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Journal articles on the topic 'Glucagon-like peptide 1'

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Published: 4 June 2021

Last updated: 14 March 2023

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1

Baggio, Laurie L., and Daniel J. Drucker. "Glucagon-like peptide-1 and glucagon-like peptide-2." Best Practice & Research Clinical Endocrinology & Metabolism 18, no. 4 (December 2004): 531–54. http://dx.doi.org/10.1016/j.beem.2004.08.001.

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2

Kim, Sung-Gun, and Jong-Tae Park. "Recombinant production of human glucagon-like peptide-1 mutant." Korean Journal of Agricultural Science 41, no. 3 (September 30, 2014): 237–43. http://dx.doi.org/10.7744/cnujas.2014.41.3.237.

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3

&NA;. "Glucagon-like peptide-1." Inpharma Weekly &NA;, no. 841 (June 1992): 16. http://dx.doi.org/10.2165/00128413-199208410-00022.

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4

Giblett, Joel P., Sophie J. Clarke, David P. Dutka, and Stephen P. Hoole. "Glucagon-Like Peptide-1." JACC: Basic to Translational Science 1, no. 4 (June 2016): 267–76. http://dx.doi.org/10.1016/j.jacbts.2016.03.011.

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5

Doyle, M. E. "Glucagon-Like Peptide-1." Recent Progress in Hormone Research 56, no. 1 (January 1, 2001): 377–400. http://dx.doi.org/10.1210/rp.56.1.377.

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6

Rowzee, Anne M., Niamh X. Cawley, John A. Chiorini, and Giovanni Di Pasquale. "Glucagon-Like Peptide-1 Gene Therapy." Experimental Diabetes Research 2011 (2011): 1–5. http://dx.doi.org/10.1155/2011/601047.

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Glucagon-like peptide 1 (GLP-1) is a small peptide component of the prohormone, proglucagon, that is produced in the gut. Exendin-4, a GLP-1 receptor agonist originally isolated from the saliva ofH. suspectumor Gila monster, is a peptide that shares sequence and functional homology with GLP-1. Both peptides have been demonstrated to stimulate insulin secretion, inhibit glucagon secretion, promote satiety and slow gastric emptying. As such, GLP-1 and Exendin-4 have become attractive pharmaceutical targets as an adjunctive therapy for individuals with type II diabetes mellitus, with several products currently available clinically. Herein we summarize the cell biology leading to GLP-1 production and secretion from intestinal L-cells and the endocrine functions of this peptide and Exendin-4 in humans. Additionally, gene therapeutic applications of GLP-1 and Exendin-4 are discussed with a focus on recent work using the salivary gland as a gene therapy target organ for the treatment of diabetes mellitus.

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7

Lutz, Thomas A., and Elena Osto. "Glucagon-like peptide-1, glucagon-like peptide-2, and lipid metabolism." Current Opinion in Lipidology 27, no. 3 (June 2016): 257–63. http://dx.doi.org/10.1097/mol.0000000000000293.

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8

Wang, XingChun, Huan Liu, Jiaqi Chen, Yan Li, and Shen Qu. "Multiple Factors Related to the Secretion of Glucagon-Like Peptide-1." International Journal of Endocrinology 2015 (2015): 1–11. http://dx.doi.org/10.1155/2015/651757.

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The glucagon-like peptide-1 is secreted by intestinal L cells in response to nutrient ingestion. It regulates the secretion and sensitivity of insulin while suppressing glucagon secretion and decreasing postprandial glucose levels. It also improves beta-cell proliferation and prevents beta-cell apoptosis induced by cytotoxic agents. Additionally, glucagon-like peptide-1 delays gastric emptying and suppresses appetite. The impaired secretion of glucagon-like peptide-1 has negative influence on diabetes, hyperlipidemia, and insulin resistance related diseases. Thus, glucagon-like peptide-1-based therapies (glucagon-like peptide-1 receptor agonists and dipeptidyl peptidase-4 inhibitors) are now well accepted in the management of type 2 diabetes. The levels of glucagon-like peptide-1 are influenced by multiple factors including a variety of nutrients. The component of a meal acts as potent stimulants of glucagon-like peptide-1 secretion. The levels of its secretion change with the intake of different nutrients. Some drugs also have influence on GLP-1 secretion. Bariatric surgery may improve metabolism through the action on GLP-1 levels. In recent years, there has been a great interest in developing effective methods to regulate glucagon-like peptide-1 secretion. This review summarizes the literature on glucagon-like peptide-1 and related factors affecting its levels.

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9

Padwal, R. "Glucagon-like peptide-1 agonists." BMJ 344, jan10 2 (January 10, 2012): d7282. http://dx.doi.org/10.1136/bmj.d7282.

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10

Müller, T. D., B. Finan, S. R. Bloom, D. D'Alessio, D. J. Drucker, P. R. Flatt, A. Fritsche, et al. "Glucagon-like peptide 1 (GLP-1)." Molecular Metabolism 30 (December 2019): 72–130. http://dx.doi.org/10.1016/j.molmet.2019.09.010.

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11

De Block, Christophe E. M., Eveline Dirinck, Ann Verhaegen, and Luc F. Van Gaal. "Efficacy and safety of high‐dose glucagon‐like peptide‐1, glucagon‐like peptide‐1/glucose‐dependent insulinotropic peptide, and glucagon‐like peptide‐1/glucagon receptor agonists in type 2 diabetes." Diabetes, Obesity and Metabolism 24, no. 5 (January 21, 2022): 788–805. http://dx.doi.org/10.1111/dom.14640.

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12

Brubaker, Patricia L., and Younes Anini. "Direct and indirect mechanisms regulating secretion of glucagon-like peptide-1 and glucagon-like peptide-2." Canadian Journal of Physiology and Pharmacology 81, no. 11 (November 1, 2003): 1005–12. http://dx.doi.org/10.1139/y03-107.

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The proglucagon-derived peptide family consists of three highly related peptides, glucagon and the glucagon-like peptides GLP-1 and GLP-2. Although the biological activity of glucagon as a counter-regulatory hormone has been known for almost a century, studies conducted over the past decade have now also elucidated important roles for GLP-1 as an antidiabetic hormone, and for GLP-2 as a stimulator of intestinal growth. In contrast to pancreatic glucagon, the GLPs are synthesized in the intestinal epithelial L cells, where they are subject to the influences of luminal nutrients, as well as to a variety of neuroendocrine inputs. In this review, we will focus on the complex integrative mechanisms that regulate the secretion of these peptides from L cells, including both direct and indirect regulation by ingested nutrients.Key words: GLP-1, GLP-2, intestine, secretion, nutrients, neural.

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13

Eom, Young Sil, and Byung-Joon Kim. "Glucagon-Like Peptide-1 (GLP-1) Agonist." Korean Journal of Medicine 87, no. 1 (2014): 9. http://dx.doi.org/10.3904/kjm.2014.87.1.9.

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14

Gribble, Fiona M., and Frank Reimann. "Metabolic Messengers: glucagon-like peptide 1." Nature Metabolism 3, no. 2 (January 11, 2021): 142–48. http://dx.doi.org/10.1038/s42255-020-00327-x.

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15

Mita, Tomoya, and Hirotaka Watada. "Glucagon Like Peptide-1 and Atherosclerosis." Cardiovascular & Hematological Agents in Medicinal Chemistry 10, no. 4 (October 1, 2012): 309–18. http://dx.doi.org/10.2174/187152512803530388.

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16

Monami, Matteo. "Glucagon-Like Peptide-1 and Diabetes." Experimental Diabetes Research 2011 (2011): 1. http://dx.doi.org/10.1155/2011/901954.

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17

van Dijk, G., T. E. Thiele, R. J. Seeley, S. C. Woods, and I. L. Bernstein. "Glucagon-like peptide-1 and satiety." Nature 385, no. 6613 (January 1997): 214. http://dx.doi.org/10.1038/385214a0.

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18

Bloom, S. R. "Glucagon-like peptide-1 and satiety." Nature 385, no. 6613 (January 1997): 214. http://dx.doi.org/10.1038/385214b0.

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19

Zhang, Yifan, and Wengen Chen. "Radiolabeled glucagon-like peptide-1 analogues." Nuclear Medicine Communications 33, no. 3 (March 2012): 223–27. http://dx.doi.org/10.1097/mnm.0b013e32834e7f47.

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20

Dailey, Megan J., and Timothy H. Moran. "Glucagon-like peptide 1 and appetite." Trends in Endocrinology & Metabolism 24, no. 2 (February 2013): 85–91. http://dx.doi.org/10.1016/j.tem.2012.11.008.

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21

Fava, Genevieve E., Emily W. Dong, and Hongju Wu. "Intra-islet glucagon-like peptide 1." Journal of Diabetes and its Complications 30, no. 8 (November 2016): 1651–58. http://dx.doi.org/10.1016/j.jdiacomp.2016.05.016.

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22

Ritzel, R. A. "„Glucagon-like peptide-1“-basierende Therapie." Der Diabetologe 7, no. 5 (July 2011): 321–28. http://dx.doi.org/10.1007/s11428-011-0698-8.

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23

Gallwitz, B. "Rezeptoragonisten des „glucagon-like peptide 1”." Der Diabetologe 13, no. 7 (October 5, 2017): 487–97. http://dx.doi.org/10.1007/s11428-017-0266-y.

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24

Spasov, A. A., and N. I. Chepljaeva. "Potential of pharmacological modulation of level and activity incretins on diabetes mellitus type 2." Biomeditsinskaya Khimiya 61, no. 4 (2015): 488–96. http://dx.doi.org/10.18097/pbmc20156104488.

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This review summarizes data on the main approaches used for the search of biologically active compounds modulating the level and physiological activity of incretins. Currently two groups of drugs are used in clinical practice: they either replenish the deficit of incretins (glucagon-like peptide-1 receptor agonists) or inhibit the degradation processes (dipeptidyl peptidase 4 inhibitors). In addition, new groups of substances are actively searched. These include non-peptide agonists of glucagon-like peptide-1 receptors, agonists/antagonists of glucose-dependent insulinotropic peptide, the hybrid polypeptides based on glucagon-like peptide-1 and glucagon

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25

St. Onge, Erin L., Shannon A. Miller, and James R. Taylor. "Novel Approaches to the Treatment of Type 2 Diabetes." Journal of Pharmacy Practice 22, no. 3 (January 6, 2009): 320–32. http://dx.doi.org/10.1177/0897190008326578.

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The emergence of the glucoregulatory hormone, glucagon-like peptide-1, has expanded our understanding of glucose homeostasis. The glucoregulatory actions of glucagon-like peptide-1 include enhancement of glucose-dependent insulin secretion, suppression of inappropriately elevated glucagon secretion, slowing of gastric emptying, and reduction of food intake. Two approaches have been developed to potentiate the effects of glucagon-like peptide-1 in those with type 2 diabetes. The glucagon-like peptide-1 analogs, such as exenatide, and dipeptidyl peptidase-IV inhibitors, such as sitagliptin, are currently available whereas others are in the final stages of development. These agents effectively reduce hemoglobin A1c while providing the other benefits associated with increased glucagon-like peptide-1. They also offer the potential to preserve the β-cell function. The effects on cardiovascular disease, if any, are unknown. Based on the current evidence, these agents represent viable second-and third-line options in the management of type 2 diabetes.

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26

Holst, Jens Juul. "The Physiology of Glucagon-like Peptide 1." Physiological Reviews 87, no. 4 (October 2007): 1409–39. http://dx.doi.org/10.1152/physrev.00034.2006.

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Glucagon-like peptide 1 (GLP-1) is a 30-amino acid peptide hormone produced in the intestinal epithelial endocrine L-cells by differential processing of proglucagon, the gene which is expressed in these cells. The current knowledge regarding regulation of proglucagon gene expression in the gut and in the brain and mechanisms responsible for the posttranslational processing are reviewed. GLP-1 is released in response to meal intake, and the stimuli and molecular mechanisms involved are discussed. GLP-1 is extremely rapidly metabolized and inactivated by the enzyme dipeptidyl peptidase IV even before the hormone has left the gut, raising the possibility that the actions of GLP-1 are transmitted via sensory neurons in the intestine and the liver expressing the GLP-1 receptor. Because of this, it is important to distinguish between measurements of the intact hormone (responsible for endocrine actions) or the sum of the intact hormone and its metabolites, reflecting the total L-cell secretion and therefore also the possible neural actions. The main actions of GLP-1 are to stimulate insulin secretion (i.e., to act as an incretin hormone) and to inhibit glucagon secretion, thereby contributing to limit postprandial glucose excursions. It also inhibits gastrointestinal motility and secretion and thus acts as an enterogastrone and part of the “ileal brake” mechanism. GLP-1 also appears to be a physiological regulator of appetite and food intake. Because of these actions, GLP-1 or GLP-1 receptor agonists are currently being evaluated for the therapy of type 2 diabetes. Decreased secretion of GLP-1 may contribute to the development of obesity, and exaggerated secretion may be responsible for postprandial reactive hypoglycemia.

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27

Göke, R., T. Cole, and J. M. Conlon. "Characterization of the receptor for glucagon-like peptide-1(7–36)amide on plasma membranes from rat insulinoma-derived cells by covalent cross-linking." Journal of Molecular Endocrinology 2, no. 2 (March 1989): 93–98. http://dx.doi.org/10.1677/jme.0.0020093.

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ABSTRACT 125I-Labelled glucagon-like peptide-1(7–36)amide was cross-linked to a specific binding protein in plasma membranes prepared from RINm5F rat insulinoma-derived cells using disuccinimidyl suberate. Consistent with the presence of a single class of binding site on the surface of intact cells, only a single radiolabelled band at Mr 63 000 was identified by SDS-PAGE after solubilization of the ligand—binding protein complex. The band was not observed when 10 nm glucagon-like peptide-1(7–36)amide was included in the binding assay, but 1 μm concentrations of glucagon-like peptide1(1–36)amide, glucagon-like peptide-2 and glucagon did not decrease the intensity of labelling. No change in the mobility of the band was observed under reducing conditions, suggesting that the binding protein in the receptor is not attached to other subunits via disulphide bonds. In control incubations using plasma membranes from pig intestinal epithelial cells, which do not contain specific binding sites for glucagon-like peptide-1(7–36)amide, no cross-linked ligand-binding protein complex was observed.

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28

Gutzwiller, Jean-Pierre, Lukas Degen, Ludwig Heuss, and Christoph Beglinger. "Glucagon-like peptide 1 (GLP-1) and eating." Physiology & Behavior 82, no. 1 (August 2004): 17–19. http://dx.doi.org/10.1016/j.physbeh.2004.04.019.

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29

Wewer Albrechtsen, Nicolai J., Monika J. Bak, Bolette Hartmann, Louise Wulff Christensen, Rune E. Kuhre, Carolyn F. Deacon, and Jens J. Holst. "Stability of glucagon-like peptide 1 and glucagon in human plasma." Endocrine Connections 4, no. 1 (March 2015): 50–57. http://dx.doi.org/10.1530/ec-14-0126.

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To investigate the stability of glucagon-like peptide 1 (GLP-1) and glucagon in plasma under short- and long-term storage conditions. Pooled human plasma (n=20), to which a dipeptidyl peptidase 4 (DPP4) inhibitor and aprotinin were added, was spiked with synthetic GLP-1 (intact, 7–36NH2 as well as the primary metabolite, GLP-1 9–36NH2) or glucagon. Peptide recoveries were measured in samples kept for 1 and 3 h at room temperature or on ice, treated with various enzyme inhibitors, after up to three thawing–refreezing cycles, and after storage at −20 and −80 °C for up to 1 year. Recoveries were unaffected by freezing cycles or if plasma was stored on ice for up to 3 h, but were impaired when samples stood at RT for more than 1 h. Recovery of intact GLP-1 increased by addition of a DPP4 inhibitor (no ice), but was not further improved by neutral endopeptidase 24.11 inhibitor or an inhibitor cocktail. GLP-1, but not glucagon, was stable for at least 1 year. Surprisingly, the recovery of glucagon was reduced by almost 50% by freezing compared with immediate analysis, regardless of storage time. Plasma handling procedures can significantly influence results of subsequent hormone analysis. Our data support addition of DPP4 inhibitor for GLP-1 measurement as well as cooling on ice of both GLP-1 and glucagon. Freeze–thaw cycles did not significantly affect stability of GLP-1 or glucagon. Long-term storage may affect glucagon levels regardless of storage temperature and results should be interpreted with caution.

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30

Ørskov, C., H. Kofod, L. Rabenhøj, A. Wettergren, and J. J. Holst. "Structure of human GLP-1(glucagon-like peptide-1) containing peptides." Regulatory Peptides 40, no. 2 (July 1992): 223. http://dx.doi.org/10.1016/0167-0115(92)90363-y.

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31

Arora, Pankaj. "Glucagon-Like Peptide-1 Receptor–Atrial Natriuretic Peptide Axis." Circulation: Cardiovascular Genetics 6, no. 5 (October 2013): 523. http://dx.doi.org/10.1161/circgenetics.113.000361.

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32

Haseeb, Abdul. "Multidimensional effects of glucagon-like peptide-1." El Mednifico Journal 1, no. 1 (January 29, 2013): 20. http://dx.doi.org/10.18035/emj.v1i1.8.

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33

Gupta, Vishal. "Glucagon-like peptide-1 analogues: An overview." Indian Journal of Endocrinology and Metabolism 17, no. 3 (2013): 413. http://dx.doi.org/10.4103/2230-8210.111625.

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34

Kheder, Murad H., Simon R. Bailey, Kevin J. Dudley, Martin N. Sillence, and Melody A. de Laat. "Equine glucagon-like peptide-1 receptor physiology." PeerJ 6 (January 29, 2018): e4316. http://dx.doi.org/10.7717/peerj.4316.

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Background Equine metabolic syndrome (EMS) is associated with insulin dysregulation, which often manifests as post-prandial hyperinsulinemia. Circulating concentrations of the incretin hormone, glucagon-like peptide-1 (GLP-1) correlate with an increased insulin response to carbohydrate intake in animals with EMS. However, little is known about the equine GLP-1 receptor (eGLP-1R), or whether GLP-1 concentrations can be manipulated. The objectives were to determine (1) the tissue localisation of the eGLP-1R, (2) the GLP-1 secretory capacity of equine intestine in response to glucose and (3) whether GLP-1 stimulated insulin secretion from isolated pancreatic islets can be attenuated. Methods Archived and abattoir-sourced tissues from healthy horses were used. Reverse transcriptase PCR was used to determine the tissue distribution of the eGLP-1R gene, with immunohistochemical confirmation of its pancreatic location. The GLP-1 secretion from intestinal explants in response to 4 and 12 mM glucose was quantified in vitro. Pancreatic islets were freshly isolated to assess the insulin secretory response to GLP-1 agonism and antagonism in vitro, using concentration-response experiments. Results The eGLP-1R gene is widely distributed in horses (pancreas, heart, liver, kidney, duodenum, digital lamellae, tongue and gluteal skeletal muscle). Within the pancreas the eGLP-1R was immunolocalised to the pancreatic islets. Insulin secretion from pancreatic islets was concentration-dependent with human GLP-1, but not the synthetic analogue exendin-4. The GLP-1R antagonist exendin 9-39 (1 nM) reduced (P = 0.08) insulin secretion by 27%. Discussion The distribution of the eGLP-1R across a range of tissues indicates that it may have functions beyond insulin release. The ability to reduce insulin secretion, and therefore hyperinsulinemia, through eGLP-1R antagonism is a promising and novel approach to managing equine insulin dysregulation.

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35

&NA;. "Glucagon-like peptide-1 stops gastric emptying." Inpharma Weekly &NA;, no. 1024 (February 1996): 10. http://dx.doi.org/10.2165/00128413-199610240-00019.

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36

Papazafiropoulou, A., S. I. Pappas, D. Papadogiannis, and N. Tentolouris. "Cardiovascular Effects of Glucagon-Like Peptide 1." Mini-Reviews in Medicinal Chemistry 11, no. 1 (January 1, 2011): 97–105. http://dx.doi.org/10.2174/138955711793564033.

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37

Monami, Matteo, Giovanni Di Pasquale, Anna Rowzee, Carlo Maria Rotella, and Edoardo Mannucci. "Glucagon-Like Peptide-1 and Diabetes 2012." Experimental Diabetes Research 2012 (2012): 1. http://dx.doi.org/10.1155/2012/768760.

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38

Lund, P. Kay. "The discovery of glucagon-like peptide 1." Regulatory Peptides 128, no. 2 (June 2005): 93–96. http://dx.doi.org/10.1016/j.regpep.2004.09.001.

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39

Murr, Michel M. "Is Glucagon-like peptide-1 for real?" Surgery for Obesity and Related Diseases 10, no. 5 (September 2014): 786. http://dx.doi.org/10.1016/j.soard.2014.02.006.

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40

Treiman, Marek, Mikkel Elvekjær, Thomas Engstrøm, and Jan Skov Jensen. "Glucagon-Like Peptide 1—A Cardiologic Dimension." Trends in Cardiovascular Medicine 20, no. 1 (January 2010): 8–12. http://dx.doi.org/10.1016/j.tcm.2010.02.012.

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41

Kauth, Th, and J. Metz. "Immunohistochemical localization of glucagon-like peptide 1." Histochemistry 86, no. 5 (1987): 509–15. http://dx.doi.org/10.1007/bf00500625.

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42

Sörhede Winzell, M., and B. Ahrén. "Glucagon-like Peptide-1 and Islet Lipolysis." Hormone and Metabolic Research 36, no. 11/12 (November 2004): 795–803. http://dx.doi.org/10.1055/s-2004-826166.

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43

Jeong, In-Kyung. "Extrapancreatic Effect of Glucagon like Peptide-1." Korean Journal of Medicine 89, no. 4 (October 1, 2015): 404–12. http://dx.doi.org/10.3904/kjm.2015.89.4.404.

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44

Burcelin, Rémy, Patrice D. Cani, and Claude Knauf. "Glucagon-Like Peptide-1 and Energy Homeostasis." Journal of Nutrition 137, no. 11 (November 1, 2007): 2534S—2538S. http://dx.doi.org/10.1093/jn/137.11.2534s.

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45

HOLST, J. J. "Glucagon, glucagon-like peptide-1 and their receptors: an introduction." Acta Physiologica Scandinavica 157, no. 3 (July 1996): 309–15. http://dx.doi.org/10.1046/j.1365-201x.1996.32261000.x.

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46

Shima, K., C. Ohboshi, M. Sato, and M. Hirota. "Effect of Glucagon on Secretion of Glucagon-Like Peptide 1." Hormone and Metabolic Research 20, no. 02 (February 1988): 123–24. http://dx.doi.org/10.1055/s-2007-1010770.

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47

Lee, Seungah, and Dong Yun Lee. "Glucagon-like peptide-1 and glucagon-like peptide-1 receptor agonists in the treatment of type 2 diabetes." Annals of Pediatric Endocrinology & Metabolism 22, no. 1 (2017): 15. http://dx.doi.org/10.6065/apem.2017.22.1.15.

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48

Hjorth, S. A., K. Adelhorst, B. B. Pedersen, O. Kirk, and T. W. Schwartz. "Glucagon and glucagon-like peptide 1: selective receptor recognition via distinct peptide epitopes." Journal of Biological Chemistry 269, no. 48 (1994): 30121–24. http://dx.doi.org/10.1016/s0021-9258(18)43785-4.

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49

Volkova, Anna R., Galina V. Semikova, Valentina S. Mozgunova, Margarita N. Maltseva, Vladimir L. Bondarenko, and Nadezhda S. Katysheva. "Glucagon-like peptid-1 in obese and diabetic patients after bariatric interventions." Bulletin of the Russian Military Medical Academy 23, no. 1 (May 12, 2021): 89–94. http://dx.doi.org/10.17816/brmma57488.

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The relationship between the level of glucagon-like peptide-1 and repeated weight gain was evaluated in 31 patients suffering from grade IIIII obesity and type 2 diabetes mellitus after bariatric interventions for 3 years. It was found that the level of stimulated glucagon-like peptide-1 significantly increased by the third day after sleeve gastroplasty and gastroschunt compared to the initial parameters (p = 0.001 for obese patients; p = 0.000 for obese patients and diabetes mellitus). In the plateau phase (body weight retention) after bariatric intervention, the level of stimulated glucagon-like peptide-1 in obese patients and patients suffering from obesity in combination with diabetes mellitus did not significantly differ from the indicators of healthy individuals. There was no association between the level of glucagon-like peptide-1 and repeated weight gain. This may be due to the limited contribution of glucagon-like peptide-1 to body weight dynamics after bariatric interventions and the predominance of patient compliance. Thus, the level of stimulated glucagon-like peptide-1 at baseline, on the third day and in the plateau phase after bariatric intervention was not associated with the value of repeated weight gain.

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50

Villanueva-Peñacarrillo, M. L., E. Delgado, M. A. Trapote, A. Alcántara, F. Clemente, M. A. Luque, A. Perea, and I. Valverde. "Glucagon-like peptide-1 binding to rat hepatic membranes." Journal of Endocrinology 146, no. 1 (July 1995): 183–89. http://dx.doi.org/10.1677/joe.0.1460183.

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Abstract We have found [125I]glucagon-like peptide (GLP)-1(7–36)amide specific binding activity in rat liver and isolated hepatocyte plasma membranes, with an Mr of approximately 63 000, estimated by cross-linking and SDS-PAGE. The specific binding was time- and membrane protein concentration-dependent, and equally displaced by unlabelled GLP-1(7–36)amide and by GLP-1(1–36)amide, achieving its ID50 at 3×10−9 m of the peptides. GLP-1(7–36)amide did not modify the basal or the glucagon (10−8 m)-stimulated adenylate cyclase in the hepatocyte plasma membranes. These data, together with our previous findings of a potent glycogenic effect of GLP-1(7–36)amide in isolated rat hepatocytes, led us to postulate that the insulin-like effects of this peptide on glucose liver metabolism could be mediated by a type of receptor probably different from that described for GLP-1 in pancreatic B-cells or, alternatively, by the same receptor which, in this tissue as well as in muscle, uses a different transduction system. Journal of Endocrinology (1995) 146, 183–189

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