Cited by 1,124Diabetes Treatment and ManagementPeptidase Inhibition and AnalysisPancreatic function and diabetes

The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.

Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV.

Kieffer, T J, McIntosh, C H, Pederson, R A·1995·Endocrinology

Open this paper in CoChat — free account

Abstract

The combined actions of glucose-dependent insulinotropic polypeptide (GIP) and truncated glucagon-like peptide-1 (tGLP-1) may fully account for the incretin effect. These hormones are released from the small intestine in response to oral glucose and stimulate insulin release. Recently, evidence has been provided demonstrating the degradation of GIP-(1-42) and GLP-1-(7-36)NH2 by the serum enzyme dipeptidyl peptidase IV (DPP IV) into the biologically inactive products GIP-(3-42) and GLP-1-(9-36)NH2. The objective of the current investigation was to develop a method to monitor the degradation of these hormones in vivo. Synthetic peptides were radiolabeled and purified by HPLC. Subsequent degradation of the peptides under various conditions was then monitored by further HPLC analysis. Incubation of [125I]GIP-(1-42) or [125I]GLP-1-(7-36)NH2 with Wistar rat serum or purified DPP IV resulted in the major N-terminal-truncated products [125I]GIP-(3-42) and [125I]GLP-1-(9-36)NH2. These products were significantly reduced when the specific DPP IV inhibitor diprotin A was included in the incubation mixture and were absent when serum from DPP IV-deficient rats was used. When the labeled peptides were infused into rats at hormone levels within the physiological range, over 50% was metabolized to the truncated forms within 2 min. These products were absent when the tracers were infused into DPP IV-deficient animals. It is concluded that DPP IV may be a primary inactivating enzyme of both GIP and tGLP-1 in vivo. As the N-terminal-truncated products of the DPP IV cleavage may not be distinguished from the biologically active hormone by currently employed assays, reports of circulating hormone levels should be reconsidered. The method described in this manuscript may be useful for investigating the durations of action of GIP and tGLP-1 in normal and pathophysiological conditions.

Integrity signals

Registry

Crossref · 10.1210/endo.136.8.7628397

Cites

36 of 36 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Glucagon-like peptide-1 7–36: a physiological incretin in man
Kreymann, B., Ghatei, M. A., Williams, G., & Bloom, S. R. (1987) · The Lancet · doi:10.1016/s0140-6736(87)91194-9 · Cited by 1,928
Preserved incretin activity of glucagon-like peptide 1 [7-36 amide] but not of synthetic human gastric inhibitory polypeptide in patients with type-2 diabetes mellitus
Nauck, M. A., Heimesaat, M. M., Orskov, C., Holst, J. J., Ebert, R., & Creutzfeldt, W. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116186 · Cited by 1,651
Dipeptidyl‐peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon‐like peptide‐1(7–36)amide, peptide histidine methionine and is responsible for their degradation in human serum
MENTLEIN, R., GALLWITZ, B., & SCHMIDT, W. E. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17986.x · Cited by 1,161
Antidiabetogenic effect of glucagon-like peptide-1 (7–36)amide in normal subjects and patients with diabetes mellitus
Gutniak, M., Ørkov, C., Holst, J. J., Ahrén, B., & Efendić, S. (1992) · New England Journal of Medicine · doi:10.1056/nejm199205143262003 · Cited by 868
Preproglucagon gene expression in pancreas and intestine diversifies at the level of post-translational processing
Mojsov, S., Heinrich, G., Wilson, I. B., Ravazzola, M., Orci, L., & Habener, J. F. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67324-7 · Cited by 724
Hamster preproglucagon contains the sequence of glucagon and two related peptides
Bell, G. I., Santerre, R. F., & Mullenbach, G. T. (1983) · Nature · doi:10.1038/302716a0 · Cited by 649
Pancreatic beta-cells are rendered glucose-competent by the insulinotropic hormone glucagon-like peptide-1(7-37)
Holz, G. G., Kiihtreiber, W. M., & Habener, J. F. (1993) · Nature · doi:10.1038/361362a0 · Cited by 591
Proline-Dependent Structural and Biological Properties of Peptides and Proteins
Yaron, A., Naider, F. R., & Scharpé, S. (1993) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239309082572 · Cited by 551
A new dipeptide naphthylamidase hydrolyzing glycyl-prolyl-?-naphthylamide
Hopsu-Havu, V. K., & Glenner, G. G. (1966) · Histochemistry and Cell Biology · doi:10.1007/bf00577838 · Cited by 437
Entero-Insular Axis
Unger, R. H. (1969) · Archives of Internal Medicine · doi:10.1001/archinte.1969.00300130043007 · Cited by 371

Show all 36 references

Sorted by citations

The incretin system: Glucagon-like peptide-1 receptor agonists and dipeptidyl peptidase-4 inhibitors in type 2 diabetes
Drucker, D. J., & Nauck, M. A. (2006) · The Lancet · doi:10.1016/s0140-6736(06)69705-5 · Cited by 3,896
Biology of Incretins: GLP-1 and GIP
Baggio, L. L., & Drucker, D. J. (2007) · Gastroenterology · doi:10.1053/j.gastro.2007.03.054 · Cited by 3,639
The biology of incretin hormones
Drucker, D. J. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.01.004 · Cited by 2,210
Glucagon-like peptide 1 (GLP-1)
Müller, T. D., Finan, B., Bloom, S. R., D'Alessio, D., Drucker, D. J., Flatt, P. R., Fritsche, A., Gribble, F., Grill, H. J., Habener, J. F., et al. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.09.010 · Cited by 1,868
Glucagon-like peptide 1 promotes satiety and suppresses energy intake in humans.
Flint, A., Raben, A., Astrup, A., & Holst, J. J. (1998) · Journal of Clinical Investigation · doi:10.1172/jci990 · Cited by 1,402
Targeting proteases: successes, failures and future prospects
Turk, B. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2092 · Cited by 1,362
GLP-1 receptor agonists for individualized treatment of type 2 diabetes mellitus
Meier, J. J. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2012.140 · Cited by 1,311
Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides
Mentlein, R. (1999) · Regulatory Peptides · doi:10.1016/s0167-0115(99)00089-0 · Cited by 1,273
The Glucagon-Like Peptides
Kieffer, T. J., & Habener, J. F. (1999) · Endocrine Reviews · doi:10.1210/edrv.20.6.0385 · Cited by 1,062
Self-citation
Cardioprotective and Vasodilatory Actions of Glucagon-Like Peptide 1 Receptor Are Mediated Through Both Glucagon-Like Peptide 1 Receptor–Dependent and –Independent Pathways
Ban, K., Noyan-Ashraf, M. H., Hoefer, J., Bolz, S.-S., Drucker, D. J., & Husain, M. (2008) · Circulation · doi:10.1161/circulationaha.107.739938 · Cited by 1,057
Glucagon-like peptide-1 receptor: mechanisms and advances in therapy
Zheng, Z., Zong, Y., Ma, Y., Tian, Y., Pang, Y., Zhang, C., & Gao, J. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01931-z · Cited by 1,036
Dipeptidyl-Peptidase IV from Bench to Bedside: An Update on Structural Properties, Functions, and Clinical Aspects of the Enzyme DPP IV
Lambeir, A.-M., Durinx, C., Scharpé, S., & De Meester, I. (2003) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/713609354 · Cited by 955
The role of incretins in glucose homeostasis and diabetes treatment
Kim, W., & Egan, J. M. (2008) · Pharmacological Reviews · doi:10.1124/pr.108.000604 · Cited by 824
(2 R )-4-Oxo-4-[3-(Trifluoromethyl)-5,6-dihydro[1,2,4]triazolo[4,3- a ]pyrazin- 7(8 H )-yl]-1-(2,4,5-trifluorophenyl)butan-2-amine: A Potent, Orally Active Dipeptidyl Peptidase IV Inhibitor for the Treatment of Type 2 Diabetes
Kim, D., Wang, L., Beconi, M. G., Eiermann, G. J., Fisher, M. H., He, H., Hickey, G. J., Kowalchick, J. E., Leiting, B., Lyons, K. A., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0493156 · Cited by 827
GIP and GLP-1, the two incretin hormones: Similarities and differences
Seino, Y., Fukushima, M., & Yabe, D. (2010) · Journal of Diabetes Investigation · doi:10.1111/j.2040-1124.2010.00022.x · Cited by 746
Inhibition of Dipeptidyl Peptidase-4 Reduces Glycemia, Sustains Insulin Levels, and Reduces Glucagon Levels in Type 2 Diabetes
Åhrén, B., Landin‐Olsson, M., Jansson, P., Svensson, M. K. E., Holmes, D., & Schweizer, A. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-031907 · Cited by 706
Gut microbes and metabolites as modulators of blood-brain barrier integrity and brain health
Parker, A., Fonseca, S., & Carding, S. R. (2019) · Gut Microbes · doi:10.1080/19490976.2019.1638722 · Cited by 745
Potent Derivatives of Glucagon-like Peptide-1 with Pharmacokinetic Properties Suitable for Once Daily Administration
Knudsen, L. B., Nielsen, P. F., Huusfeldt, P. O., Johansen, N. L., Madsen, K., Pedersen, F. Z., Thøgersen, H., Wilken, M., & Agersø, H. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm9909645 · Cited by 711
Incretin-based therapies for type 2 diabetes mellitus
Lovshin, J. A., & Drucker, D. J. (2009) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2009.48 · Cited by 645
Discovery and Preclinical Profile of Saxagliptin (BMS-477118): A Highly Potent, Long-Acting, Orally Active Dipeptidyl Peptidase IV Inhibitor for the Treatment of Type 2 Diabetes
Augeri, D. J., Robl, J. A., Betebenner, D. A., Magnin, D. R., Khanna, A., Robertson, J. G., Wang, A., Simpkins, L. M., Taunk, P. C., Huang, Q. Z., et al. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm050261p · Cited by 629
1-[[(3-Hydroxy-1-adamantyl)amino]acetyl]-2-cyano-(S)-pyrrolidine: A Potent, Selective, and Orally Bioavailable Dipeptidyl Peptidase IV Inhibitor with Antihyperglycemic Properties
Villhauer, E. B., Brinkman, J. A., Naderi, G. B., Burkey, B. F., Dunning, B. E., Prasad, K., Mangold, B. L. K., Russell, M. E., & Hughes, T. E. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm030091l · Cited by 618
The role of gut hormones in glucose homeostasis
Drucker, D. J. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30076 · Cited by 628
Pharmacology, Physiology, and Mechanisms of Action of Dipeptidyl Peptidase-4 Inhibitors
Mulvihill, E. E., & Drucker, D. J. (2014) · Endocrine Reviews · doi:10.1210/er.2014-1035 · Cited by 641
Glucagon-Like Peptides
Drucker, D. J. (1998) · Diabetes · doi:10.2337/diab.47.2.159 · Cited by 598
Glucagon-Like Peptide-1-(7–36)Amide Is Transformed to Glucagon-Like Peptide-1-(9–36)Amide by Dipeptidyl Peptidase IV in the Capillaries Supplying the L Cells of the Porcine Intestine1
Hansen, L., Deacon, C. F., Ørskov, C., & Holst, J. J. (1999) · Endocrinology · doi:10.1210/endo.140.11.7143 · Cited by 595
Glucagon-like Peptide-1 Receptor Signaling Modulates β Cell Apoptosis
Li, Y., Hansotia, T., Yusta, B., Ris, F., Halban, P. A., & Drucker, D. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209423200 · Cited by 589
Enhancing Incretin Action for the Treatment of Type 2 Diabetes
Drucker, D. J. (2003) · Diabetes Care · doi:10.2337/diacare.26.10.2929 · Cited by 581
Exendin-4, a glucagon-like protein-1 (GLP-1) receptor agonist, reverses hepatic steatosis in ob/ob mice
Ding, X., Saxena, N. K., Lin, S., Gupta, N., & Anania, F. A. (2006) · Hepatology · doi:10.1002/hep.21006 · Cited by 557
Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26
Marguet, D., Baggio, L. L., Kobayashi, T., Bernard, A., Pierres, M., Nielsen, P. F., Ribel, U., Watanabe, T., Drucker, D. J., & Wagtmann, N. R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.120069197 · Cited by 538
The gut and energy balance: visceral allies in the obesity wars
Badman, M. K., & Flier, J. S. (2005) · Science · doi:10.1126/science.1109951 · Cited by 532
Incretin secretion in relation to meal size and body weight in healthy subjects and people with type 1 and type 2 diabetes mellitus
Vilsbøll, T., Krarup, T., Sonne, J., Madsbad, S., Vølund, A., Juul, A. G., & Holst, J. J. (2003) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2002-021873 · Cited by 528
Cardiovascular Biology of the Incretin System
Ussher, J. R., & Drucker, D. J. (2012) · Endocrine Reviews · doi:10.1210/er.2011-1052 · Cited by 534
Biomarkers of satiation and satiety
de Graaf, C., Blom, W. A. M., Smeets, P. A. M., Stafleu, A., & Hendriks, H. (2004) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/79.6.946 · Cited by 539
International Union of Pharmacology. XXXV. The Glucagon Receptor Family
Mayo, K. E., Miller, L. J., BATAILLE, D., Dalle, S., Göke, B., Thorens, B., & Drucker, D. J. (2003) · Pharmacological Reviews · doi:10.1124/pr.55.1.6 · Cited by 514
Biological actions and therapeutic potential of the glucagon-like peptides
Drucker, D. J. (2002) · Gastroenterology · doi:10.1053/gast.2002.31068 · Cited by 509
Dipeptidyl Peptidase IV Inhibition for the Treatment of Type 2 Diabetes
Lankas, G. R., Leiting, B., Roy, R. S., Eiermann, G. J., Beconi, M. G., Biftu, T., Chan, C., Edmondson, S. D., Feeney, W. P., He, H., et al. (2005) · Diabetes · doi:10.2337/diabetes.54.10.2988 · Cited by 494
Distribution and characterisation of Glucagon-like peptide-1 receptor expressing cells in the mouse brain
Cork, S. C., Richards, J. E., Holt, M. K., Gribble, F. M., Reimann, F., & Trapp, S. (2015) · Molecular Metabolism · doi:10.1016/j.molmet.2015.07.008 · Cited by 478
Interactions of Glucagon-Like Peptide-1 (GLP-1) with the Blood-Brain Barrier
Kastin, A. J., Akerstrom, V., & Pan, W. (2002) · Journal of Molecular Neuroscience · doi:10.1385/jmn:18:1-2:07 · Cited by 480
Energy intake and appetite are suppressed by glucagon-like peptide-1 (GLP-1) in obese men.
Näslund, E., Barkeling, B., King, N., Gutniak, M., Blundell, J., Holst, J., Rössner, S., & Hellström, P. (1999) · International Journal of Obesity · doi:10.1038/sj.ijo.0800818 · Cited by 468
Exendin-4 reduces fasting and postprandial glucose and decreases energy intake in healthy volunteers
Edwards, C. M. B., Stanley, S. A., Davis, R. P., Brynes, A. E., Frost, G. S., Seal, L., Ghatei, M. A., & Bloom, S. R. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.281.1.e155 · Cited by 468
Pharmacology of exenatide (synthetic exendin-4): a potential therapeutic for improved glycemic control of type 2 diabetes
Nielsen, L. L., Young, A. A., & Parkes, D. G. (2003) · Regulatory Peptides · doi:10.1016/j.regpep.2003.10.028 · Cited by 459
CD26, let it cut or cut it down
Meester, I. D., Korom, S., van Damme, J., & Scharpé, S. (1999) · Immunology Today · doi:10.1016/s0167-5699(99)01486-3 · Cited by 451
Gastrointestinal hormones and food intake
Strader, A. D., & Woods, S. C. (2005) · Gastroenterology · doi:10.1053/j.gastro.2004.10.043 · Cited by 461
Incretins, insulin secretion and Type 2 diabetes mellitus
Vilsbøll, T., & Holst, J. J. (2004) · Diabetologia · doi:10.1007/s00125-004-1342-6 · Cited by 456
Serine peptidases: Classification, structure and function
Page, M. J., & Di, E. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7565-9 · Cited by 441
Pharmacokinetics, pharmacodynamics, and safety of exenatide in patients with type 2 diabetes mellitus
Kolterman, O., Kim, D. D. H., Shen, L. Z., Ruggles, J. A., Nielsen, L. L., Fineman, M. S., & Baron, A. (2005) · American Journal of Health-System Pharmacy · doi:10.1093/ajhp/62.2.173 · Cited by 441
Physiology and Pharmacology of DPP-4 in Glucose Homeostasis and the Treatment of Type 2 Diabetes
Deacon, C. F. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00080 · Cited by 459
Inhibition of Dipeptidyl Peptidase IV Improves Metabolic Control Over a 4-Week Study Period in Type 2 Diabetes
Ahrén, B., Simonsson, E., Larsson, H., Landin-Olsson, M., Torgeirsson, H., Jansson, P.-A., Sandqvist, M., Båvenholm, P., Efendic, S., Eriksson, J. W., et al. (2002) · Diabetes Care · doi:10.2337/diacare.25.5.869 · Cited by 421
Minireview: The Glucagon-Like Peptides
Drucker, D. J. (2001) · Endocrinology · doi:10.1210/endo.142.2.7983 · Cited by 419
The New Biology and Pharmacology of Glucagon
Müller, T. D., Finan, B., Clemmensen, C., DiMarchi, R. D., & Tschöp, M. H. (2017) · Physiological Reviews · doi:10.1152/physrev.00025.2016 · Cited by 419
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., Nauck, M. A., Meier, J. J., Hücking, K., & Holst, J. J. (2000) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.85.10.6855 · Cited by 445
DPP-4 inhibitors and their potential role in the management of type 2 diabetes
Barnett, A. H. (2006) · International Journal of Clinical Practice · doi:10.1111/j.1742-1241.2006.01178.x · Cited by 396
The glucagon-like peptide 1 (GLP) receptor as a therapeutic target in Parkinson's disease: mechanisms of action
Athauda, D., & Foltynie, T. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.01.013 · Cited by 383
Therapeutic Potential of Boron-Containing Compounds
Baker, S. J., Ding, C. Z., Akama, T., Zhang, Y.-K., Hernandez, V. S., & Xia, Y. (2009) · Future Medicinal Chemistry · doi:10.4155/fmc.09.71 · Cited by 377
Gut Hormones and Appetite Control: A Focus on PYY and GLP-1 as Therapeutic Targets in Obesity
Silva, A. D., & Bloom, S. R. (2012) · Gut and Liver · doi:10.5009/gnl.2012.6.1.10 · Cited by 373
Dipeptidyl peptidase 4 inhibitors in the treatment of type 2 diabetes mellitus
Deacon, C. F. (2020) · Nature Reviews Endocrinology · doi:10.1038/s41574-020-0399-8 · Cited by 398
Dipeptidyl Peptidase-4 Inhibition and the Treatment of Type 2 Diabetes
Drucker, D. J. (2007) · Diabetes Care · doi:10.2337/dc07-0228 · Cited by 367
CD26: A Multifunctional Integral Membrane and Secreted Protein of Activated Lymphocytes
Gorrell, M. D., Gysbers, V., & McCaughan, G. W. (2001) · Scandinavian Journal of Immunology · doi:10.1046/j.1365-3083.2001.00984.x · Cited by 366
Entry of exendin-4 into brain is rapid but may be limited at high doses
Kastin, A. J., & Akerstrom, V. L. (2003) · International Journal of Obesity · doi:10.1038/sj.ijo.0802206 · Cited by 358
Mice lacking dipeptidyl peptidase IV are protected against obesity and insulin resistance
Conarello, S., Li, Z., Ronan, J., Roy, R. S., Zhu, L., Jiang, G., Liu, F., Woods, J. W., Zycband, E., Moller, D. E., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0631828100 · Cited by 348
Gastrointestinal hormones regulating appetite
Chaudhri, O. B., Small, C. J., & Bloom, S. R. (2006) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2006.1856 · Cited by 362
Peptide hormone exendin‐4 stimulates subventricular zone neurogenesis in the adult rodent brain and induces recovery in an animal model of parkinson's disease
Bertilsson, G., Patrone, C., Zachrisson, O., Andersson, A., Dannaeus, K., Heidrich, J., Kortesmaa, J., Mercer, A., Nielsen, E., Rönnholm, H., et al. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21483 · Cited by 345
The multifunctional or moonlighting protein CD26/DPPIV
Boonacker, E., & Noorden, C. J. F. V. (2003) · European Journal of Cell Biology · doi:10.1078/0171-9335-00302 · Cited by 337
Secretion, Degradation, and Elimination of Glucagon-Like Peptide 1 and Gastric Inhibitory Polypeptide in Patients with Chronic Renal Insufficiency and Healthy Control Subjects
Meier, J. J., Nauck, M. A., Kranz, D., Holst, J. J., Deacon, C. F., Gaeckler, D., Schmidt, W. E., & Gallwitz, B. (2004) · Diabetes · doi:10.2337/diabetes.53.3.654 · Cited by 334
Dipeptidyl Peptidase IV Inhibitor Treatment Stimulates β-Cell Survival and Islet Neogenesis in Streptozotocin-Induced Diabetic Rats
Pospisilik, J. A., Martin, J., Doty, T., Ehses, J. A., Pamir, N., Lynn, F. C., Piteau, S., Demuth, H.-U., McIntosh, C. H. S., & Pederson, R. A. (2003) · Diabetes · doi:10.2337/diabetes.52.3.741 · Cited by 332
Self-citation
Insulin resistance and Parkinson’s disease: A new target for disease modification?
Athauda, D. S., & Foltynie, T. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.10.001 · Cited by 340
Glucagon-like peptide-1 (GLP-1) receptors expressed on nerve terminals in the portal vein mediate the effects of endogenous GLP-1 on glucose tolerance in rats
Vahl, T. P., Tauchi, M., Durler, T. S., Elfers, E. E., Fernandes, T. M., Bitner, R. D., Ellis, K. S., Woods, S. C., Seeley, R. J., Herman, J. P., et al. (2007) · Endocrinology · doi:10.1210/en.2006-0153 · Cited by 318
Effects of glucagon-like peptide 1 on appetite and body weight: focus on the CNS
van Bloemendaal, L., ten Kulve, J. S., la Fleur, S. E., Ijzerman, R. G., & Diamant, M. (2014) · Journal of Endocrinology · doi:10.1530/joe-13-0414 · Cited by 312
Liraglutide for weight management: a critical review of the evidence
Mehta, A., Marso, S. P., & Neeland, I. J. (2017) · Obesity Science & Practice · doi:10.1002/osp4.84 · Cited by 311
European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS)
Egea, J., Fabregat, I., Frapart, Y., Ghezzi, P., Görlach, A., Kietzmann, T., Kubaichuk, K. I., Knaus, U. G., López, M. G., González, G. O., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.05.007 · Cited by 321
Engineering and characterization of the long‐acting glucagon‐like peptide‐1 analogue LY2189265, an Fc fusion protein
Glaesner, W., Vick, A., Millican, R. L., Ellis, B., Tschang, S., Tian, Y., Bokvist, K. B., Brenner, M. B., Köester, A., Pørksen, N. K., et al. (2010) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.1080 · Cited by 314
Dipeptidyl peptidase IV resistant analogues of glucagon-like peptide-1 which have extended metabolic stability and improved biological activity
Deacon, C. F., Knudsen, L. B., Madsen, K., Wiberg, F. C., Jacobsen, O., & Holst, J. J. (1998) · Diabetologia · doi:10.1007/s001250050903 · Cited by 304
A Novel Neurotrophic Property of Glucagon-Like Peptide 1: A Promoter of Nerve Growth Factor-Mediated Differentiation in PC12 Cells
Perry, T., Lahiri, D. K., Chen, D., Zhou, J., Shaw, K. T. Y., Egan, J. M., & Greig, N. H. (2002) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.300.3.958 · Cited by 303
Incretin-Based Therapies for Type 2 Diabetes Mellitus: Properties, Functions, and Clinical Implications
Nauck, M. A. (2010) · The American Journal of Medicine · doi:10.1016/j.amjmed.2010.11.002 · Cited by 298
Therapeutic Strategies Based on Glucagon-Like Peptide 1
Deacon, C. F. (2004) · Diabetes · doi:10.2337/diabetes.53.9.2181 · Cited by 296
8-(3-(R)-Aminopiperidin-1-yl)-7-but-2-ynyl-3-methyl-1-(4-methyl-quinazolin-2-ylmethyl)-3,7-dihydropurine-2,6-dione (BI 1356), a Highly Potent, Selective, Long-Acting, and Orally Bioavailable DPP-4 Inhibitor for the Treatment of Type 2 Diabetes
Eckhardt, M., Langkopf, E., Mark, M., Tadayyon, M., Thomas, L. H., Nar, H., Pfrengle, W., Guth, B. D., Lotz, R. R. H., Sieger, P., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm701280z · Cited by 293
Glucagon-like peptide 1(GLP-1) in biology and pathology
Meier, J. J., & Nauck, M. A. (2005) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.538 · Cited by 288
Regulation of Glucose Homeostasis by GLP-1
Nadkarni, P., Chepurny, O. G., & Holz, G. G. (2014) · Progress in Molecular Biology and Translational Science · doi:10.1016/b978-0-12-800101-1.00002-8 · Cited by 287
Regulation of the biological activity of glucagon-like peptide 2 in vivo by dipeptidyl peptidase IV
Drucker, D. J., Shi, Q., Crivici, A., Sumner-Smith, M., Tavares, W., Hill, M. E., DeForest, L., Cooper, S., & Brubaker, P. L. (1997) · Nature Biotechnology · doi:10.1038/nbt0797-673 · Cited by 278
Peptide therapeutics from venom: Current status and potential
Pennington, M. W., Czerwiński, A. A., & Norton, R. S. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.09.029 · Cited by 278
Peptides Derived from Atlantic Salmon Skin Gelatin as Dipeptidyl-peptidase IV Inhibitors
Li‐Chan, E. C. Y., Hunag, S.-L., Jao, C., Ho, K.-P., & Hsu, K. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf204720q · Cited by 270
Mechanism of action of inhibitors of dipeptidyl-peptidase-4 (DPP-4)
Thornberry, N. A., & Gallwitz, B. (2009) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2009.03.004 · Cited by 285
Molecular characterization of dipeptidyl peptidase activity in serum
Durinx, C., Lambeir, A., Bosmans, E., Falmagne, J., Berghmans, R., Haemers, A., Scharpé, S., & Meester, I. D. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01634.x · Cited by 267
Improved Glucose Tolerance in Zucker Fatty Rats by Oral Administration of the Dipeptidyl Peptidase IV Inhibitor Isoleucine Thiazolidide
Pederson, R. A., White, H. A., Schlenzig, D., Pauly, R. P., McIntosh, C. H. S., & Demuth, H. (1998) · Diabetes · doi:10.2337/diab.47.8.1253 · Cited by 267
Self-citation
GIF biology and fat metabolism
Yip, R. G. C., & Wolfe, M. M. (1999) · Life Sciences · doi:10.1016/s0024-3205(99)00314-8 · Cited by 266
Pharmacokinetic and pharmacodynamic properties of multiple oral doses of sitagliptin, a dipeptidyl peptidase-IV inhibitor: A double-blind, randomized, placebo-controlled study in healthy male volunteers
Bergman, A. J., Stevens, C., Zhou, Y., Yi, B., Laethem, M. E., Smet, M. D., Snyder, K., Hilliard, D. A., Tanaka, W. K., Zeng, W., et al. (2006) · Clinical Therapeutics · doi:10.1016/j.clinthera.2006.01.015 · Cited by 265
Mechanisms of action and therapeutic applications of GLP-1 and dual GIP/GLP-1 receptor agonists
Liu, Q. K. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1431292 · Cited by 265
The glucagon-like peptide 1 analog liraglutide reduces TNF-α-induced oxidative stress and inflammation in endothelial cells
Shiraki, A., Oyama, J.-I., Komoda, H., Asaka, M., Komatsu, A., Sakuma, M., Kodama, K., Sakamoto, Y., Kotooka, N., Hirase, T., et al. (2012) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2011.12.039 · Cited by 263
Systemic Administration of the Long-Acting GLP-1 Derivative NN2211 Induces Lasting and Reversible Weight Loss in Both Normal and Obese Rats
Larsen, P. J., Fledelius, C., Knudsen, L. B., & Tang‐Christensen, M. (2001) · Diabetes · doi:10.2337/diabetes.50.11.2530 · Cited by 259
Beyond the pancreas: contrasting cardiometabolic actions of GIP and GLP1
Hammoud, R., & Drucker, D. J. (2023) · Nature Reviews Endocrinology · doi:10.1038/s41574-022-00783-3 · Cited by 244
Sitagliptin Treatment at the Time of Hospitalization Was Associated With Reduced Mortality in Patients With Type 2 Diabetes and COVID-19: A Multicenter, Case-Control, Retrospective, Observational Study
Solerte, S. B., D’Addio, F., Trevisan, R., Lovati, E., Rossi, A., Pastore, I., Dell’Acqua, M., Ippolito, E., Scaranna, C., Bellante, R., et al. (2020) · Diabetes Care · doi:10.2337/dc20-1521 · Cited by 257
What do we know about the secretion and degradation of incretin hormones?
Deacon, C. F. (2005) · Regulatory Peptides · doi:10.1016/j.regpep.2004.06.007 · Cited by 244
Exenatide (Exendin-4) Improves Insulin Sensitivity and β-Cell Mass in Insulin-Resistant Obesefa/faZucker Rats Independent of Glycemia and Body Weight
Gedulin, B. R., Nikoulina, S. E., Smith, P. A., Gedulin, G., Nielsen, L. L., Baron, A., Parkes, D. G., & Young, A. A. (2004) · Endocrinology · doi:10.1210/en.2004-1349 · Cited by 241
Sitagliptin Exerts an Antinflammatory Action
Makdissi, A., Ghanim, H., Vora, M., Green, K., Abuaysheh, S., Chaudhuri, A., Dhindsa, S., & Dandona, P. (2012) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2012-1544 · Cited by 247
Effect of protein, fat, carbohydrate and fibre on gastrointestinal peptide release in humans
Karhunen, L. J., Juvonen, K. R., Huotari, A., Purhonen, A., & Herzig, K. (2008) · Regulatory Peptides · doi:10.1016/j.regpep.2007.10.008 · Cited by 240
Crystal structure of the incretin-bound extracellular domain of a G protein-coupled receptor
Parthier, C., Kleinschmidt, M., Neumann, P., Rudolph, R., Manhart, S., Schlenzig, D., Fanghänel, J., Rahfeld, J., Demuth, H., & Stubbs, M. T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706404104 · Cited by 236
Long-Term Treatment With the Dipeptidyl Peptidase IV Inhibitor P32/98 Causes Sustained Improvements in Glucose Tolerance, Insulin Sensitivity, Hyperinsulinemia, and β-Cell Glucose Responsiveness in VDF (fa/fa) Zucker Rats
Pospisilik, J. A., Stafford, S. G., Demuth, H.-U., Brownsey, R. W., Parkhouse, W. S., Finegood, D. T., McIntosh, C. H. S., & Pederson, R. A. (2002) · Diabetes · doi:10.2337/diabetes.51.4.943 · Cited by 232
Self-citation
Identification of osteoclast-osteoblast coupling factors in humans reveals links between bone and energy metabolism
Weivoda, M. M., Chew, C. K., Monroe, D. G., Farr, J. N., Atkinson, E. J., Geske, J. R., Eckhardt, B., Thicke, B., Ruan, M., Tweed, A. J., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-14003-6 · Cited by 230
Gastric Inhibitory Polypeptide: the neglected incretin revisited
Meier, J. J., Nauck, M. A., Schmidt, W. E., & Gallwitz, B. (2002) · Regulatory Peptides · doi:10.1016/s0167-0115(02)00039-3 · Cited by 234
Glucagon-like peptide-1: From extract to agent. The Claude Bernard Lecture, 2005
Holst, J. J. (2006) · Diabetologia · doi:10.1007/s00125-005-0107-1 · Cited by 228

Authors: Kieffer, T. J., McIntosh, C. H., & Pederson, R. A.
Affiliations: University of British Columbia (CA)
ORCID: Kieffer, T J
Venue: Endocrinology
Publisher: The Endocrine Society
Published: 1995-08
Volume: 136
Issue: 8
Pages: 3585-3596
ISSN: 0013-7227 (ISSN-L)
1945-7170
DOI: 10.1210/endo.136.8.7628397
OpenAlex: W1978953702
Cited by: 1,124
References: 36
Citations by year: 2026: 9 · 2025: 31 · 2024: 30 · 2023: 15 · 2022: 27 · 2021: 36 · 2020: 23 · 2019: 37 · 2018: 25 · 2017: 40 · 2016: 39 · 2015: 54 · 2014: 47 · 2013: 53 · 2012: 61
FWCI: 6.60
Type: journal article
Language: en
Open access: closed
Locations: Endocrinology (publishedVersion)
PubMed (publishedVersion)
Funders: Massachusetts General Hospital
Novo Nordisk
Topics: Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Peptidase Inhibition and Analysis
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
Keywords: glucose-dependent insulinotropic polypeptide, glucagon-like peptide-1, dipeptidyl peptidase IV, hormone degradation, incretin effect, N-terminal truncation, diprotin A, radiolabeled peptides, insulin secretion, circulating hormone levels
MeSH terms: Animals, Blood Physiological Phenomena, Glucagon-Like Peptides, Glucagon, Glucose, Peptide Fragments, Peptides, Protein Precursors, Rats, Inbred F344, Rats, Wistar, Dipeptidyl Peptidase 4, Rats, Glucagon-Like Peptide 1

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks