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kisspeptin-13 on insulin, glucagon, and somatostatin secretion. The study was performed in the isolated perfused rat pancreas. Animals, materials, and methods Animals Male Wistar rats (200–225 g body weight) from our inbred colony were used as
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, it is noteworthy that local high concentration of ginsenosides in intestine may interact with intestinal epithelium, where numerous endocrine cells are located. Glucagon-like peptide-1 (GLP1), secreted by enteroendocrine L-cells, is one of the most
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Introduction Glucagon-like peptide (GLP)-1 is an intestinal hormone that exerts its effects in the regulation of glucose metabolism, the stimulation of pancreatic insulin secretion, proinsulin gene expression, and the proliferation and anti
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. 2010 ). Glucagon-like peptide-1 (GLP-1) is an incretin hormone secreted by gastrointestinal L cells in response to oral nutrient ingestion ( Wan et al . 2017 ) and is an ideal therapy for obesity and T2DM ( Rajeev & Wilding 2016 ). However, native
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SUMMARY
A solid phase radioimmunoassay for glucagon was specially modified in order to overcome the problems involved in the measurement of glucagon release from incubated pieces of pancreas. The modified immunoassay procedure was used to study glucagon release from pieces of pancreas taken from newborn rats aged from 1 to 20 days. The glucagon content of rat pancreas was also measured during this period.
It was found that glucagon release from rat pancreas was stimulated by arginine and inhibited by octanoic acid at 1 and 2 days of age. However, glucagon release at 3 days of age was low, and between 3 and 7 days of age glucagon release could not be inhibited by octanoic acid or stimulated by arginine. At 10 and 20 days of age, the stimulatory action of arginine and the inhibitory action of octanoic acid were again noted. Glucagon release, measured at several ages, was not significantly affected by changes in glucose concentration. The glucagon content of the rat pancreas rose to a maximum at 5 days of age and then decreased gradually over a period of 90 days.
It is suggested that the low rate of glucagon release between 3 and 7 days of age may be a result of the high levels of blood fatty acids and ketone bodies found in the rat during this period.
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SUMMARY
The effect of glucagon on bone was studied in rats. Urinary hydroxyproline excretion and incorporation of [3H]proline into bone hydroxyproline were used as indices of bone collagen breakdown and formation respectively. Parathyroid extract (15 USP units/rat/h, i.v.), infused into thyroparathyroidectomized animals, increased urinary hydroxyproline excretion. This increase was nullified by simultaneous administration of glucagon (50 μg/rat/h, i.v.). Rats treated with glucagon for 12 days (30 μg/100 g/day, s.c.) excreted slightly less hydroxyproline in their urine than controls. In both intact and thyroparathyroidectomized rats, glucagon (10 μg/100 g/h, s.c.) decreased incorporation of [3H]proline into bone. Similar results were obtained in nephrectomized rats, evidence that changes produced by glucagon were not solely due to alterations in proline pool size caused by increased renal excretion. From these data it is concluded that: (1) glucagon can inhibit bone resorption (the effect being slight in normal rats, but easily demonstrable in parathyroid hormone-treated thyroparathyroidectomized rats), (2) release of endogenous calcitonin is not required to produce this effect, (3) parathyroid hormone and glucagon may act on the same target cell in bone, (4) inhibition of skeletal resorption may contribute to glucagon-induced hypocalcaemia, and (5) the hormone possibly decreases bone formation. Since pharmacological doses of glucagon were used in our studies, the relationship of the observations made to the physiological role of glucagon is unknown.
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Abstract
It has been shown that peripheral glucagon secreting cells (A-cells) are lost during most of the isolation procedures employed for pig islets. Loss of A-cells decreases intra-islet glucagon levels and cAMP levels in B-cells and might reduce glucose-induced insulin release. This study was designed to test this hypothesis, by evaluating the effects of culture of porcine islets with exogenous glucagon on insulin secretion and on insulin and cAMP content in islets. Islets were isolated from adult 2-year old Large White pigs using an automated method. The number of A-cells was calculated by immunostaining for glucagon in islets before and after isolation and a significant decrease in A-cells was observed. After an overnight culture, islets were cultured for 48 h in a standard medium (CMRL 1066, 10% foetal calf serum, 1% antibiotics, 1% glutamine) alone or in the presence of glucagon at two different concentrations (1·0 and 10·0 μm); exposure to glucagon was either continuous or alternated with periods of incubation in CMRL 1066 alone. After the 48-h culture in standard medium, the islet glucagon response to arginine was almost negligible and significantly lower than that observed in human islets. After culture, islet insulin response to glucose, and islet insulin and cAMP content were evaluated; continuous exposure to glucagon did not produce any significant effect on either insulin secretion or insulin and cAMP content; in contrast, discontinuous exposure to glucagon induced a significant improvement in insulin release, proportional to glucagon concentrations (integrated insulin release: −13·8 ±20·12 pg/islet/20 min in control islets, 111·0±50·73 and 144·7± 47·54 pg/islet/20 min in islets exposed to 1·0 and 10·0 μg glucagon respectively; n=10, P=0·01). Intracellular insulin and cAMP content of islets cultured in different culture media were not different. In conclusion, discontinuous exposure of isolated pig islets to exogenous glucagon induced a significant increase in glucose-induced insulin release which was not associated with an increase in cAMP content. The fact that even in the presence of glucagon the secretory activity of pig islets was lower than the reported activity of human or rat islets suggests that glucagon is only one of the factors involved in the poor insulin responsiveness of pig islets.
Journal of Endocrinology (1995) 147, 87–93
Australian Centre for Blood Diseases, Eastern Clinical Research Unit, Novo Nordisk A/S, Department of Diabetes and Endocrinology, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia
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Australian Centre for Blood Diseases, Eastern Clinical Research Unit, Novo Nordisk A/S, Department of Diabetes and Endocrinology, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia
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Australian Centre for Blood Diseases, Eastern Clinical Research Unit, Novo Nordisk A/S, Department of Diabetes and Endocrinology, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia
Australian Centre for Blood Diseases, Eastern Clinical Research Unit, Novo Nordisk A/S, Department of Diabetes and Endocrinology, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia
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protected from the development of biochemical abnormalities associated with endothelial cell dysfunction and development of atherosclerosis ( Eitzman et al . 2000 , Mao et al . 2004 ). Liraglutide, an acylated glucagon-like peptide-1 (GLP-1) analogue, has
Eastern Clinical Research Unit, Department of Diabetes and Endocrinology, Biotechnology Division, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia
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Eastern Clinical Research Unit, Department of Diabetes and Endocrinology, Biotechnology Division, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia
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Eastern Clinical Research Unit, Department of Diabetes and Endocrinology, Biotechnology Division, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia
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Eastern Clinical Research Unit, Department of Diabetes and Endocrinology, Biotechnology Division, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia
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Introduction Glucagon-like peptide-1 (GLP-1), an incretin first identified in 1984, has been proposed as a potential candidate target for therapy in the treatment of type 2 diabetes ( Nauck et al . 1993 , Edwards 2005 ). GLP-1, the product of the
Unit of Animal Biology, Université catholique de Louvain, Brussels, Belgium
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Unit of Animal Biology, Université catholique de Louvain, Brussels, Belgium
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( Reimer & McBurney 1996 , Cani et al. 2004 ). In the intestine, the post-translational modification of the proglucagon gene by prohormone convertase 1 (PC1) leads to the production of glucagon-like peptide-1(7–36) amide (GLP-1(7–36) amide) which, among
