Glucagon-like peptide-2 mobilization of intestinal lipid does not require canonical enterocyte chylomicron synthetic machinery.


Journal

Biochimica et biophysica acta. Molecular and cell biology of lipids
ISSN: 1879-2618
Titre abrégé: Biochim Biophys Acta Mol Cell Biol Lipids
Pays: Netherlands
ID NLM: 101731727

Informations de publication

Date de publication:
09 2022
Historique:
received: 16 03 2022
revised: 25 05 2022
accepted: 31 05 2022
pubmed: 10 6 2022
medline: 14 7 2022
entrez: 9 6 2022
Statut: ppublish

Résumé

Dietary triglycerides (TG) retained in the intestine after a meal can be mobilized many hours later by glucagon-like peptide-2 (GLP-2) in humans and animal models, despite the well-documented absence of expression of the GLP-2 receptor on enterocytes. In this study, we examined the site of GLP-2 action to mobilize intestinal lipids and enhance chylomicron production. In mesenteric lymph duct-cannulated rats, we assessed GLP-2-stimulated lymph flow rate, TG concentration, TG output, and apoB48 abundance 5 h after an intraduodenal lipid bolus, in the presence of a validated GLP-2 antagonist or vehicle. Additionally, the same GLP-2-stimulated parameters were examined in the presence or absence of cis-Golgi disruption by Brefeldin A (BFA). Compared to placebo, GLP-2 administration increased lymph flow by 2.8-fold (P < 0.001), cumulative lymph volume by 2.69-fold (P < 0.001) and total TG output 2-fold (P = 0.015). GLP-2 receptor antagonism markedly diminished GLP-2's ability to stimulate lymph flow, cumulative lymph volume and total TG output, demonstrating the dependence of GLP-2 stimulation of lymph flow and TG output on its receptor activation. In contrast, disruption of the cis-Golgi apparatus with Brefeldin A did not diminish the GLP-2-response of lymph flow i.e., increased lymph flow by 2.7-fold (P = 0.001), lymph volume by 2.9-fold (P = 0.001), and total TG output i.e., increased by 2.5-fold (P = 0.003). GLP-2 mobilizes enteral lipid at a site distal to the Golgi, acting via its receptor. Since GLP-2 receptors are not expressed on enterocytes, GLP-2 likely mobilizes intestinal lipid residing extracellularly, either in the lamina propria or in the lymphatics.

Sections du résumé

BACKGROUND & AIMS
Dietary triglycerides (TG) retained in the intestine after a meal can be mobilized many hours later by glucagon-like peptide-2 (GLP-2) in humans and animal models, despite the well-documented absence of expression of the GLP-2 receptor on enterocytes. In this study, we examined the site of GLP-2 action to mobilize intestinal lipids and enhance chylomicron production.
METHODS
In mesenteric lymph duct-cannulated rats, we assessed GLP-2-stimulated lymph flow rate, TG concentration, TG output, and apoB48 abundance 5 h after an intraduodenal lipid bolus, in the presence of a validated GLP-2 antagonist or vehicle. Additionally, the same GLP-2-stimulated parameters were examined in the presence or absence of cis-Golgi disruption by Brefeldin A (BFA).
RESULTS
Compared to placebo, GLP-2 administration increased lymph flow by 2.8-fold (P < 0.001), cumulative lymph volume by 2.69-fold (P < 0.001) and total TG output 2-fold (P = 0.015). GLP-2 receptor antagonism markedly diminished GLP-2's ability to stimulate lymph flow, cumulative lymph volume and total TG output, demonstrating the dependence of GLP-2 stimulation of lymph flow and TG output on its receptor activation. In contrast, disruption of the cis-Golgi apparatus with Brefeldin A did not diminish the GLP-2-response of lymph flow i.e., increased lymph flow by 2.7-fold (P = 0.001), lymph volume by 2.9-fold (P = 0.001), and total TG output i.e., increased by 2.5-fold (P = 0.003).
CONCLUSIONS
GLP-2 mobilizes enteral lipid at a site distal to the Golgi, acting via its receptor. Since GLP-2 receptors are not expressed on enterocytes, GLP-2 likely mobilizes intestinal lipid residing extracellularly, either in the lamina propria or in the lymphatics.

Identifiants

pubmed: 35680083
pii: S1388-1981(22)00084-1
doi: 10.1016/j.bbalip.2022.159194
pii:
doi:

Substances chimiques

Chylomicrons 0
Glucagon-Like Peptide 2 0
Glucagon-Like Peptide-2 Receptor 0
Triglycerides 0
Brefeldin A 20350-15-6

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

159194

Subventions

Organisme : CIHR
ID : PJT-153301
Pays : Canada

Informations de copyright

Copyright © 2022 Elsevier B.V. All rights reserved.

Auteurs

Majid M Syed-Abdul (MM)

Departments of Medicine and Physiology and Banting and Best Diabetes Centre, University of Toronto, Toronto, ON, Canada.

Priska Stahel (P)

Departments of Medicine and Physiology and Banting and Best Diabetes Centre, University of Toronto, Toronto, ON, Canada.

Lili Tian (L)

Departments of Medicine and Physiology and Banting and Best Diabetes Centre, University of Toronto, Toronto, ON, Canada.

Changting Xiao (C)

Department of Anatomy, Physiology and Pharmacology, College of Medicine, University of Saskatchewan, Saskatoon, SK, Canada.

Avital Nahmias (A)

Maccabi Healthcare Services, Endocrinology Division, Tel Aviv, Israel.

Gary F Lewis (GF)

Departments of Medicine and Physiology and Banting and Best Diabetes Centre, University of Toronto, Toronto, ON, Canada. Electronic address: gary.lewis@uhn.ca.

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Classifications MeSH