake by pig enterocytes has been measured in piglet mid intestine both during normal development and 3 days after injection of dexamethasone and epidermal growth factor (EGF) into 3-day-old animals. 2. Alanine uptake measured in the presence of sodium increased markedly during the first 4 weeks of post-natal life. Similar effects on alanine uptake could be produced through injection of dexamethasone, but not EGF, into 3-day-old piglets. Alanine uptake measured in the absence of sodium and lysine uptake measured in the presence of sodium remained unchanged during development and unaffected by injection of dexamethasone or EGF. 3. Enterocytes capable of transporting alanine in the presence of sodium were found, by quantitative autoradiography, to cover the top 400 micron of the villus in 6-day-old and 3-4-week-old control pigs. Alanine concentrations in villus tip enterocytes in 3-4-week-old pigs were four times those found in 6-day-old animals. Qualitative examination of selected villi, however, showed alanine uptake taking place over a considerably greater area of villus surface in 6-day-old compared with 3-4-week-old animals. 4. Injection of dexamethasone and EGF into 3-day-old piglets caused an increase in crypt depth without apparent change in crypt cell proliferation. The rate at which enterocytes migrated out of the crypt and the length of individual villi also remained unchanged by dexamethasone or EGF injection. 5. Dexamethasone produces its effect on alanine uptake by acting on older enterocytes present on the upper part of the villus. These enterocytes can be shown, by calculations based on enterocyte migration rate, to have already been present on the villus at the time the pig was born. 6. The above findings are discussed in relation to the ability of villus as well as crypt enterocytes to change their programme of differentiation in response to external stimuli. The particular ability of dexamethasone to induce system A type carrier function is further discussed in relation to normal changes found to occur during neonatal development. It is finally suggested, as a working hypothesis, that endogenous glucagon might act as the final mediator of both developmentally controlled and dexamethasone-induced changes in amino acid transport.
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PMID:Dexamethasone selectively increases sodium-dependent alanine transport across neonatal piglet intestine. 350 67

Gabonase, an enzyme which acts on fibrinogen and factor XIII in uniquely thrombin-like ways, was purified to electrophoretic homogeneity from the venom of Bitis gabonica. On sodium dodecyl sulfate-polyacrylamide electrophoresis, the reduced protein behaved as a single chain with Mr = 30,600. The enzyme contains 20.6% carbohydrate, no free sulfhydryl groups and hence, from amino acid analysis, five disulfide bonds. Its extinction coefficient (E1%1cm) at 280 nm is 9.6. Its pI is 5.3. Gabonase has an active serine residue, is inactivated by phenylmethanesulfonyl fluoride, and has an active histidine which reacts with the chloromethyl ketone of tosyl-L-lysine. Its NH2-terminal amino acid sequence (Val-Val-Gly-Gly-Ala-Glu-Cys-Lys-Ile-Asp-Gly-His-Arg-Cys-Leu-Ala-Leu-Leu -Tyr-) is homologous to the B chain of thrombin. The activity of the enzyme is stabilized by calcium ion. It exhibits strong N alpha-p-tosyl-L-arginine methyl esterase activity, hydrolyzes tripeptide nitroanilide derivatives weakly or not at all, and cleaves no peptide bonds in insulin, glucagon, or the S peptide of ribonuclease. Gabonase clots fibrinogen with a specific activity of 45 NIH thrombin-equivalent units/mg, releasing both fibrinopeptides A and B and showing substrate inhibition at fibrinogen concentrations of 3 mg/ml or greater. The enzyme also activates factor XIII. It is not inactivated by either heparin or hirudin.
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PMID:Thrombin-like enzyme from the venom of Bitis gabonica. Purification, properties, and coagulant actions. 352 80

A thiol peptidase that catalyzes at near neutral pH the hydrolysis of insulin, the isolated A and B chains of insulin, and glucagon was purified from rat liver cytosol by fractionation on Sephadex G-200, Affi-Gel Blue, and Spherogel TSK-G 3000 SW. The purified enzyme showed a single component by chromatography on a Spherogel TSK column and by gel filtration on a Sephadex G-200 column. The native enzyme has a molecular weight of approximately 180,000 and consists of two subunits having pI's of 5.9 and 6.3. Studies on its substrate specificity showed that the purified enzyme degrades glucagon, insulin, insulin B chain, and insulin A chain, but it does not degrade proinsulin, ACTH, or denatured hemoglobin. Kinetic analyses were performed on three substrates. The Km values were: 34 nM for insulin, 276 nM for insulin B chain, and 3.5 microM for glucagon. The kcat and Vm/Km values were glucagon greater than B chain greater than insulin. Thus, the enzyme has the highest affinity/lowest efficiency for insulin, an intermediate affinity/intermediate efficiency for B chain of insulin and the lowest affinity/highest efficiency for glucagon. The effect of several potential activators and inhibitors on the enzyme's activity was investigated. The enzyme activity was markedly inhibited by N-ethylmaleimide, p-chloromercuribenzoic acid, iodoacetamide, and Np-tosyl-L-phenylalanine chloromethyl ketone (TPCK), and was partially inhibited by dithiothreitol, by the chelating agents EDTA and EGTA, and by phenylmethylsulfonyl fluoride (PMSF). Bacitracin inhibited the activity of the enzyme, but the protease inhibitors aprotinin, leupeptin, pepstatin, and phosphoramidon had little or no effect. Reduced glutathione, iodoacetate, and N alpha,p-tosyl-L-lysine chloromethyl ketone (TLCK) also had little or no effect on the enzyme activity.
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PMID:Purification and characterization of a rat liver cytosol neutral thiol peptidase that degrades glucagon, insulin, and isolated insulin A and B chains. 388 Oct 83

The relationships between changes in the plasma levels of immunoreactive insulin (IRI) and glucagon (IRG) in response to the postprandial increments of circulating amino acids were studied under normal physiological conditions in healthy dogs. In the presence of a unique postprandial physiological euglycemic "glucose clamp" which occurs in these dogs, plasma IRG rose to an earlier peak than IRI and both remained elevated for 16-19 hr. Amino acid (AA) profiles also showed postprandial incremental responses for up to 16 hr. Multiple correlation analyses indicated that only branched chain AAs were significantly correlated with IRI profiles and were devoid of a relationship to IRG. Similarly, only ornithine, lysine and glycine were significantly correlated with IRG profiles and devoid of a relationship to IRI. The significance of individual IRG stimulating effects of alanine and arginine were masked by other amino acid interactions, as significant intercorrelation was found among all 13 amino acids. Two equations were derived from the multiple regression analysis accounting for the postprandial time course of changes in IRI and IRG levels with only 5 amino acid concentrations: (1) (delta IRI) = 0.37 (delta Leu) -0.45(delta His), and (2) (delta IRG) = 0.55(delta Orn) + 0.37(delta Gly) -0.69 (delta Ser). These observations confirm the physiologic role in islet hormone secretion of the postprandial increments in circulating amino acids in the absence of glycemic change.
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PMID:Changes in blood amino acids account for the insulin and glucagon responses to mixed meals in dogs. 388 96

Three analogues of posterior pituitary hormones, 1-deamino-2-D-Tyr(OEt)-4-Val-8-Orn-vasotocin(dE-VVT), 1-deamino-2-D-Tyr(OEt)-4-Thr-8-Orn-vasotocin(dE-TVT) and 1-deamino-2-D-Tyr(OEt)-oxytocin(dE-OXY) were compared for their inhibitory effects on vasopressin (VP)-induced uterine activity in healthy women. At menstruation, during recording of intrauterine pressure (18 recording sessions in 11 women), intravenous infusion of lysine vasopressin (LVP, 1 ng/min/kg/body weight) induced an increase of the uterine activity and dysmenorrhoea-like symptoms. Intravenous injections of all analogues (10 micrograms/kg body weight) caused relief of symptoms and inhibition of uterine activity, dE-TVT was the most effective and dE-OXY was least active. With dE-TVT almost complete inhibition of contractions was seen during the first 10 min after injection. The duration of effect was also greatest with that analogue (40-50 min). Only dE-OXY had an agonist effect on spontaneous uterine activity. Pharmacokinetic studies of intravenous dE-TVT (10 ng/kg body weight) showed that the plasma half-life was approximately 16 min and the clearance 30 l/h. The bioavailability of 100 ng/kg given intranasally was about 5.5%. Further studies are recommended.
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PMID:Vasotocin analogues which competitively inhibit vasopressin stimulated uterine activity in healthy women. 394 2

Glucagon has been isolated from the pancreas of Torpedo marmorata, an elasmobranchian cartilaginous fish, and purified to homogeneity using only reverse-phase high-performance liquid chromatography. Amino acid sequence analysis indicates that the molecule differs from mammalian glucagon at position 3 (glutamic acid for glutamine), position 16 (asparagine for serine), and position 20 (lysine for glutamine). Extracts of T. marmorata intestine and brain were associated with glucagon-like immunoreactivity determined by radioimmunoassay using antisera directed against the C-terminal and N-terminal to central regions of porcine glucagon. Although elasmobranchian and teleostean fish are believed to have diverged from the main line of vertebrate evolution at about the same time, the structure of two glucagons from the teleost, Lophius americanus (anglerfish) differ from mammalian glucagon by seven and nine residues. This study supports the assertion that the structure of glucagon has been highly conserved during evolution and suggests that the considerable morphological development of the pancreas is teleosts was associated with an accelerated rate of molecular evolution.
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PMID:Primary structure of glucagon from an elasmobranchian fish. Torpedo marmorata. 407 59

1. The epigastric adipose tissue of rabbits has been prepared so that the effects of close arterial injections and infusions on blood flow and release of free fatty acids (FFA) can be studied. The effects of pharmacologically active agents and hormone preparations have been investigated.2. Release of FFA was stimulated by synthetic adrenocorticotrophic hormone (ACTH), alpha and beta melanophore stimulating hormone (MSH), porcine growth hormone, glucagon, thyrotropic hormone (TSH) and luteotropic hormone (LTH). Single injections of fat-mobilizing agents produce a sustained rise in the release of FFA.3. Although pitressin caused release of FFA, synthetic vasopressin and oxytocin failed to do so. The FFA releasing activity of pitressin has therefore been attributed to a contaminant.4. Catecholamines were found not to stimulate release of FFA from this fat depot, but were found to increase plasma FFA when infused intravenously.5. Injections of acetylcholine, histamine, bradykinin, 5-hydroxytryptamine, synthetic arginine vasopressin, and lysine vasopressin, oxytocin, angiotensin and FSH did not stimulate release of FFA although marked effects on blood flow were produced.6. Injections of prostaglandin E(1) gave sustained increases in blood flow, and inhibited FFA release when stimulated by growth hormone.7. The mobilization of FFA is sometimes associated with an increased rate of blood flow.
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PMID:The mobilization of free fatty acids from rabbit adipose tissue in situ. 430 78

The administration of glucagon to rats causes a marked increase in the phosphorylation of a specific serine residue in lysine-rich (f1) histone of liver during a one-hour period following the administration of the hormone. It is proposed that histone phosphorylation is the mechanism by which glucagon, and perhaps other hormones whose actions are mediated by adenosine 3',5'-cyclic phosphate (cyclic AMP), induce RNA synthesis in target tissues. The incorporation of (32)P-phosphate into lysine-rich histone is determined by isolation of a tryptic peptide which contains the phosphorylated serine residue. This peptide is identical to the major tryptic phosphopeptide obtained from lysine-rich histone after phosphorylation in vitro by a purified cyclic AMP-dependent liver histone kinase preparation; the partial sequence Lys-Ala-SerPO(4)(Thr,Ser,Glu,Pro(2),Gly,Val,Ile,Leu)Lys has been determined for the peptide. Hydrocortisone and adrenocorticotrophic hormone do not cause a detectable increase in histone phosphorylation in liver. However, insulin, which like glucagon induces an actinomycin sensitive synthesis of liver enzymes, also causes increased histone phosphorylation.
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PMID:Phosphorylation of liver histone following the administration of glucagon and insulin. 431 47


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