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On the Physiology of GIP and GLP-1
Abstract
Recent studies have indicated that GIP and GLP-1 are about as important as each other in the incretin effect, being released rapidly after meals and being active already at fasting glucose levels. Although the density of GLP-1 producing cells is higher distally, GlP-1 is normally secreted by jejunal L-cells, explaining the rapid onset of secretion. Moreover, many endocrine cells in the small intestine appear to produce both GIP and GLP-1. Both are metabolized rapidly by the dipeptidyl peptidase IV enzyme, but unlike GIP, about 90 % of GLP-1 is degraded before it reaches the systemic circulation. Apparently, before it is degraded, GLP-1 activates sensory afferents in the gastrointestinal mucosa with cell bodies in the nodose ganglion, signaling onwards to the brain stem and the hypothalamus. A similar mechanism seems to be involved in GLP-1's effect on gastrointestinal motility and secretion, and perhaps its actions on appetite and food intake, all of which may be even more physiologically important than its effects on the beta cells. Cardiovascular and neuroprotective actions of GLP-1 have also recently been reported. Regarding GIP, several lines of evidence suggest that GIP, in addition to its incretin effects, may affect lipid metabolism and promote lipid storage.
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“These signals include release of the gut peptides glucosedependent insulinotropic polypeptide (GIP) from K-cells located in the proximal intestine and glucagon-like peptide-1 and 2 (GLP-1, GLP-2) from L-cells located in more distal regions of the intestine (5,6)”
From Gut mechanisms linking intestinal sweet sensing to glycemic control (2018) · cites this paper as [6]
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“Incretins are gastrointestinal hormones secreted by specific enteroendocrine cells in the gastric mucosa in response to food intake [7].”
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“glucagon-like peptide 1 (GLP-1), secreted from the intestinal K- and L-cells, respectively, play an important role in this process, as they both stimulate insulin secretion, and GLP-1 suppresses appetite and slows gastric emptying [5].”
BackgroundSelf-citationMaino, B., Ciotti, M. T., Calissano, P., & Cavallaro, S. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15045596 · Cited by 41
“secretion, Gip is known to exert a range of pleiotropic and extra-pancreatic actions [20–30].”
BackgroundGut mechanisms linking intestinal sweet sensing to glycemic control
Kreuch, D., Keating, D. J., Wu, T., Horowitz, M., Rayner, C. K., & Young, R. L. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00741 · Cited by 40
“These signals include release of the gut peptides glucosedependent insulinotropic polypeptide (GIP) from K-cells located in the proximal intestine and glucagon-like peptide-1 and 2 (GLP-1, GLP-2) from L-cells located in more distal regions of the intestine (5, 6), and release of the bioamine serotonin (5HT) from enter…”
BackgroundHolst, J. J., & McGill, M. A. (2011) · Clinical Drug Investigation · doi:10.2165/11595370-000000000-00000 · Cited by 40
Self-citationArtificial sweeteners and their implications in diabetes: a review
Angelin, M., Kumar, J., Vajravelu, L. K., Satheesan, A., Chaithanya, V., & Murugesan, R. (2024) · Frontiers in Nutrition · doi:10.3389/fnut.2024.1411560 · Cited by 48
Removal of Duodenum Elicits GLP-1 Secretion
Muscogiuri, G., Mezza, T., Prioletta, A., Sorice, G. P., Clemente, G., Sarno, G., Nuzzo, G., Pontecorvi, A., Holst, J. J., & Giaccari, A. (2013) · Diabetes Care · doi:10.2337/dc12-0811 · Cited by 38
“89390, reacting equally with intact GLP-1 (7-36)amide and its primary NH2-terminally truncated metabolite GLP-1(9-36) amide (14).”
BackgroundSelf-citationCampbell, R. K. (2006) · Annals of Pharmacotherapy · doi:10.1345/aph.1h459 · Cited by 39
Pancreatic Blood Flow with Special Emphasis on Blood Perfusion of the Islets of Langerhans
Jansson, L. E., & Carlsson, P. (2019) · Comprehensive physiology · doi:10.1002/cphy.c160050 · Cited by 45
Moritoh, Y., Takeuchi, K., Asakawa, T., Kataoka, O., & Odaka, H. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.11.017 · Cited by 37
“GLP-1 and GIP are secreted from gut L- and K-cells in response to meal ingestion and serve as potent prandial stimulators of insulin secretion thereby playing a major role in glucose homeostasis (Holst, 2004).”
BackgroundGIP-induced vasodilation in human adipose tissue involves capillary recruitment
Asmar, M., Asmar, A., Simonsen, L., Dela, F., Holst, J. J., & Bülow, J. (2019) · Endocrine Connections · doi:10.1530/ec-19-0144 · Cited by 37
Self-citationA Comparative Perspective on Wnt/β-Catenin Signalling in Cell Fate Determination
Garcin, C. L., & Habib, S. J. (2017) · Results and problems in cell differentiation · doi:10.1007/978-3-319-53150-2_15 · Cited by 40
Moving beyond energy homeostasis: New roles for glucagon-like peptide-1 in food and drug reward
Reddy, I. A., Stanwood, G. D., & Galli, A. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.10.003 · Cited by 36
“Thus, earlier research focused on the effects of GLP-1 on the hypothalamus and brainstem, regions highly involved in homeostatic metabolic control (Baggio and Drucker, 2007; Holst, 2004).”
Mechanisms of Weight Loss after Gastric Bypass and Gastric Banding
Bueter, M., Ashrafian, H., & le Roux, C. W. (2009) · Obesity Facts · doi:10.1159/000232383 · Cited by 35
Exenatide can reduce glucose independent of islet hormones or gastric emptying
Ionut, V., Zheng, D., Stefanovski, D., & Bergman, R. N. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90222.2008 · Cited by 35
GLP-1 antagonism with exendin (9–39) fails to increase spontaneous meal size in rats
Rüttimann, E. B., Arnold, M., Geary, N., & Langhans, W. (2010) · Physiology & Behavior · doi:10.1016/j.physbeh.2010.02.022 · Cited by 34
Usinger, L., Hansen, K. B., Kristiansen, V. B., Larsen, S., Holst, J. J., & Knop, F. K. (2011) · Obesity Surgery · doi:10.1007/s11695-011-0362-9 · Cited by 33
“Another major determinant of the post OGTT plasma glucose profiles is the secretion of the incretin hormones glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1) affecting both insulin and glucagon secretion from the pancreas [11].”
BackgroundSelf-citationMathieu, C., & Bollaerts, K. (2007) · International Journal of Clinical Practice · doi:10.1111/j.1742-1241.2007.01437.x · Cited by 32
GIP-Dependent Expression of Hypothalamic Genes
Ambati, S., DUAN, J., Hartzell, D. L., Choi, Y., Della‐Fera, M. A., & Baile, C. A. (2011) · Physiological Research · doi:10.33549/physiolres.932151 · Cited by 31
“GIP regulates lipid metabolism and storage (Holst 2004) partly through its effect on insulin secretion https://doi.org/10.33549/physiolres.932151 942 Ambati et al. Vol. 60 and the resulting increased uptake and incorporation of glucose into lipids, as well as through direct effects in adipose…”
BackgroundInfluentialWren, A. (2008) · KARGER eBooks · doi:10.1159/000115364 · Cited by 30
Badole, S. L., Bagul, P. P., Mahamuni, S. P., Khose, R. D., Joshi, A. C., Jangam, G. B., Ghule, A. E., Raut, C. G., Khedkar, V. M., & Coutinho, E. C. (2013) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2013.02.006 · Cited by 29
Diabetes After Pancreatic Surgery: Novel Issues
Scavini, M., Dugnani, E., Pasquale, V., Liberati, D., Aleotti, F., Terlizzi, G. D., Petrella, G., Balzano, G., & Piemonti, L. (2015) · Current Diabetes Reports · doi:10.1007/s11892-015-0589-2 · Cited by 29
A role for Glucagon-Like Peptide-1 in the regulation of β-cell autophagy
Arden, C. (2018) · Peptides · doi:10.1016/j.peptides.2017.12.002 · Cited by 28
“Glucagon-Like Peptide-1 (GLP-1) is released from intestinal L-cells in response to food intake and acts on multiple tissues to lower blood glucose [60].”
BackgroundGejl, M., Rungby, J., Brock, B., & GJEDDE, A. H. (2014) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.12240 · Cited by 28
Stem cells and diabetes treatment
MADSEN, O. D. (2005) · Apmis · doi:10.1111/j.1600-0463.2005.apm_418.x · Cited by 27
The bile–gut axis and metabolic consequences of cholecystectomy
Lange, A. H., Pedersen, M. G., Ellegaard, A., Nerild, H. H., Brønden, A., Sonne, D. P., & Knop, F. K. (2024) · European Journal of Endocrinology · doi:10.1093/ejendo/lvae034 · Cited by 29
Metadata
- Authors
- Holst, J. J.
- Affiliations
- University of Copenhagen (DK)
- Corresponding author
- Holst, J. J.
- ORCID
- Holst, J. J.
- Venue
- Hormone and Metabolic Research
- Publisher
- Georg Thieme Verlag KG
- Published
- 2004-11
- Volume
- 36
- Issue
- 11/12
- Pages
- 747-754
- ISSN
- 0018-5043 (ISSN-L)
- 1439-4286
- OpenAlex
- W2074835704
- Cited by
- 189
- References
- 0
- Citations by year
- 2026: 1 · 2025: 7 · 2024: 7 · 2023: 2 · 2022: 2 · 2021: 5 · 2020: 7 · 2019: 8 · 2018: 7 · 2017: 6 · 2016: 5 · 2015: 11 · 2014: 16 · 2013: 14 · 2012: 11
- FWCI
- 7.23
- Type
- journal article
- Language
- de
- Open access
- closed
- Locations
- Hormone and Metabolic Research (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Regulation of Appetite and Obesity
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
- Keywords
- glucagon-like peptide-1, glucose-dependent insulinotropic polypeptide, incretin effect, dipeptidyl peptidase IV, GLP-1 receptor, nodose ganglion, gastrointestinal motility, beta-cell function, cardiovascular effects, neuroprotection, lipid metabolism, fat deposition
- MeSH terms
- Animals, Appetite, Cardiovascular System, Gastric Inhibitory Polypeptide, Gastrointestinal Motility, Glucagon, Humans, Intestine, Small, Jejunum, Neurosecretory Systems, Peptide Fragments, Protein Precursors, Mice, Knockout, Mice, Glucagon-Like Peptide 1
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