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Updated: Dec 30, 2025

Detection of G Protein-coupled Receptor Expression in Mouse Vagal Afferent Neurons using Multiplex In Situ Hybridization
Published on: September 20, 2021
Differences in the expression of catecholamine-synthesizing enzymes between vesicular monoamine transporter 1- and
Kouki Kato1, Takuya Yokoyama2, Tatsumi Kusakabe3
1Center for Laboratory Animal Science, National Defense Medical College, 3-2 Namiki, Tokorozawa, Saitama 359-8513, Japan.
Abstract:
Vesicular monoamine transporters (VMAT) 1 and 2 are responsible for monoamine transportation into secretary vesicles and are tissue-specifically expressed in central and peripheral monoaminergic tissues, including the carotid body (CB). The aim of the present study was to examine the expression of catecholamine-synthesizing enzymes in VMAT1- and VMAT2-immunoreactive glomus cells in the rat CB using multiple immunolabeling. The expression of VMAT1 and VMAT2 mRNA in the CB was confirmed by RT-PCR. Immunohistochemistry revealed that VMAT1 immunoreactivity was predominant in glomus cells rather than VMAT2 immunoreactivity. Glomus cells with VMAT1 immunoreactivity exhibited weak/negative VMAT2 immunoreactivity, and vice versa. Immunoreactivities for VMAT1 and tyrosine hydroxylase, the rate-limiting enzyme for catecholamine biosynthesis, were co-localized in the same glomus cells and a positive correlation was confirmed between the two immunoreactivities (Spearman's coefficient = 0.82; p < 0.05). Although some glomus cells showed co-localization of VMAT2 and dopamine β-hydroxylase immunoreactivity, the biosynthetic enzyme for noradrenaline, VMAT2 immunoreactivity appeared to be less associated with both catecholamine-synthesizing enzymes as indicated by a correlation analysis (TH: Spearman's coefficient = 0.38, DBH: Spearman's coefficient = 0.26). These results indicate that heterogeneity on functional role would exist among glomus cells in terms of VMAT isoform and catecholamine-synthesizing enzymes expression.
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