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Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV.
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.
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In the citing paper
“DPP-4 cleaves GLP-1(7-36) at the 8th position, generating GLP-1(9–36).”
From Glucagon-like peptide-1 receptor: mechanisms and advances in therapy (2024) · cites this paper as [257]
In the citing paper
“GIP and GLP-1 are both degraded very quickly by dipeptidyl peptidase 4 (DPP4) [57–59], making analogues of these endogenous hormones poor drug candidates.”
From Dual and Triple Incretin-Based Co-agonists: Novel Therapeutics for Obesity and Diabetes (2024) · cites this paper as [58]
In the citing paper
“Because GLP-1 has a short half-life of approximately 2 minutes, GLP-1 analogues with longer half-lives have been developed and are now widely used for the treatment of type 2 diabetes mellitus and obesity (41–43).”
From The glucagon-like peptide-1 (GLP-1) analogue semaglutide reduces alcohol drinking and modulates central GABA neurotransmission (2023) · cites this paper as [41]
Citations
Cites
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
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
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
Gutniak, M., Ørkov, C., Holst, J. J., Ahrén, B., & Efendić, S. (1992) · New England Journal of Medicine · doi:10.1056/nejm199205143262003 · Cited by 868
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
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
Unger, R. H. (1969) · Archives of Internal Medicine · doi:10.1001/archinte.1969.00300130043007 · Cited by 371
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Gault, V. A., O'Harte, F. P. M., Harriott, P., & Flatt, P. R. (2003) · Metabolism · doi:10.1016/s0026-0495(03)00027-1 · Cited by 17
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Koo, K. D., Kim, M. J., Kim, S.-S., Kim, K.-H., Hong, S. Y., Hur, G., Yim, H. J., Kim, G. T., Han, H. O., Kwon, O.-S., et al. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.05.046 · Cited by 17
Weber, A. E., & Thornberry, N. A. (2007) · Annual reports in medicinal chemistry · doi:10.1016/s0065-7743(07)42007-3 · Cited by 17
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Gault, V. A., Irwin, N., & Flatt, P. R. (2008) · Current Chemical Biology · doi:10.2174/187231308783334108 · Cited by 17
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Synthesis and biological evaluation of triazepane derivatives as DPP-IV inhibitors
Park, W. S., Jun, M. A., Shin, M. S., Kwon, S. W., Kang, S. K., Kim, K. Y., Rhee, S. D., Bae, M. A., Narsaiah, B., Lee, D., et al. (2009) · Journal of Fluorine Chemistry · doi:10.1016/j.jfluchem.2009.08.001 · Cited by 16
Protection of pancreatic β-cells against glucotoxicity by short-term treatment with GLP-1
Park, S.-H., Park, J., Shim, H. M., Na, A., Bae, K.-C., Lim, J.-G., & Song, D. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.02.139 · Cited by 17
Ikuma, Y., Hochigai, H., Kimura, H., Nunami, N., Kobayashi, T., Uchiyama, K., Umezome, T., Sakurai, Y., Sawada, N., Tadano, J., et al. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.12.051 · Cited by 16
Patterson, J. T., Day, J. W., Gelfanov, V. M., & DiMarchi, R. D. (2011) · Journal of Peptide Science · doi:10.1002/psc.1385 · Cited by 16
Adapting the GLP-1-Signaling System to the Treatment of Type 2 Diabetes
Salvatore, T., Carbonara, O., Cozzolino, D., Torella, R., & Sasso, F. C. (2007) · Current Diabetes Reviews · doi:10.2174/157339907779802076 · Cited by 16
Neuroendocrine Control of Food Intake
Park, S. (2007) · Journal of Korean Endocrine Society · doi:10.3803/jkes.2007.22.6.391 · Cited by 16
Bai, X., Niu, Y., Zhu, J., Yang, A.-Q., Wu, Y., & Ye, X. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.01.036 · Cited by 16
Torrecillas-Baena, B., Gálvez-Moreno, M. Á., Quesada‐Gómez, J. M., Dorado, G., & Casado‐Díaz, A. (2021) · Stem Cell Reviews and Reports · doi:10.1007/s12015-021-10285-w · Cited by 18
Glucose-Dependent Insulinotropic Polypeptide (GIP)
Wolfe, M. M., Boylan, M. O., Kieffer, T. J., & Tseng, C. (1999) · Humana Press eBooks · doi:10.1007/978-1-59259-695-9_18 · Cited by 16
Self-citationNISHII, N., Takashima, S., Iguchi, A., Murahata, Y., Matsuu, A., Hikasa, Y., & KITAGAWA, H. (2014) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2014.04.006 · Cited by 16
Nakaya, K., Kubota, N., Takamoto, I., Kubota, T., Katsuyama, H., Sato, H., Tokuyama, K., Hashimoto, S., Goto, M., Jomori, T., et al. (2013) · Metabolism · doi:10.1016/j.metabol.2013.01.010 · Cited by 16
Voutetakis, A., Cotrim, A. P., Rowzee, A. M., Zheng, C., Rathod, T., Yanık, T., Loh, Y. P., Baum, B. J., & Cawley, N. X. (2010) · Endocrinology · doi:10.1210/en.2010-0193 · Cited by 16
Non-peptidic glucose-like peptide-1 receptor agonists: aftermath of a serendipitous discovery
Wang, M., Liu, Q., & Zhou, C. (2010) · Acta Pharmacologica Sinica · doi:10.1038/aps.2010.107 · Cited by 16
Marzilli, L. A., Barry, J. P., Sells, T. B., Law, S., Vouros, P., & Harsch, A. (1999) · Journal of Mass Spectrometry · doi:10.1002/(sici)1096-9888(199904)34:4 · Cited by 19
Therapeutic Potential of Dipeptidyl Peptidase-IV Inhibitors in Patients With Diabetes Mellitus
Moore, K. B., & Saudek, C. D. (2008) · American Journal of Therapeutics · doi:10.1097/mjt.0b013e3180ed42dc · Cited by 15
Pyrazolidine Derivatives with Heteroaryl Urea as Dipeptidyl Peptidase IV Inhibitors
Ahn, J. H., Jung, S. H., Kim, J. A., Song, S. B., Kwon, S. J., Kim, K. R., Rhee, S. D., Park, S.-D., Lee, J., Kim, S. S., et al. (2005) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.53.1048 · Cited by 16
Matsuyama‐Yokono, A., Tahara, A., Nakano, R., Someya, Y., Nagase, I., Hayakawa, M., & Shibasaki, M. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.03.021 · Cited by 16
Larsen, M. O., Rolin, B., Ribel, U., Wilken, M., Deacon, C. F., Svendsen, O., Gotfredsen, C. F., & Carr, R. D. (2003) · Journal of Diabetes Research · doi:10.1155/edr.2003.93 · Cited by 17
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Yamane, S., Harada, N., & Inagaki, N. (2025) · Endocrine Journal · doi:10.1507/endocrj.ej25-0087 · Cited by 15
Kweon, S., Lee, J.-H., Yang, S.-B., Park, S. J., Subedi, L., Shim, J., Cho, S., Choi, J. U., Byun, Y., Park, J., et al. (2023) · Biomaterials Research · doi:10.1186/s40824-023-00421-7 · Cited by 15
The combination of colesevelam with sitagliptin enhances glycemic control in diabetic ZDF rat model
Shang, Q., Liu, M. K., Saumoy, M., Holst, J. J., Salen, G., & Xu, G. (2012) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00295.2011 · Cited by 15
Sun, L., Wang, C., Dai, Y., Chu, Y., Han, J. D. J., Zhou, J., Cai, X., Huang, W., & Qian, H. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.10.028 · Cited by 15
Wu, L., Zhou, M., Xie, Y., Lang, H., Li, T., Yi, L., Zhang, Q., & Mi, M. (2022) · Nutrients · doi:10.3390/nu14214583 · Cited by 15
Role and development of GLP-1 receptor agonists in the management of diabetes.
Chia, C. W., & Egan, J. M. (2009) · Europe PMC (PubMed Central) · Cited by 15
Patterson, J. T., Li, P., Day, J. W., Gelfanov, V. M., & DiMarchi, R. D. (2013) · Molecular Metabolism · doi:10.1016/j.molmet.2013.01.003 · Cited by 15
Nordhoff, S., Cerezo, S., Deppe, H., Hill, O., López-Canet, M., Rummey, C., Thiemann, M., Matassa, V. G., Edwards, P. J., & Feurer, A. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.05.109 · Cited by 15
Prasadan, K. L., Koizumi, M., Tulachan, S., Shiota, C., Lath, N. R., Paredes, J. L., Guo, P., El‐Gohary, Y., Malek, M. M., Shah, S. R., et al. (2011) · Diabetes · doi:10.2337/db09-0035 · Cited by 14
Castillo, G. M., Reichstetter, S., & Bolotin, E. M. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0542-2 · Cited by 15
Kim, H. Y., Hwang, J., Moon, M. J., & Seong, J. Y. (2014) · Endocrinology and Metabolism · doi:10.3803/enm.2014.29.3.320 · Cited by 15
Medicinal Chemistry of Glucagon-Like Peptide Receptor Agonists
Jones, L. H., & Price, D. A. (2013) · Progress in medicinal chemistry · doi:10.1016/b978-0-444-62652-3.00002-8 · Cited by 15
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Gault, V. A., Hunter, K., Irwin, N., Green, B. D., Greer, B., Harriott, P., O'Harte, F. P. M., & Flatt, P. R. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.001 · Cited by 15
Design and synthesis of new potent dipeptidyl peptidase IV inhibitors with enhanced ex vivo duration
Kondo, T., Nekado, T., Sugimoto, I., Ochi, K., Takai, S., Kinoshita, A., Tajima, Y., Yamamoto, S., Kawabata, K., Nakai, H., et al. (2007) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2007.01.041 · Cited by 15
Coumar, M. S., Chang, C., Chen, C., Chen, X., Chien, C., Tsai, T., Cheng, J., Wu, H., Han, C.-H., Wu, S., et al. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.12.019 · Cited by 15
Review: DPP IV inhibitors - current evidence and future directions
Vilsbøll, T., & Knop, F. K. (2007) · The British Journal of Diabetes · doi:10.1177/14746514070070020401 · Cited by 16
Roges, O. A., Baron, M., & Philis‐Tsimikas, A. (2005) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.14.6.705 · Cited by 15
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Woods, S. C. (2006) · Obesity · doi:10.1038/oby.2006.301 · Cited by 15
Nakamori, H., Iida, K., & Hashitani, H. (2021) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00175.2021 · Cited by 14
Abubakar, M., Nama, L., Ansari, M. M., Ansari, M. M., Bhardwaj, S., Daksh, R., Syamala, K. L. V., Jamadade, M. S., Chhabra, V., Kumar, D., et al. (2024) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266293416240515075450 · Cited by 14
Chehade, J. M., Alcalde, R., Naem, E., Mooradian, A. D., Wong, N. C. W., & Haas, M. J. (2012) · Metabolism · doi:10.1016/j.metabol.2012.07.005 · Cited by 15
Liang, J. B., Leung, K. K., Lam, S. Y., & Leung, P. S. (2012) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2012.01612.x · Cited by 14
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Lee, C. Y. (2015) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.12524 · Cited by 14
Luo, X., Pan, L., Nie, A., Wang, Q., Gu, Y., Li, F., Zhang, H., Li, W., & Li, X. (2013) · Journal of Diabetes · doi:10.1111/1753-0407.12061 · Cited by 14
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Kim, M., & Lee, M. (2010) · Korean Diabetes Journal · doi:10.4093/kdj.2010.34.1.2 · Cited by 14
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Wallner, M., Eaton, D., von Lewinski, D., & Sourij, H. (2018) · Current Diabetes Reports · doi:10.1007/s11892-018-1116-z · Cited by 14
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Asakawa, T., Moritoh, Y., Kataoka, O., Suzuki, N., Takeuchi, K., & Odaka, H. (2009) · Life Sciences · doi:10.1016/j.lfs.2009.04.024 · Cited by 14
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Salem, V., & Bloom, S. R. (2009) · Expert Review of Clinical Pharmacology · doi:10.1586/ecp.09.54 · Cited by 15
Li, Y., Cui, T., Kong, X., Yi, X., Kong, D., Zhang, J., Liu, C., & Gong, M. (2018) · The FASEB Journal · doi:10.1096/fj.201701033rrr · Cited by 14
Exenatide: Its position in the treatment of type 2 diabetes
Guerci, B., & Martin, C. S. (2008) · Annales d Endocrinologie · doi:10.1016/j.ando.2008.03.004 · Cited by 14
Recent Advances in the Development of Agents for the Treatment of Type 2 Diabetes
Cobb, J. E., & Dukes, I. D. (1998) · Annual reports in medicinal chemistry · doi:10.1016/s0065-7743(08)61086-6 · Cited by 14
Hinke, S. A., Lynn, F. C., Ehses, J. A., Pamir, N., Manhart, S., Kühn‐Wache, K., Rosche, F., Demuth, H.-U., Pederson, R. A., & McIntosh, C. H. S. (2005) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-47920-6_35 · Cited by 14
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Riedel, M. J., & Kieffer, T. J. (2010) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2010.532786 · Cited by 13
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Ludvigsson, J. (2013) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.2014.855197 · Cited by 13
Ma, J., & Vella, A. V. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00324 · Cited by 14
Wang, S., Su, M., Wang, J., Li, Z., Zhang, L. J., Ji, X., Li, J., Li, J., & Liu, H. S. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.09.051 · Cited by 13
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Raman, V. S., & Heptulla, R. A. (2009) · Pediatric Research · doi:10.1203/pdr.0b013e3181975ee4 · Cited by 13
Troutt, J. S., Siegel, R. W., Chen, J., Sloan, J. H., Deeg, M. A., Cao, G., & Konrad, R. J. (2011) · Clinical Chemistry · doi:10.1373/clinchem.2010.159954 · Cited by 13
Forest, T. W., Holder, D., Smith, A., Cunningham, C., Yao, X., Dey, M., Frederick, C. B., & Prahalada, S. R. (2014) · Endocrinology · doi:10.1210/en.2013-1781 · Cited by 13
Aziz, A. A., Anderson, G. H., Giacca, A., & Cho, F. (2005) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00850.2004 · Cited by 12
Biology and therapeutic potential of GLP-1 in the treatment of diabetes
Chia, C. W., & Egan, J. M. (2005) · Drug Discovery Today Disease Mechanisms · doi:10.1016/j.ddmec.2005.08.013 · Cited by 13
Someya, Y., Tahara, A., Nakano, R., Matsuyama‐Yokono, A., Nagase, I., Fukunaga, Y., Takasu, T., Hayakawa, M., & Shibasaki, M. (2008) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-008-0277-8 · Cited by 13
Nutrient regulation of pancreatic β-cell function in diabetes: problems and potential solutions
Flatt, P. R., & Green, B. D. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340774 · Cited by 13
Ruggles, J. A., Kelemen, D. W., & Baron, A. (2004) · Endocrinology and Metabolism Clinics of North America · doi:10.1016/s0889-8529(03)00098-7 · Cited by 12
Lu, C., Xu, C., & Yang, J. (2024) · Medicina · doi:10.3390/medicina61010017 · Cited by 14
Zargar, A. A., Mehta, V., Huddar, V., Gupta, R., Bhandari, K., Posa, M. K., Ramya, T. S., Snigdha, D., Vijayakumar, B., Sharma, M. C., et al. (2025) · Current Proteomics · doi:10.1016/j.curpro.2025.100014 · Cited by 15
Molecular Basis of cAMP Signaling in Pancreatic β Cells
Holz, G. G., Chepurny, O. G., Leech, C. A., Song, W., & Hussain, M. A. (2014) · Springer eBooks · doi:10.1007/978-94-007-6686-0_25 · Cited by 11
Obesity–An Update on the Basic Pathophysiology and Review of Recent Therapeutic Advances
Gjermeni, E., Kirstein, A., Kolbig, F., Kirchhof, M., Bundalian, L., Katzmann, J. L., Laufs, U., Blüher, M., Garten, A., & Duc, D. L. (2021) · Biomolecules · doi:10.3390/biom11101426 · Cited by 127
Kamoi, K., Shinozaki, Y., Furukawa, K., & Sasaki, H. (2011) · Endocrine Journal · doi:10.1507/endocrj.k11e-125 · Cited by 12
Active glucagon-like peptide-1 (GLP-1): Storage of human plasma and stability over time
Marino, L. D., Griffo, E., Maione, S., & Mirabella, M. (2011) · Clinica Chimica Acta · doi:10.1016/j.cca.2011.05.011 · Cited by 12
Das, A., Geetha, K. M., & Hazarika, I. (2019) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-019-09927-y · Cited by 12
Esser, N., Mongovin, S. M., Parilla, J. H., Barrow, B. M., Mundinger, T. O., Fountaine, B. S., Larmore, M. J., Castillo, J., Akter, R., Hull, R. L., et al. (2022) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00234.2021 · Cited by 12
Ismaeil, A., Babiker, F. A., & Al‐Sabah, S. (2022) · Pharmaceuticals · doi:10.3390/ph15060720 · Cited by 12
Sun, L., Dai, Y., Wang, C., Chu, Y., Su, X., Yang, J., Zhou, J., Huang, W., & Qian, H. (2015) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12615 · Cited by 12
Genetic Variation in the GCG and in the GLP1R Genes and Antipsychotic-Induced Weight Gain
Brandl, E. J., Tiwari, A. K., Chowdhury, N. I., Zai, C. C. H., Lieberman, J. A., Meltzer, H. Y., Kennedy, J. L., & Müller, D. J. (2014) · Pharmacogenomics · doi:10.2217/pgs.13.247 · Cited by 12
Kamoi, K., Ohara, N., Ikarashi, T., Shinozaki, Y., & Furukawa, K. (2011) · Journal of Diabetes & Metabolism · doi:10.4172/2155-6156.1000147 · Cited by 12
Xu, F., Wang, K. Y., Wang, N., Li, G., & Liu, D. (2017) · PLoS ONE · doi:10.1371/journal.pone.0181939 · Cited by 12
Incretins: B eyond type 2 diabetes
Dandona, P., Ghanim, H., & Chaudhuri, A. (2018) · Diabetes Obesity and Metabolism · doi:10.1111/dom.13153 · Cited by 13
Lv, J., Pan, Y., Li, X., Cheng, D., Liu, S., Shi, H., & Zhang, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096833 · Cited by 12
Kim, H. J., Kwak, W. Y., Min, J. P., Sung, S. Y., Kim, H. D., Kim, M.-K., Kim, H. S., Park, K. J., Son, M. H., Kim, S. H., et al. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.07.019 · Cited by 12
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Metadata
- 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
- 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
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