The role of incretins in glucose homeostasis and diabetes treatment

Kim, Wook; Egan, Josephine M.

doi:10.1124/pr.108.000604

Cited by 824Diabetes Treatment and ManagementPancreatic function and diabetesDiabetes Management and Research

The role of incretins in glucose homeostasis and diabetes treatment

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Kim, Wook, Egan, Josephine M.·2008·Pharmacological Reviews

DOI 10.1124/pr.108.000604PMC PMC2696340

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Abstract

Incretins are gut hormones that are secreted from enteroendocrine cells into the blood within minutes after eating. One of their many physiological roles is to regulate the amount of insulin that is secreted after eating. In this manner, as well as others to be described in this review, their final common raison d'être is to aid in disposal of the products of digestion. There are two incretins, known as glucose-dependent insulinotropic peptide (GIP) and glucagon-like peptide-1 (GLP-1), that share many common actions in the pancreas but have distinct actions outside of the pancreas. Both incretins are rapidly deactivated by an enzyme called dipeptidyl peptidase 4 (DPP4). A lack of secretion of incretins or an increase in their clearance are not pathogenic factors in diabetes. However, in type 2 diabetes (T2DM), GIP no longer modulates glucose-dependent insulin secretion, even at supraphysiological (pharmacological) plasma levels, and therefore GIP incompetence is detrimental to beta-cell function, especially after eating. GLP-1, on the other hand, is still insulinotropic in T2DM, and this has led to the development of compounds that activate the GLP-1 receptor with a view to improving insulin secretion. Since 2005, two new classes of drugs based on incretin action have been approved for lowering blood glucose levels in T2DM: an incretin mimetic (exenatide, which is a potent long-acting agonist of the GLP-1 receptor) and an incretin enhancer (sitagliptin, which is a DPP4 inhibitor). Exenatide is injected subcutaneously twice daily and its use leads to lower blood glucose and higher insulin levels, especially in the fed state. There is glucose-dependency to its insulin secretory capacity, making it unlikely to cause low blood sugars (hypoglycemia). DPP4 inhibitors are orally active and they increase endogenous blood levels of active incretins, thus leading to prolonged incretin action. The elevated levels of GLP-1 are thought to be the mechanism underlying their blood glucose-lowering effects.

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Reversing GIP resistance while enhancing GLP-1 effects is thought to bolster the incretin effect more than GLP-1 receptor agonism alone and create synergistic effects on glucose control.
“Reversing GIP resistance while simultaneously enhancing the effects of GLP-1 is thought to bolster the previously described incretin effect even more than GLP-1 receptor agonism alone and create synergistic effects on glucose control”
From Tirzepatide: Clinical review of the twincretin injectable (2023) · cites this paper as [19]
Section V.B reports additive effects of GLP-1 and GIP on insulin secretion in β-cell lines, but only at submaximal concentrations. Section VI.A raises the possibility that stimulating both receptors might benefit people with type 2 diabetes. Neither passage establishes that reversing GIP resistance produces synergistic glucose control or improves the incretin effect more than GLP-1 receptor agonism alone; page numbers are unavailable in our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measured
In non-diabetic subjects, incretins are responsible for 50-70% of total insulin secreted after oral glucose.
“In non-diabetic subjects, Incretins are responsible for 50–70% of the total insulin secreted after oral glucose administration.[23–25]”
From Postprandial Reactive Hypoglycemia (2019) · cites this paper as [24]
The Background and Introduction states that the incretin effect accounts for at least 50% of insulin secreted after oral glucose. This supports the lower end of the claim, but the passage does not establish a 70% upper bound; no page number is available in our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Recent research has demonstrated that it is possible to reverse GIP resistance.
“recent research has demonstrated that it is possible to reverse GIP resistance.”
From Tirzepatide: Clinical review of the twincretin injectable (2023) · cites this paper as [19]

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Reduced Incretin Effect in Type 2 Diabetes
Knop, F. K., Vilsbøll, T., Højberg, P. V., Larsen, S., Madsbad, S., Vølund, A., Holst, J. J., & Krarup, T. (2007) · Diabetes · doi:10.2337/db07-0100 · Cited by 349 · see citing works
Glucagon-like peptide-1 treatment delays the onset of diabetes in 8 week-old db/db mice
Wang, Q.-H., & Brubaker, P. (2002) · Diabetologia · doi:10.1007/s00125-002-0828-3 · Cited by 348 · see citing works
Disruption of PC1/3 expression in mice causes dwarfism and multiple neuroendocrine peptide processing defects
Zhu, X., Zhou, A., Dey, A., Norrbom, C., Carroll, R., Zhang, C., Laurent, V., Lindberg, I., Ugleholdt, R., Holst, J. J., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162352599 · Cited by 348 · see citing works
A Gastric Inhibitory Polypeptide II: The Complete Amino Acid Sequence
Brown, J. C., & Dryburgh, J. R. (1971) · Canadian Journal of Biochemistry · doi:10.1139/o71-122 · Cited by 344 · see citing works
Glucagon-like peptide 1 has a physiological role in the control of postprandial glucose in humans: studies with the antagonist exendin 9-39.
Edwards, C. M., Todd, J. F., Mahmoudi, M., Wang, Z., Wang, R. M., Ghatei, M. A., & Bloom, S. R. (1999) · Diabetes · doi:10.2337/diabetes.48.1.86 · Cited by 344 · cited 2× · see citing works
“Removal of GLP-1 action, whether by Ex-9-39 or by its immunoneutralization, causes increases in both fasting and postprandial glycemia and reduces glucose-stimulated insulin release in both animals and humans (Kolligs et al., 1995; Wang et al., 1995; D’Alessio et al., 1996; Edwards et al., 1999; Baggio et al., 2000).”
Background
Divergent tissue-specific and developmental expression of receptors for glucagon and glucagon-like peptide-1 in the mouse.
Campos, R. V., Lee, Y. C., & Drucker, D. J. (1994) · Endocrinology · doi:10.1210/endo.134.5.8156917 · Cited by 342 · see citing works
Peripheral Oxyntomodulin Reduces Food Intake and Body Weight Gain in Rats
Dakin, C. L., Small, C. J., Batterham, R. L., Neary, N. M., Cohen, M. A., Patterson, M., Ghatei, M. A., & Bloom, S. R. (2004) · Endocrinology · doi:10.1210/en.2003-1338 · Cited by 342 · see citing works
A Meta-Analysis of the Effect of Glucagon-Like Peptide-1 (7-36) Amide on Ad Libitum Energy Intake in Humans
Verdich, C. (2001) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.86.9.4382 · Cited by 340 · see citing works
Glucagon-like peptide-1 prevents beta cell glucolipotoxicity
Joly, E. C., Prentki, M., Buteau, J., El-Assaad, W., Rhodes, C. J., & Rosenberg, L. (2004) · Diabetologia · doi:10.1007/s00125-004-1379-6 · Cited by 337 · see citing works
Distribution of glucagonlike peptide I (GLP‐I), glucagon, and glicentin in the rat brain: An immunocytochemical study
Jin, S.-L. C., Han, V. K. M., Simmons, J. G., Towle, A. C., Lauder, J. M., & Lund, P. K. (1988) · The Journal of Comparative Neurology · doi:10.1002/cne.902710405 · Cited by 335 · see citing works
Identification and Actions of Gastric Inhibitory Polypeptide
Brown, J. C., Dryburgh, J. R., ROSS, S. A., & DUPRÉ, J. (1975) · Elsevier eBooks · doi:10.1016/b978-0-12-571131-9.50017-7 · Cited by 333 · see citing works
Glucagonostatic Actions and Reduction of Fasting Hyperglycemia by Exogenous Glucagon-Like Peptide I(7–36) amide in type I diabetic patients
Creutzfeldt, W., Kleine, N., Willms, B., Ørskov, C., Holst, J. J., & Nauck, M. A. (1996) · Diabetes Care · doi:10.2337/diacare.19.6.580 · Cited by 328 · see citing works
Glucagon-like Peptide-1 Activation of TCF7L2-dependent Wnt Signaling Enhances Pancreatic Beta Cell Proliferation
Liu, Z., & Habener, J. F. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706105200 · Cited by 323 · see citing works
Glucagon-like peptide 1 and exendin-4 convert pancreatic AR42J cells into glucagon- and insulin-producing cells.
Zhou, J., Wang, X., Piñeyro, M. A., & Egan, J. (1999) · Diabetes · doi:10.2337/diabetes.48.12.2358 · Cited by 319 · see citing works
Self-citation
Glucagon-like peptide-1 but not glucagon-like peptide-2 stimulates insulin release from isolated rat pancreatic islets
Schmidt, W. E., Siegel, E. G., & Creutzfeldt, W. (1985) · Diabetologia · doi:10.1007/bf00291980 · Cited by 318 · see citing works
The Murine Glucagon-Like Peptide-1 Receptor Is Essential for Control of Bone Resorption
Yamada, C., Yamada, Y., Tsukiyama, K., Yamada, K., Udagawa, N., Takahashi, N., Tanaka, K., Drucker, D. J., Seino, Y., & Inagaki, N. (2008) · Endocrinology · doi:10.1210/en.2007-1292 · Cited by 318 · see citing works
Central Administration of Glucagon-Like Peptide-1 Activates Hypothalamic Neuroendocrine Neurons in the Rat
Larsen, P. J., Tang‐Christensen, M., & Jessop, D. S. (1997) · Endocrinology · doi:10.1210/endo.138.10.5270 · Cited by 316 · see citing works
Arcuate Glucagon-Like Peptide 1 Receptors Regulate Glucose Homeostasis but Not Food Intake
Sandoval, D. A., Bagnol, D., Woods, S. C., D’Alessio, D. A., & Seeley, R. J. (2008) · Diabetes · doi:10.2337/db07-1824 · Cited by 316 · see citing works
Gastric inhibitory polypeptide (GIP) dose-dependently stimulates glucagon secretion in healthy human subjects at euglycaemia
Meier, J. J., Gallwitz, B., Siepmann, N., Holst, J. J., Deacon, C. F., Schmidt, W. E., & Nauck, M. A. (2003) · Diabetologia · doi:10.1007/s00125-003-1103-y · Cited by 314 · see citing works
Improved Glycemic Control With No Weight Increase in Patients With Type 2 Diabetes After Once-Daily Treatment With the Long-Acting Glucagon-Like Peptide 1 Analog Liraglutide (NN2211)
Madsbad, S., Schmitz, O., Ranstam, J., Jakobsen, G., Matthews, D. R., & on behalf of the NN2211-1310 International Study Group (2004) · Diabetes Care · doi:10.2337/diacare.27.6.1335 · Cited by 312 · see citing works
The carboxy-terminal segment of the yeast α-factor receptor is a regulatory domain
Reneke, J. E., Blumer, K., Courchesne, W. E., & Thorner, J. W. (1988) · Cell · doi:10.1016/0092-8674(88)90045-1 · Cited by 311 · see citing works
Brain glucagon-like peptide-1 increases insulin secretion and muscle insulin resistance to favor hepatic glycogen storage
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Double Incretin Receptor Knockout (DIRKO) Mice Reveal an Essential Role for the Enteroinsular Axis in Transducing the Glucoregulatory Actions of DPP-IV Inhibitors
Hansotia, T., Baggio, L. L., Delmeire, D., Hinke, S. A., Yamada, Y., Tsukiyama, K., Seino, Y., Holst, J. J., Schuit, F., & Drucker, D. J. (2004) · Diabetes · doi:10.2337/diabetes.53.5.1326 · Cited by 309 · see citing works
The insulinotropic actions of glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (7–37) in normal and diabetic subjects
Elahi, D., McAloon-Dyke, M., Fukagawa, N. K., Meneilly, G. S., Sclater, A. L., Minaker, K. L., Habener, J. F., & Andersen, D. K. (1994) · Regulatory Peptides · doi:10.1016/0167-0115(94)90136-8 · Cited by 308 · see citing works
Glucagon-Like Peptide-1 Inhibits Apoptosis of Insulin-Secreting Cells via a Cyclic 5′-Adenosine Monophosphate-Dependent Protein Kinase A- and a Phosphatidylinositol 3-Kinase-Dependent Pathway
Hui, H., Nourparvar, A., Zhao, X., & Perfetti, R. (2003) · Endocrinology · doi:10.1210/en.2002-220897 · Cited by 307 · see citing works
Peripheral Exendin-4 and Peptide YY3–36 Synergistically Reduce Food Intake through Different Mechanisms in Mice
Talsania, T., Anini, Y., Siu, S., Drucker, D. J., & Brubaker, P. L. (2005) · Endocrinology · doi:10.1210/en.2005-0473 · Cited by 306 · see citing works
Activation of proglucagon gene transcription by protein kinase-A in a novel mouse enteroendocrine cell line
Drucker, D. J., Jin, T., Asa, S. L., Young, T. A., & Brubaker, P. L. (1994) · Molecular Endocrinology · doi:10.1210/mend.8.12.7535893 · Cited by 303 · see citing works
Repeated Intracerebroventricular Administration of Glucagon-Like Peptide-1-(7–36) Amide or Exendin-(9–39) Alters Body Weight in the Rat**This work was supported by the United Kingdom Medical Research Council.
Meeran, K., O’Shea, D., Edwards, C. M. B., Turton, M. D., Heath, M. M., Gunn, I., Abusnana, S., Rossi, M., Small, C. J., Goldstone, A. P., et al. (1999) · Endocrinology · doi:10.1210/endo.140.1.6421 · Cited by 303 · see citing works
Glucagon-Like Peptide I Receptors in the Subfornical Organ and the Area Postrema Are Accessible to Circulating Glucagon-Like Peptide I
Ørskov, C., Poulsen, S. S., Mørten, M., & Holst, J. J. (1996) · Diabetes · doi:10.2337/diab.45.6.832 · Cited by 303 · see citing works
Degradation of Endogenous and Exogenous Gastric Inhibitory Polypeptide in Healthy and in Type 2 Diabetic Subjects as Revealed Using a New Assay for the Intact Peptide
Deacon, C. F. (2000) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.85.10.3575 · Cited by 303 · see citing works
Direct Effects of Glucagon-Like Peptide-1 on Myocardial Contractility and Glucose Uptake in Normal and Postischemic Isolated Rat Hearts
Zhao, T., Parikh, P., Bhashyam, S., Bölükoglu, H., Poornima, I. G., Shen, Y., & Shannon, R. P. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.100982 · Cited by 298 · see citing works
Epac-selective cAMP Analog 8-pCPT-2′-O-Me-cAMP as a Stimulus for Ca2+-induced Ca2+ Release and Exocytosis in Pancreatic β-Cells
Kang, G., Joseph, J. W., Chepurny, O. G., Monaco, M., Wheeler, M. B., Bos, J. L., Schwede, F., Genieser, H.-G., & Holz, G. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211682200 · Cited by 298 · see citing works
Exenatide augments first- and second-phase insulin secretion in response to intravenous glucose in subjects with type 2 diabetes
Fehse, F., Trautmann, M., Holst, J. J., Halseth, A. E., Nanayakkara, N., Nielsen, L. L., Fineman, M. S., Kim, D. D., & Nauck, M. A. (2005) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2005-1093 · Cited by 297 · see citing works
Protective effects of GLP-1 analogues exendin-4 and GLP-1(9–36) amide against ischemia–reperfusion injury in rat heart
Sonne, D. P., Engstrøm, T., & Treiman, M. (2007) · Regulatory Peptides · doi:10.1016/j.regpep.2007.10.001 · Cited by 294 · see citing works
Glucagon-Like Peptide-1-Responsive Catecholamine Neurons in the Area Postrema Link Peripheral Glucagon-Like Peptide-1 with Central Autonomic Control Sites
Yamamoto, H., Kishi, T., Lee, C. E., Choi, B. J., Fang, H., Hollenberg, A. N., Drucker, D. J., & Elmquist, J. K. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-07-02939.2003 · Cited by 294 · see citing works
β-Cell Secretory Products Activate α-Cell ATP-Dependent Potassium Channels to Inhibit Glucagon Release
Franklin, I., Gromada, J., Gjinovci, A., Theander, S., & Wollheim, C. (2005) · Diabetes · doi:10.2337/diabetes.54.6.1808 · Cited by 291 · see citing works
Receptor gene expression of glucagon-like peptide-1, but not glucose-dependent insulinotropic polypeptide, in rat nodose ganglion cells
Nakagawa, A., 佐竹, 英., Nakabayashi, H., Nishizawa, M., Furuya, K., Nakano, S., Kigoshi, T., Nakayama, K., & Uchida, K. (2004) · Autonomic Neuroscience · doi:10.1016/j.autneu.2003.11.001 · Cited by 290 · see citing works
Insulinotropic Action of Glucagonlike Peptide-I-(7–37) in Diabetic and Nondiabetic Subjects
Nathan, D. M., Schreiber, E., Fogel, H., Mojsov, S., & Habener, J. F. (1992) · Diabetes Care · doi:10.2337/diacare.15.2.270 · Cited by 289 · see citing works
Glucokinase as pancreatic beta cell glucose sensor and diabetes gene.
Matschinsky, F. M., Liang, Y. T., Kesavan, P., Wang, L., Froguel, P., Velho, G., Cohen, D., Permutt, M. A., Tanizawa, Y., & Jetton, T. L. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116809 · Cited by 287 · see citing works
Modulation of taste sensitivity by GLP‐1 signaling
Shin, Y., Martin, B., Golden, E. J., Dotson, C. D., Maudsley, S. R., Kim, W., Jang, H.-J., Mattson, M. P., Drucker, D. J., Egan, J. M., et al. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05397.x · Cited by 287 · see citing works
Self-citation
A novel lipid‐anchored A‐kinase Anchoring Protein facilitates cAMP‐responsive membrane events
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Analysis of upstream glucokinase promoter activity in transgenic mice and identification of glucokinase in rare neuroendocrine cells in the brain and gut.
Jetton, T. L., Liang, Y. T., Pettepher, C. C., Zimmerman, E. C., Cox, F., Horvath, K., Matschinsky, F. M., & Magnuson, M. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41910-7 · Cited by 279 · see citing works
On the treatment of Diabetus mellitus by acid extract of Duodenal Mucous Membrane
Moore, B., Edie, E. S., & Abram, J. H. (1906) · Biochemical Journal · doi:10.1042/bj0010028 · Cited by 279 · see citing works
Betacellulin and activin A coordinately convert amylase-secreting pancreatic AR42J cells into insulin-secreting cells.
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Endogenous glucagon-like peptide 1 controls endocrine pancreatic secretion and antro-pyloro-duodenal motility in humans
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Role of Leptin in the Regulation of Glucagon-Like Peptide-1 Secretion
Anini, Y., & Brubaker, P. L. (2003) · Diabetes · doi:10.2337/diabetes.52.2.252 · Cited by 274 · see citing works
ENTEROGLUCAGON
Holst, J. J. (1997) · Annual Review of Physiology · doi:10.1146/annurev.physiol.59.1.257 · Cited by 269 · see citing works
GIF biology and fat metabolism
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Glucagon gene expression in vertebrate brain.
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Osteoblast-Derived Cells Express Functional Glucose-Dependent Insulinotropic Peptide Receptors1
Bollag, R. J., Zhong, Q. P. W., Phillips, P., Min, L., Zhong, L., Cameron, R. S., Mulloy, A. L., Rasmussen, H., Qin, F., Ding, K., et al. (2000) · Endocrinology · doi:10.1210/endo.141.3.7366 · Cited by 265 · see citing works
Neonatal Exendin-4 Prevents the Development of Diabetes in the Intrauterine Growth Retarded Rat
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Cellular regulation of islet hormone secretion by the incretin hormone glucagon-like peptide 1
Gromada, J., Holst, J. J., & Rorsman, P. (1998) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s004240050558 · Cited by 254 · see citing works
Gluco-incretins control insulin secretion at multiple levels as revealed in mice lacking GLP-1 and GIP receptors
Preitner, F., Ibberson, M. R., Franklin, I., Binnert, C., Pende, M., Gjinovci, A., Hansotia, T., Drucker, D. J., Wollheim, C. B., Burcelin, R., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20518 · Cited by 254 · see citing works
Protein Kinase Cζ Activation Mediates Glucagon-Like Peptide-1–Induced Pancreatic β-Cell Proliferation
Buteau, J., Foisy, S., Rhodes, C. J., Carpenter, L., Biden, T. J., & Prentki, M. (2001) · Diabetes · doi:10.2337/diabetes.50.10.2237 · Cited by 252 · see citing works
Expression and Functional Activity of Glucagon, Glucagon-Like Peptide I, and Glucose-Dependent Insulinotropic Peptide Receptors in Rat Pancreatic Islet Cells
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Glucose Competence of the Hepatoportal Vein Sensor Requires the Presence of an Activated Glucagon-Like Peptide-1 Receptor
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Tornehave, D., Kristensen, P., Rømer, J., Knudsen, L. B., & Heller, R. S. (2008) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.2008.951319 · Cited by 248 · see citing works
β-Cell Pdx1 Expression Is Essential for the Glucoregulatory, Proliferative, and Cytoprotective Actions of Glucagon-Like Peptide-1
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The Insulinotropic Effect of Acute Exendin-4 Administered to Humans: Comparison of Nondiabetic State to Type 2 Diabetes
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Self-citation

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A human liver cell atlas reveals heterogeneity and epithelial progenitors
Aizarani, N., Saviano, A., Sagar, Mailly, L., Durand, S., Herman, J. S., Pessaux, P., Baumert, T. F., & Grün, D. (2019) · Nature · doi:10.1038/s41586-019-1373-2 · Cited by 1,147 · see citing works
Incretin therapies: highlighting common features and differences in the modes of action of glucagon‐like peptide‐1 receptor agonists and dipeptidyl peptidase‐4 inhibitors
Nauck, M. (2016) · Diabetes, Obesity and Metabolism · doi:10.1111/dom.12591 · Cited by 429 · see citing works
Energy intake and exercise as determinants of brain health and vulnerability to injury and disease
Mattson, M. P. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.08.012 · Cited by 434 · see citing works
<scp>GLP</scp> ‐1 receptor activated insulin secretion from pancreatic β‐cells: mechanism and glucose dependence
Meloni, A. R., DeYoung, M. B., Lowe, C., & Parkes, D. G. (2013) · Diabetes, Obesity and Metabolism · doi:10.1111/j.1463-1326.2012.01663.x · Cited by 407 · see citing works
Anti-diabetic actions of glucagon-like peptide-1 on pancreatic beta-cells
Lee, Y.-S., & Jun, H.-S. (2014) · Metabolism · doi:10.1016/j.metabol.2013.09.010 · Cited by 315 · see citing works
Glucagon-like peptide-1: a multi-faceted anti-inflammatory agent
Mehdi, S. F., Pusapati, S., Anwar, M. S., Lohana, D., Kumar, P., Nandula, S. A., Nawaz, F. K., Tracey, K., Yang, H., LeRoith, D., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1148209 · Cited by 317 · see citing works
Metabolic effects of non-nutritive sweeteners
Pepino, M. Y. (2015) · Physiology & Behavior · doi:10.1016/j.physbeh.2015.06.024 · Cited by 285 · see citing works
A high-protein diet for reducing body fat: mechanisms and possible caveats
Pesta, D. H., & Samuel, V. T. (2014) · Nutrition & Metabolism · doi:10.1186/1743-7075-11-53 · Cited by 276 · see citing works
“Incretins potentiate glucose disposal by stimulating insulin secretion, estimated to account for at least 50% of the total postprandial insulin release [30,31].”
Native incretins prevent the development of atherosclerotic lesions in apolipoprotein E knockout mice
Nagashima, M., Watanabe, T., Terasaki, M., Tomoyasu, M., Nohtomi, K., Kim-Kaneyama, J., Miyazaki, A., & Hirano, T. (2011) · Diabetologia · doi:10.1007/s00125-011-2241-2 · Cited by 259 · see citing works
Effects of Glucagon-Like Peptide-1 on Oxidative Stress and Nrf2 Signaling
Oh, Y., & Jun, H.-S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms19010026 · Cited by 217 · see citing works
“Many studies have reported on the preventive effects of GLP-1 and GLP-1R agonists on beta cells against various toxic stimuli including glucose, fatty acids, cytokines, and ROS [65].”
Background
Biosynthesis and Chemical Applications of Thioamides
Mahanta, N., Szantai-Kis, D. M., Petersson, E. J., & Mitchell, D. A. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.8b01022 · Cited by 218 · see citing works
Cardiovascular effects of gliptins
Scheen, A. J. (2013) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2012.183 · Cited by 175 · see citing works
Pathophysiology of NASH: perspectives for a targeted treatment
Marra, F., & Lotersztajn, S. (2013) · Current Pharmaceutical Design · doi:10.2174/13816128113199990344 · Cited by 163 · see citing works
Glucagon-Like Peptide-1 Receptor Agonist Inhibits Asymmetric Dimethylarginine Generation in the Kidney of Streptozotocin-Induced Diabetic Rats by Blocking Advanced Glycation End Product–Induced Protein Arginine Methyltranferase-1 Expression
Ojima, A., Ishibashi, Y., Matsui, T., Maeda, S., Nishino, Y., Takeuchi, M., Fukami, K., & Yamagishi, S.-I. (2013) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.09.016 · Cited by 156 · see citing works
A glucagon-like peptide-1 analog liraglutide suppresses macrophage foam cell formation and atherosclerosis
Tashiro, Y., Sato, K., Watanabe, T., Nohtomi, K., Terasaki, M., Nagashima, M., & Hirano, T. (2014) · Peptides · doi:10.1016/j.peptides.2013.12.015 · Cited by 149 · see citing works
The GLP-1 receptor agonist liraglutide inhibits progression of vascular disease via effects on atherogenesis, plaque stability and endothelial function in an ApoE −/− mouse model
Gaspari, T., Welungoda, I., Widdop, R. E., Simpson, R. W., & Dear, A. E. (2013) · Diabetes and Vascular Disease Research · doi:10.1177/1479164113481817 · Cited by 148 · see citing works
The intestine as an endocrine organ and the role of gut hormones in metabolic regulation
Bany Bakar, R., Reimann, F., & Gribble, F. M. (2023) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-023-00830-y · Cited by 144 · see citing works
Effects of GLP-1 and Incretin-Based Therapies on Gastrointestinal Motor Function
Marathe, C. S., Rayner, C. K., Jones, K. L., & Horowitz, M. (2011) · Experimental Diabetes Research · doi:10.1155/2011/279530 · Cited by 138 · see citing works
A New Treatment Strategy for Parkinson's Disease through the Gut–Brain Axis: The Glucagon-Like Peptide-1 Receptor Pathway
Kim, D. S., Choi, H.-I., Wang, Y., Luo, Y., Hoffer, B. J., & Greig, N. H. (2017) · Cell Transplantation · doi:10.1177/0963689717721234 · Cited by 136 · see citing works
Incretin and insulin signaling as novel therapeutic targets for Alzheimer’s and Parkinson’s disease
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Authors: Kim, W., & Egan, J. M.
Affiliations: National Institutes of Health (US)
ORCID: Egan, Josephine M.
Venue: Pharmacological Reviews
Publisher: Elsevier BV
Published: 2008-12
Volume: 60
Issue: 4
Pages: 470-512
ISSN: 0031-6997 (ISSN-L)
DOI: 10.1124/pr.108.000604
PMC: PMC2696340
OpenAlex: W2146466098
Cited by: 824
References: 565
Citations by year: 2026: 17 · 2025: 46 · 2024: 43 · 2023: 50 · 2022: 44 · 2021: 41 · 2020: 45 · 2019: 50 · 2018: 54 · 2017: 63 · 2016: 49 · 2015: 53 · 2014: 61 · 2013: 53 · 2012: 52
FWCI: 4.81
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Pharmacological Reviews (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Institute on Aging (Z01AG000905)
Topics: Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Management and Research
Keywords: incretins, glucose-dependent insulinotropic polypeptide, glucagon-like peptide-1, dipeptidyl peptidase IV, type 2 diabetes, glucose homeostasis, insulin secretion, exenatide, sitagliptin, GLP-1 receptor agonists, DPP-4 inhibitors, incretin mimetics, hypoglycemia
MeSH terms: Sitagliptin Phosphate, Exenatide, Animals, Diabetes Mellitus, Glucose, Homeostasis, Humans, Hypoglycemic Agents, Peptides, Pyrazines, Triazoles, Venoms, Incretins

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The role of incretins in glucose homeostasis and diabetes treatment

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