Apelin is a novel islet peptide.
(2010) In Regulatory Peptides 162. p.44-51- Abstract
- Apelin, a recently discovered peptide with wide tissue distribution, regulates feeding behavior, improves glucose utilization, and inhibits insulin secretion. We examined whether apelin is expressed in human islets, as well as in normal and type 2 diabetic (T2D) animal islets. Further, we studied islet apelin regulation and the effect of apelin on insulin secretion. Apelin expression and regulation was examined in human and animal specimens using immunocytochemistry, in situ hybridization, and real-time PCR. Insulin secretion was studied in INS-1 (832/13) clonal beta cells. APJ-receptor expression was studied using real-time PCR. In human and murine islets apelin was predominantly expressed in beta cells and alpha cells; a subpopulation of... (More)
- Apelin, a recently discovered peptide with wide tissue distribution, regulates feeding behavior, improves glucose utilization, and inhibits insulin secretion. We examined whether apelin is expressed in human islets, as well as in normal and type 2 diabetic (T2D) animal islets. Further, we studied islet apelin regulation and the effect of apelin on insulin secretion. Apelin expression and regulation was examined in human and animal specimens using immunocytochemistry, in situ hybridization, and real-time PCR. Insulin secretion was studied in INS-1 (832/13) clonal beta cells. APJ-receptor expression was studied using real-time PCR. In human and murine islets apelin was predominantly expressed in beta cells and alpha cells; a subpopulation of the PP cells in human islets also harbored apelin. In porcine and feline islets apelin was mainly expressed in beta cells. APJ-receptor expression was detected in INS-1 (832/13) cells, and in human and mouse islets. A high dose (1microM) of apelin-36 caused a moderate increase in glucose-stimulated insulin secretion (30%; p<0.001), while lower concentrations (10-100nM) of apelin robustly reduced insulin secretion by 50% (p<0.001). Apelin was upregulated in beta cells of T2D db/db mice (47% vs. controls; p<0.02) and GK-rats (74% vs. controls; p<0.002), but human islet apelin expression was unaffected by glucose. On the other hand, human islet apelin expression was diminished after culture in glucocorticoids (16% vs. controls; p<0.01). We conclude that apelin is a novel insulin-regulating islet peptide in humans and several laboratory animals. Islet apelin expression is negatively regulated by glucocorticoids, and upregulated in T2D animals. The presence of apelin receptors in islets suggests a role for apelin as a paracrine or autocrine messenger within the islets. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1581556
- author
- Ringström, Camilla ; Dekker Nitert, Marloes LU ; Bennet, Hedvig LU ; Fex, Malin LU ; Valet, Philippe ; Rehfeld, Jens F ; Friis-Hansen, Lennart and Wierup, Nils LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Regulatory Peptides
- volume
- 162
- pages
- 44 - 51
- publisher
- Elsevier
- external identifiers
-
- wos:000278663300007
- pmid:20346374
- scopus:77952669438
- pmid:20346374
- ISSN
- 1873-1686
- DOI
- 10.1016/j.regpep.2010.03.005
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Neuroendocrine Cell Biology (013212008), Diabetes and Celiac Unit (013241540), Diabetes and Endocrinology (013241530)
- id
- a09cb4af-77f1-4feb-9294-96feccb52f0a (old id 1581556)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/20346374?dopt=Abstract
- date added to LUP
- 2016-04-04 08:55:35
- date last changed
- 2024-01-27 06:50:56
@article{a09cb4af-77f1-4feb-9294-96feccb52f0a,
abstract = {{Apelin, a recently discovered peptide with wide tissue distribution, regulates feeding behavior, improves glucose utilization, and inhibits insulin secretion. We examined whether apelin is expressed in human islets, as well as in normal and type 2 diabetic (T2D) animal islets. Further, we studied islet apelin regulation and the effect of apelin on insulin secretion. Apelin expression and regulation was examined in human and animal specimens using immunocytochemistry, in situ hybridization, and real-time PCR. Insulin secretion was studied in INS-1 (832/13) clonal beta cells. APJ-receptor expression was studied using real-time PCR. In human and murine islets apelin was predominantly expressed in beta cells and alpha cells; a subpopulation of the PP cells in human islets also harbored apelin. In porcine and feline islets apelin was mainly expressed in beta cells. APJ-receptor expression was detected in INS-1 (832/13) cells, and in human and mouse islets. A high dose (1microM) of apelin-36 caused a moderate increase in glucose-stimulated insulin secretion (30%; p<0.001), while lower concentrations (10-100nM) of apelin robustly reduced insulin secretion by 50% (p<0.001). Apelin was upregulated in beta cells of T2D db/db mice (47% vs. controls; p<0.02) and GK-rats (74% vs. controls; p<0.002), but human islet apelin expression was unaffected by glucose. On the other hand, human islet apelin expression was diminished after culture in glucocorticoids (16% vs. controls; p<0.01). We conclude that apelin is a novel insulin-regulating islet peptide in humans and several laboratory animals. Islet apelin expression is negatively regulated by glucocorticoids, and upregulated in T2D animals. The presence of apelin receptors in islets suggests a role for apelin as a paracrine or autocrine messenger within the islets.}},
author = {{Ringström, Camilla and Dekker Nitert, Marloes and Bennet, Hedvig and Fex, Malin and Valet, Philippe and Rehfeld, Jens F and Friis-Hansen, Lennart and Wierup, Nils}},
issn = {{1873-1686}},
language = {{eng}},
pages = {{44--51}},
publisher = {{Elsevier}},
series = {{Regulatory Peptides}},
title = {{Apelin is a novel islet peptide.}},
url = {{https://lup.lub.lu.se/search/files/5211599/1636374.pdf}},
doi = {{10.1016/j.regpep.2010.03.005}},
volume = {{162}},
year = {{2010}},
}