GlutamateNMDA receptor NR1 subunit mRNA expression in Alzheimer's disease
Abstract
We analyzed the expression profile of two NMDAR1 mRNA isoform subsets, NR1 0XX and NR1 1XX, in discrete regions of human cerebral cortex. The subsets are characterized by the absence or presence of a 21‐amino acid N‐terminal cassette. Reverse transcription polymerase chain reaction for NR1 isoforms was performed on total RNA preparations from spared and susceptible regions from 10 pathologically confirmed Alzheimer's disease (AD) cases and 10 matched controls. Primers spanning the splice insert yielded two bands, 342 bp (NR1 0XX) and 405 bp (NR1 1XX), on agarose gel electrophoresis. The bands were visualized with ethidium and quantified by densitometry. NR1 1XX transcript expression was calculated as a proportion of the NR1 1XX + NR1 0XX total. Values were significantly lower in AD cases than in controls in mid‐cingulate cortex, p < 0.01, superior temporal cortex, p < 0.01 and hippocampus, p ∼ 0.05. Cortical proportionate NR1 1XX transcript expression was invariant over the range of ages and areas of controls tested, at ∼50%. This was also true for AD motor and occipital cortex. Proportionate NR1 1XX expression in AD cingulate and temporal cortex was lower at younger ages and increased with age: this regression was significantly different from that in the homotropic areas of controls. Variations in NR1 N‐terminal cassette expression may underlie the local vulnerability to excitotoxic damage of some areas in the AD brain. Alternatively, changes in NR1 mRNA expression may arise as a consequence of the AD disease process.
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GluN1 mRNA levels are significantly decreased in AD patients, and expression of a GluN1 isoform containing a unique N-terminus is significantly lower in AD brain compared to controls.
“GluN1 mRNA levels were also significantly decreased in AD patients, and expression of a GluN1 isoform containing a unique N-terminus was significantly lower in AD brain compared to controls [61].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [61]
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Src dependency of the regulation of LTP by alternative splicing of GRIN1 exon 5
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“In limbic lobe, the affected regions were Temporal Pole Sup L [26], Cingulum Mid R [28], Cingulum Post R [20, 26, 27], and”
BackgroundRole of Ionotropic Glutamate Receptors in Neurodegenerative and Other Disorders
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Role of Ionotropic Glutamate Receptors in Neurodegenerative and Other Disorders
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Self-citationN1 cassette-lacking NMDA receptors mediate the antidepressant activity of ketaminePreprint
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- Authors
- Hynd, M. R., Scott, H. L., & Dodd, P. R.
- Affiliations
- The University of Queensland (AU)
- Corresponding author
- Dodd, Peter R.
- ORCID
- Dodd, Peter R.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2001-07
- Volume
- 78
- Issue
- 1
- Pages
- 175-182
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1496193699
- Cited by
- 66
- References
- 38
- Citations by year
- 2025: 1 · 2024: 4 · 2023: 2 · 2022: 2 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 2 · 2017: 3 · 2016: 3 · 2015: 1 · 2014: 3 · 2013: 2 · 2012: 1
- FWCI
- 3.54
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, NMDA receptor 1, mRNA isoforms, glutamate receptors, cerebral cortex, hippocampus, cingulate cortex, superior temporal cortex, regional vulnerability, excitotoxicity, age-related changes, gene expression
- MeSH terms
- Aged, Aged, 80 and over, Aging, Alzheimer Disease, Brain, Female, Humans, Male, Middle Aged, Regression Analysis, RNA, Messenger, Time Factors, Tissue Distribution, Cryopreservation, Receptors, N-Methyl-D-Aspartate, Protein Isoforms
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