needed, to reach an HbA 1C level of 7% or less. Among the most prescribed drugs, the glucagon-like peptide-1 receptor agonists (GLP-1RAs) have recently attracted attention as Glp-1r -knockout animals, and GLP-1-supplemented animals exhibited
Guillaume Mabilleau, Marie Pereira, and Chantal Chenu
Jennifer A Crookshank, Daniel Serrano, Gen-Sheng Wang, Christopher Patrick, Baylie S Morgan, Marie-France Paré, and Fraser W Scott
proteins were used: insulin (Agilent Technologies Canada Inc., Mississauga, Canada), proinsulin (Bio-Techne, Minneapolis, USA), glucagon (MilliporeSigma), BIP (Abcam Inc.). ImageJ (National Institute of Health) was used to quantify the insulin + and
Guillaume Mabilleau, Aleksandra Mieczkowska, Nigel Irwin, Peter R Flatt, and Daniel Chappard
al . 2010 ). Glucagon-like peptide-1 (GLP1) is a gut hormone synthesized and secreted into the blood stream by intestinal endocrine L cells in response to a variety of stimuli ( Wu et al . 2010 ). Biologically active GLP1 is secreted as a 7–37 or 7
Jun-ichi Eiki, Kaori Saeki, Norihiro Nagano, Tomoharu Iino, Mari Yonemoto, Yoko Takayenoki-Iino, Satoru Ito, Teruyuki Nishimura, Yoshiyuki Sato, Makoto Bamba, Hitomi Watanabe, Kaori Sasaki, Sumika Ohyama, Akio Kanatani, Toshio Nagase, and Toshihiko Yada
Introduction Glucagon-like peptide-1 (GLP-1) is a hormone secreted from enteroendocrine L-cells, and is well recognized as an incretin that induces insulin secretion in a glucose-dependent manner ( Drucker 2006 ). The functions of GLP-1 have been
Can Liu, Mian Zhang, Meng-yue Hu, Hai-fang Guo, Jia Li, Yun-li Yu, Shi Jin, Xin-ting Wang, Li Liu, and Xiao-dong Liu
, 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
Mi-Hyun Kim, Jae-Hwan Jee, Sunyoung Park, Myung-Shik Lee, Kwang-Won Kim, and Moon-Kyu Lee
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
Li Zhao, Chunfang Zhu, Meng Lu, Chi Chen, Xiaomin Nie, Buatikamu Abudukerimu, Kun Zhang, Zhiyuan Ning, Yi Chen, Jing Cheng, Fangzhen Xia, Ningjian Wang, Michael D Jensen, and Yingli Lu
. 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
R A Silvestre, E M Egido, R Hernández, and J Marco
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
J. C. EDWARDS, K. ASPLUND, and G. LUNDQVIST
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.
D. N. KALU, CARMEL HILLYARD, and G. V. FOSTER
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.