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)

Specific GH binding sites in isolated rat adipocytes have been partially characterized. Binding of [125I]iodohuman(h)GH was rapid, reversible, and was time and temperature dependent. Maximum specific binding occurred at 37 C in approximately 40 min at pH 7.4. Bound labeled hGH was rapidly dissociable, with the addition of excess unlabeled hormone. Specific binding is inhibited by as little as 1.0-1.5 ng/ml hGH, and 50% inhibition was obtained with 15-20 ng/ml. No inhibition was observed with insulin, glucagon, hPRL, or hTSH at concentrations up to 1 micrograms/ml. This receptor does not discriminate between monkey GH, rat GH, bovine GH, and porcine GH. Specific binding varied linearly with cell concentration. Scatchard analysis revealed linear plots with a Ka of approximately 10(9) M-1 and 15,000 sites per cell. There was less than 15% degradation of [125I]iodo-hGH over 90 min at 37 C. There was a striking increase in [125I]iodo-hGH binding to adipocytes at pH 4.85. Scatchard analysis of binding at pH 4.85 revealed a curvilinear plot with an apparent increase of sites per cell from 15,000 to 60,000, and a modest increase in the apparent affinity constant of the high affinity, low capacity sites using the two-compartment model for curvilinear plots. The GH receptors in rat fat cells displayed no ability to bind labeled hPRL or human placental lactogen, consistent with minimal recognition of lactogenic peptides by these receptors. Thus, the rat adipocyte contains specific binding sites for GH that fulfill the major criteria for receptor binding. The presence of such receptors in these cells may facilitate the study of GH receptors in relation to the biological effects of the hormone on adipose tissue in various metabolic settings.
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PMID:Growth hormone receptors in isolated rat adipocytes. 627 42

Oral glucose tolerance, plasma insulin and basal levels of glucagon, hGH, hPRL, hPL, TSH, T4, T3, thyroxine-binding globulin (TBG), cortisol, corticosteroid-binding globulin (CBG) and estriol were measured in 23 normal pregnant women in late gestation (31 +/- 0.4 weeks of pregnancy). Twelve of these subjects could be re-examined 14 +/- 2 weeks postpartum. Blood glucose was lower basal and after glucose load (100 g) in the pregnant group. Fasting plasma insulin and glucose-induced insulin release were higher in pregnancy. The insulinogenic index and the beta cell response were significantly greater antepartum, while peripheral insulin activity was unchanged. The insulin:glucagon ratio as well as TSH and hGH showed no significant differences between ante- and postpartum values. However, T4, T3, TBG, cortisol, CBG, estriol, hPRL and hPL were significantly higher during gestation than after delivery. T4:TBG and T3:TBG ratios were much lower antepartum, while the cortisol:CBG ratio was comparable ante- and postpartum. To our knowledge this is the first report in which such an extensive hormonal and metabolic analysis was performed in the same women ante- and postpartum. It could be shown that glucose tolerance is not worsened during pregnancy in healthy subjects. The higher gestational insulin values are discussed with respect to the various significant hormonal changes.
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PMID:Hormonal profile and glucose tolerance in late pregnancy and postpartum. 635 85

Human and porcine insulin were administered intravenously to a group of healthy volunteers in two different doses (0.075 IU/kg body weight and 0.12 IU/kg body weight) and to two groups of randomly selected patients with pituitary disorders in a dose adapted to their individual glucose tolerance (0.12-0.17 IU/kg body weight for porcine and 0.15-0.18 IU/kg body weight for human insulin). The blood glucose and potassium lowering effect, the feedback regulation of endogenous insulin release, and the liberation of the counterregulatory hormones glucagon, cortisol, adrenocorticotropic hormone (ACTH), prolactin (hPRL), human growth hormone (hGH), and catecholamines were measured before and after injection of human or porcine insulin. The maximal effect, the area under the concentration-time curve, the percentage effect, and the increase above baseline for the two doses of insulin and the two types of insulin were compared. There were no significant differences in the calculated parameters between the two insulin types at the same doses except with prolactin. At 0.075 IU/kg human insulin induced significantly less prolactin release than porcine insulin. Comparing the two doses of the same insulin serum insulin levels, blood glucose, glucagon, norepinephrine, and prolactin were lower at the low dose of each insulin. In addition ACTH and epinephrine were also lower after human insulin at 0.075 IU/kg. The subjective signs of hypoglycemia were less pronounced after human insulin. It is concluded that the biological effects of human insulin are comparable to porcine insulin although prolactin release is significantly reduced after human insulin. If this difference is an indication of different receptor sensitivities for human and porcine insulin in the central nervous system and if the diminished signs of hypoglycemia are a consequence of this, then further studies are required.
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PMID:Counterregulatory hormone release after human and porcine insulin in healthy subjects and patients with pituitary disorders. 638 71

The increase in protein adsorption by charcoal as ionic strength increases (salting-out adsorption), was used to separate the bound and free fractions of glucagon, insulin, hGH, hLH and hPRL in the radioimmunoassay. The hormones were labelled with 125I and to express the immunocomplex, gamma-globulin was labelled with 125I. The charcoal used to produce the separation was suspended in magnesium sulfate 3 M (charcoal-SO4Mg). The optimum amount of charcoal and the final concentration of magnesium sulfate determined for each hormone were: glucagon (charcoal 5 mg/tube, 0.125 M); insulin (charcoal 5 mg/tube, 0.131 M); hGH (charcoal 40 mg/tube, 0. 447 M); hLH (charcoal 40 mg/tube, 0.447 M) and hPRL (charcoal 60 mg/tube, 0.321 M). The serum concentration was 1/20 for all hormones, excepting glucagon, where 1/10 was used. The stability of the immunocomplex was studied and it was shown that, under suitable conditions, increased ionic strength does not cause the dissociation of the bound fraction.
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PMID:Increase of ionic strength for charcoal separation of B/F fractions in radioimmunoassays. 676 10