Analysis of the expression and distribution of protein O-linked mannose β1,2- N -acetylglucosaminyltransferase 1 in the normal adult mouse brain

Protein O-linked mannose β1,2- -acetylglucosaminyltransferase 1 (POMGNT1) is crucial for the elongation of O-mannosyl glycans. Mutations in POMGNT1 cause muscle-eye-brain (MEB) disease, one of the main features of which is anatomical aberrations in the brain. A growing number of studies have shown t...

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Published in:Frontiers in neuroanatomy Vol. 16; p. 1043924
Main Authors: Jiang, Hanxiao, Feng, Yuxue, He, Guiqiong, Liu, Yuanjie, Li, Xiaofeng
Format: Journal Article
Language:English
Published: Switzerland Frontiers Research Foundation 06-01-2023
Frontiers Media S.A
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Summary:Protein O-linked mannose β1,2- -acetylglucosaminyltransferase 1 (POMGNT1) is crucial for the elongation of O-mannosyl glycans. Mutations in POMGNT1 cause muscle-eye-brain (MEB) disease, one of the main features of which is anatomical aberrations in the brain. A growing number of studies have shown that defects in POMGNT1 affect neuronal migration and distribution, disrupt basement membranes, and misalign Cajal-Retzius cells. Several studies have examined the distribution and expression of POMGNT1 in the fetal or neonatal brain for neurodevelopmental studies in the mouse or human brain. However, little is known about the neuroanatomical distribution and expression of POMGNT1 in the normal adult mouse brain. We analyzed the expression of POMGNT1 mRNA and protein in the brains of various neuroanatomical regions and spinal cords by western blotting and RT-qPCR. We also detected the distribution profile of POMGnT1 in normal adult mouse brains by immunohistochemistry and double-immunofluorescence. In the present study, we found that POMGNT1-positive cells were widely distributed in various regions of the brain, with high levels of expression in the cerebral cortex and hippocampus. In terms of cell type, POMGNT1 was predominantly expressed in neurons and was mainly enriched in glutamatergic neurons; to a lesser extent, it was expressed in glial cells. At the subcellular level, POMGNT1 was mainly co-localized with the Golgi apparatus, but expression in the endoplasmic reticulum and mitochondria could not be excluded. The present study suggests that POMGNT1, although widely expressed in various brain regions, may has some regional and cellular specificity, and the outcomes of this study provide a new laboratory basis for revealing the possible involvement of POMGNT1 in normal physiological functions of the brain from a morphological perspective.
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Reviewed by: Botond Gaal, University of Debrecen, Hungary; Patricia Franzka, University Hospital Jena, Germany
Edited by: Zoltan Rusznak, Australian Catholic University, Australia
ISSN:1662-5129
1662-5129
DOI:10.3389/fnana.2022.1043924