Choline-acetyltransferase (ChAT) and acetylcholinesterase (AChE) in the human infant dorsal motor nucleus of the Vagus (DMNV), and alterations according to sudden infant death syndrome (SIDS) category.


Journal

Neurobiology of disease
ISSN: 1095-953X
Titre abrégé: Neurobiol Dis
Pays: United States
ID NLM: 9500169

Informations de publication

Date de publication:
Nov 2023
Historique:
received: 31 05 2023
revised: 18 09 2023
accepted: 06 10 2023
medline: 21 11 2023
pubmed: 10 10 2023
entrez: 9 10 2023
Statut: ppublish

Résumé

Amongst other molecules, the cholinergic system consists of choline-acetyltransferase (ChAT, - synthesis enzyme), acetylcholinesterase (AChE - primary hydrolysis enzyme), and butyrylcholinesterase (BuChE - secondary hydrolysis enzyme). In the brainstem, the Dorsal Motor Nucleus of The Vagus (DMNV) has high cholinergic expression and is a region of interest in the neuropathology of sudden infant death syndrome (SIDS). SIDS is the unexpected death of a seemingly healthy infant, but postmortem brainstem abnormalities suggesting altered cholinergic regulation have been found. This study aimed to determine the percentage of positive ChAT and AChE neurons within the infant DMNV through immunohistochemistry at the three levels of the brainstem medulla (caudal, intermediate, and rostral), to investigate whether the proportion of neurons positive for these enzymes differs amongst the diagnostic subgroups of SIDS compared to those with an explained cause of Sudden unexpected death in infancy (eSUDI), and whether there were any associations with SIDS risk factors (male gender, cigarette smoke exposure, co-sleeping/bed sharing, and prone sleeping). Results showed that ChAT-positive neurons were lower in the rostral DMNV in the SIDS II cohort, and within the caudal and intermediate DMNV of infants who were exposed to cigarette smoke. These findings suggest altered cholinergic regulation in the brainstem of SIDS infants, with potential contribution of cigarette smoke exposure, presumably via the nicotinic acetylcholinergic receptor system.

Identifiants

pubmed: 37813167
pii: S0969-9961(23)00335-2
doi: 10.1016/j.nbd.2023.106319
pii:
doi:

Substances chimiques

Acetylcholinesterase EC 3.1.1.7
Butyrylcholinesterase EC 3.1.1.8
Choline N91BDP6H0X
Choline O-Acetyltransferase EC 2.3.1.6
Cholinergic Agents 0
ACHE protein, human EC 3.1.1.7

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

106319

Informations de copyright

Copyright © 2023. Published by Elsevier Inc.

Auteurs

Masarra Joda (M)

Discipline of Medicine, Faculty of Medicine and Health, The University of Sydney, NSW 2006, Australia.

Karen A Waters (KA)

Discipline of Medicine, Faculty of Medicine and Health, The University of Sydney, NSW 2006, Australia; Discipline of Child and Adolescent Health, Children's Hospital at Westmead Clinical School, Faculty of Medicine and Health, The University of Sydney, NSW 2006, Australia.

Rita Machaalani (R)

Discipline of Medicine, Faculty of Medicine and Health, The University of Sydney, NSW 2006, Australia; Discipline of Child and Adolescent Health, Children's Hospital at Westmead Clinical School, Faculty of Medicine and Health, The University of Sydney, NSW 2006, Australia. Electronic address: rita.machaalani@sydney.edu.au.

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Classifications MeSH