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The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark
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The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark
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The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark
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The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark
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The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark
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The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark
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The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark
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The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark
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Introduction The intestinal incretin hormones, glucagon-like peptide-1 (7–36) amide (GLP-1) and glucose-dependent insulinotropic peptide (GIP) are released in response to fat and carbohydrate ingestion. Both peptides act to augment
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of Nutrition 134 3264 – 3269 . Hirasawa A Tsumaya K Awaji T Katsuma S Adachi T Yamada M Sugimoto Y Miyazaki S Tsujimoto G 2005 Free fatty acids regulate gut incretin glucagon-like peptide-1 secretion through GPR120 . Nature
Department of Pharmacology, University of Cambridge, Cambridge, UK
Department of Pharmacology, University of Chicago, Chicago, Illinois, USA
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Department of Pharmacology, University of Cambridge, Cambridge, UK
Department of Pharmacology, University of Chicago, Chicago, Illinois, USA
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Department of Pharmacology, University of Cambridge, Cambridge, UK
Department of Pharmacology, University of Chicago, Chicago, Illinois, USA
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Department of Pharmacology, University of Cambridge, Cambridge, UK
Department of Pharmacology, University of Chicago, Chicago, Illinois, USA
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Department of Pharmacology, University of Cambridge, Cambridge, UK
Department of Pharmacology, University of Chicago, Chicago, Illinois, USA
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Department of Pharmacology, University of Cambridge, Cambridge, UK
Department of Pharmacology, University of Chicago, Chicago, Illinois, USA
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Department of Pharmacology, University of Cambridge, Cambridge, UK
Department of Pharmacology, University of Chicago, Chicago, Illinois, USA
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Amersham Biosciences (Arlington Heights, IL, USA), containing 75% l -[ 35 S]methionine was used for islet protein synthesis radiolabeling. Uridine 5′-[α- 32 P]triphosphate (3000 Ci/mmol) was purchased from Amersham Biosciences. Glucagon-like peptide-1 (GLP
Department of Biochemistry, Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland
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Department of Biochemistry, Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland
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Department of Biochemistry, Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland
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Department of Biochemistry, Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland
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Department of Biochemistry, Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland
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, carbachol; CCK-8, cholecystokinin-8; Forsk, forskolin; GLP-1, glucagon-like peptide 1 (7-36) amide; GIP, gastric inhibitory polypeptide; HC, homocysteine; PMA, phorbol 12-myristate 13-acetate. Test Agent None 5.6 1.29 ± 0.04 0.81 ± 0.05 ΔΔΔ 0.81 ± 0.09 ΔΔΔ 0
Carnegie School of Sport, Leeds Beckett University, Headingley Campus, Leeds, UK
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–tyrosine (PYY) and glucagon-like peptide 1 (GLP-1) have been observed with continuous, high-intensity aerobic bouts of exercise lasting as little as 30 min ( Ueda et al . 2009 a ), and with intermittent exercise bouts yielding energy expenditure values of as
Biomedical Research Group (BMRG), UCD School of Biomolecular and Biomedical Science, School of Public Health, Department of Physiology, Federal University of Rio Grande do Sul School of Physical Education, School of Biomedical Sciences, School of Biomedical Sciences, Department of Science, ITT Dublin, Tallaght, Dublin 24, Ireland
Biomedical Research Group (BMRG), UCD School of Biomolecular and Biomedical Science, School of Public Health, Department of Physiology, Federal University of Rio Grande do Sul School of Physical Education, School of Biomedical Sciences, School of Biomedical Sciences, Department of Science, ITT Dublin, Tallaght, Dublin 24, Ireland
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Biomedical Research Group (BMRG), UCD School of Biomolecular and Biomedical Science, School of Public Health, Department of Physiology, Federal University of Rio Grande do Sul School of Physical Education, School of Biomedical Sciences, School of Biomedical Sciences, Department of Science, ITT Dublin, Tallaght, Dublin 24, Ireland
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Biomedical Research Group (BMRG), UCD School of Biomolecular and Biomedical Science, School of Public Health, Department of Physiology, Federal University of Rio Grande do Sul School of Physical Education, School of Biomedical Sciences, School of Biomedical Sciences, Department of Science, ITT Dublin, Tallaght, Dublin 24, Ireland
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promotes insulin secretion in pancreatic islets via a mechanism that is dependent on the release of glucagon-like peptide-1 (GLP1; Ellingsgaard et al . 2011 ). Ellingsgaard et al . (2011) have shown that administration of IL6 or elevated IL6
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glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP; Vilsboll & Holst 2004 , Drucker 2006 ). The effect is, however, also partially achieved by autonomic nerves activated by oral glucose. Thus, cholinergic nerves
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Abstract
The effects of intravenous somatostatin-28 (S28) infusion on glucose-stimulated and glucagon-like peptide-1(7–36)amide (GLP-1)-augmented insulin secretion were studied in sheep. S28 was infused via a jugular catheter for 15 min at a rate of 1·1 pmol/kg/min either alone or together with GLP-1 and/or glucose. S28 infusion did not significantly lower circulating basal insulin concentrations in fed sheep. Glucose-stimulated insulin secretion was significantly inhibited by S28 infusion, serum concentrations decreasing from about 200 to 150 pmol/l. GLP-1 significantly augmented glucose-stimulated insulin secretion, serum concentrations increasing from about 230 to 280 pmol/l. S28 completely counteracted this effect of GLP-1. S28 infusion also significantly decreased the circulating concentrations of glucose-dependent insulinotrophic polypeptide (GIP) and GLP-1 in fed sheep (from about 110 to 45 pmol/l for GIP and from about 25 to 15 pmol/l for GLP-1). The physiological implications of these observations are discussed with particular reference to the ruminant. It is concluded that S28 may have an important endocrine role in the control of insulin secretion and regulation of nutrient partitioning.
Journal of Endocrinology (1996) 151, 107–112
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This study was undertaken to determine whether the internal clock contributes to the hormone and metabolic responses following food, in an experiment designed to dissociate internal clock effects from other factors. Nine female subjects participated. They lived indoors for 31 days with normal time cues, including the natural light: darkness cycle. For 7 days they retired to bed from 0000 h to 0800 h. They then underwent a 26-h 'constant routine' (CR) starting at 0800 h, being seated awake in dim light with hourly 88 Kcal drinks. They then lived on an imposed 27-h day (18 h of wakefulness, 9 h allowed for sleep), for a total of 27 days. A second 26-h CR, starting at 2200 h, was completed. During each CR salivary melatonin and plasma glucose, triacylglycerol (TAG), non-essential fatty acids (NEFA), insulin, gastric inhibitory peptide (GIP) and glucagon-like peptide-1 (GLP-1) were measured hourly. Melatonin and body temperature data indicated no shift in the endogenous clock during the 27-h imposed schedule. Postprandial NEFA, GIP and GLP-1 showed no consistent effects. Glucose, TAG and insulin increased during the night in the first CR. There was a significant effect of both the endogenous clock and sleep for glucose and TAG, but not for insulin. These findings may be relevant to the known increased risk of cardiovascular disease amongst shift workers.
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Abstract
We have characterized the specific binding of glucagon in hepatocytes isolated from two teleost species, the American eel (Anguilla rostrata) and the brown bullhead (Ictalurus nebulosus). Specific glucagon binding was 9·3 and 10·7% in bullhead and eel hepatocytes respectively, after a 2-h incubation at 12 °C. Curvilinear Scatchard plots suggest the presence of two classes of binding sites with apparent dissociation constants (K d) of 1·97 nm (high affinity) and 17·3 nm (low affinity) for bullhead and 2·68 and 22·9 nm for eel cells. The number of high-affinity binding sites per cell was significantly higher in the eel (10 413) than in the bullhead (3811). The number of high-affinity insulin-binding sites was approximately two times higher than that for glucagon in bullheads and the opposite in the eel hepatocytes. In competition experiments, insulin did not displace 125I-labelled glucagon binding in the hepatocytes of either species, while glucagon-like peptide-1(7–37) (GLP-1) displaced glucagon but only at high concentrations, suggesting separate glucagon- and GLP-1-binding sites. The rate of dissociation of hepatocyte-bound 125I-labelled glucagon was similar for both species. Preincubation of hepatocytes in 100 nm glucagon decreased the number of high-affinity glucagon-binding sites by approximately 55% in both species, while the K d values remained unchanged. Glucagon bound to the cell surface is internalized by fish hepatocytes. These properties indicate that the glucagon binding to hepatocytes of these two teleost species is similar to that reported for mammalian hepatocytes.
Journal of Endocrinology (1994) 140, 217–227
