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

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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.

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

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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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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

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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

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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.

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