Muscarinic acetylcholine receptors in macaque V1 are most frequently expressed by parvalbumin‐immunoreactive neurons
Open accessAbstract
Acetylcholine (ACh) is believed to underlie mechanisms of arousal and attention in mammals. ACh also has a demonstrated functional effect in visual cortex that is both diverse and profound. We have reported previously that cholinergic modulation in V1 of the macaque monkey is strongly targeted toward GABAergic interneurons. Here we examine the localization of m1 and m2 muscarinic receptor subtypes across subpopulations of GABAergic interneurons—identified by their expression of the calcium‐binding proteins parvalbumin, calbindin, and calretinin—using dual‐immunofluorescence confocal microscopy in V1 of the macaque monkey. In doing so, we find that the vast majority (87%) of parvalbumin‐immunoreactive neurons express m1‐type muscarinic ACh receptors. m1 receptors are also expressed by 60% of calbindin‐immunoreactive neurons and 40% of calretinin‐immunoreactive neurons. m2 AChRs, on the other hand, are expressed by only 31% of parvalbumin neurons, 23% of calbindin neurons, and 25% of calretinin neurons. Parvalbumin‐immunoreactive cells comprise ≈75% of the inhibitory neuronal population in V1 and included in this large subpopulation are neurons known to veto and regulate the synchrony of principal cell spiking. Through the expression of m1 ACh receptors on nearly all of these PV cells, the cholinergic system avails itself of powerful control of information flow through and processing within the network of principal cells in the cortical circuit. J. Comp. Neurol. 507:1748–1762, 2008. © 2008 Wiley‐Liss, Inc.
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Cholinergic receptors are expressed by inhibitory and excitatory cortical neurons and on the terminals of thalamocortical neurons.
“Cholinergic receptors are expressed by inhibitory and excitatory cortical neurons119,124,158–164, as well as on the terminals of thalamocortical neurons165–169.”
From Mechanisms underlying gain modulation in the cortex (2020) · cites this paper as [159]
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Howe, W. M. (2012) · Deep Blue (University of Michigan)
Stay focussed – muffle that resonant bass!
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is mediated by GABAergic inhibition Cholinergic suppression of visual responses in primate V1
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Self-citation
- Authors
- Disney, A. A., & Aoki, C.
- Affiliations
- New York University (US)
- Corresponding author
- Disney, Anita A.
- Venue
- Journal of Comparative Neurology
- Publisher
- Wiley
- Published
- 2008-02-08
- Volume
- 507
- Issue
- 5
- Pages
- 1748-1762
- ISSN
- 0021-9967 (ISSN-L)
- 1096-9861
- PMC
- PMC2845159
- OpenAlex
- W1992057648
- Cited by
- 109
- References
- 67
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 7 · 2023: 4 · 2022: 2 · 2021: 7 · 2020: 7 · 2019: 4 · 2018: 13 · 2017: 7 · 2016: 1 · 2015: 6 · 2014: 11 · 2013: 9 · 2012: 10
- FWCI
- 2.45
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The Journal of Comparative Neurology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Eye Institute (P30 EY-13079, R01EY013145, R01EY13145, P30EY013079)
- National Institute of Neurological Disorders and Stroke (R01 NS41091, R01NS041091, R25NS080686)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
- Keywords
- muscarinic receptors, M1 muscarinic receptor, M2 muscarinic receptor, parvalbumin, GABAergic interneurons, visual cortex, macaque, calbindin, calretinin, calcium-binding proteins, cholinergic modulation, principal cells, neuronal synchronization
- MeSH terms
- Acetylcholine, Animals, Fluorescent Antibody Technique, gamma-Aminobutyric Acid, Immunohistochemistry, Interneurons, Macaca mulatta, Male, Parvalbumins, Receptors, Muscarinic, Visual Cortex, Microscopy, Confocal, Calbindins, S100 Calcium Binding Protein G
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