Gluthatione level is altered in lymphoblasts from patients with familial Alzheimer’s disease
Abstract
Intracellular levels of glutathione (GSH), glutathione disulphide (GSSG), glutamic acid and gamma-glutamyl cysteine synthetase (gamma-GCS) were measured in lymphoblast lines from patients with familial and sporadic Alzheimer's disease (AD) and from age-matched controls. Lymphoblasts carrying presenilins (PS) and amyloid precursor protein (APP) genes mutations showed significantly decreased GSH content with respect to controls. Levels of GSSG and glutamic acid, as well as the activity of gamma-GCS were not significantly different in lymphoblasts carrying genes mutations as compared with control cells. These results indicate that even peripheral cells not involved in the neurodegenerative process of AD show altered GSH content when carrying PS and APP genes mutations. The provided data appear to be in accordance with the known alteration of GSH levels in central nervous system and strengthen the hypothesis of oxidative stress as an important, possibly crucial mechanism in the pathogenesis of AD.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
GCLC is the main regulating protein for glutathione production, a process impacted by AD pathology.
“GCLC is the main regulating protein for glutathione production, a process impacted by AD pathology [24,25,26].”
From Centella Asiatica Improves Memory and Promotes Antioxidative Signaling in 5XFAD Mice (2019) · cites this paper as [26]
Cites
Amyloid, the presenilins and Alzheimer’s disease
Hardy, J. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)01030-2 · Cited by 1,370 · see citing works
Harman, D. (1992) · Mutation Research/DNAging · doi:10.1016/0921-8734(92)90030-s · Cited by 902 · see citing works
Cell Biology of the Amyloid beta-Protein Precursor and the Mechanism of Alzheimer's Disease
Selkoe, D. J. (1994) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.10.110194.002105 · Cited by 748 · see citing works
Bains, J. S., & Shaw, C. A. (1997) · Brain Research Reviews · doi:10.1016/s0165-0173(97)00045-3 · Cited by 716 · see citing works
Mark, R. J., Hensley, K., Butterfield, D. A., & Mattson, M. P. (1995) · Journal of Neuroscience · doi:10.1523/jneurosci.15-09-06239.1995 · Cited by 553 · see citing works
Increased peroxidation and reduced antioxidant enzyme activity in Alzheimer's disease
Marcus, D. L., Thomas, C., Rodriguez, C., Simberkoff, K., Tsai, J. S., Strafaci, J. A., & Freedman, M. L. (1998) · Experimental Neurology · doi:10.1006/exnr.1997.6750 · Cited by 513 · see citing works
High-performance liquid chromatography of thiols and disulfides: Dinitrophenol derivatives
Fariss, M. W., & Reed, D. J. (1987) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(87)43018-8 · Cited by 505 · see citing works
Guo, Q., Sopher, B. L., Furukawa, K., Pham, D. G., Robinson, N., Martin, G. M., & Mattson, M. P. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-11-04212.1997 · Cited by 487 · see citing works
Wolozin, B. L., Iwasaki, K., Vito, P., Ganjei, J. K., Lacaná, E., Sunderland, T., Zhao, B., Kusiak, J. W., Wasco, W., & D'adamio, L. (1996) · Science · doi:10.1126/science.274.5293.1710 · Cited by 421 · see citing works
Are reactive oxygen species involved in Alzheimer's disease?
Benzi, G. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00066-n · Cited by 365 · see citing works
Guo, Q., Furukawa, K., Sopher, B. L., Pham, D. G., Xie, J., Robinson, N., Martin, G. M., & Mattson, M. P. (1996) · Neuroreport · doi:10.1097/00001756-199612200-00074 · Cited by 320 · see citing works
Presenilins, the Endoplasmic Reticulum, and Neuronal Apoptosis in Alzheimer's Disease
Mattson, M. P., Guo, Q., Furukawa, K., & Pedersen, W. A. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70010001.x · Cited by 246 · see citing works
Involvement of free radicals in dementia of the Alzheimer type: A hypothesis
Volicer, L., & Crino, P. B. (1990) · Neurobiology of Aging · doi:10.1016/0197-4580(90)90119-k · Cited by 190 · see citing works
Mitochondrial function, GSH and iron in neurodegeneration and Lewy body diseases
Gu, M., Owen, A., Toffa, S., Cooper, J. A. D., Dexter, D. T., Jenner, P. G., MARSDEN, C. D., & Schapira, A. H. V. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00095-1 · Cited by 164 · see citing works
Cellular Mechanisms of Resistance to Chronic Oxidative Stress
Sagara, Y., Dargusch, R., Chambers, D. J., Davis, J. B., Schubert, D. A., & Maher, P. A. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00457-7 · Cited by 163 · see citing works
Molecular genetics of Alzheimer's disease
Cruts, M., & Broeckhoven, C. V. (1998) · Annals of Medicine · doi:10.3109/07853899809002605 · Cited by 148 · see citing works
Perry, T. L., Yong, V. W., Bergeron, C., Hansen, S., & Jones, K. L. (1987) · Annals of Neurology · doi:10.1002/ana.410210403 · Cited by 121 · see citing works
Harman, D. (1993) · AGE · doi:10.1007/bf02436127 · Cited by 63 · see citing works
Glutathione Metabolism in Crohn′s Disease
Iantomasi, T., Marraccini, P., Favilli, F., VINCENZINI, M. T., Ferretti, P., & Tonelli, F. (1994) · Biochemical Medicine and Metabolic Biology · doi:10.1006/bmmb.1994.1062 · Cited by 62 · see citing works
Self-citationBracco, L., & Amaducci, L. A. (1992) · Neuroepidemiology · doi:10.1159/000110906 · Cited by 15 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Review: Alzheimer's Amyloid β-Peptide-Associated Free Radical Oxidative Stress and Neurotoxicity
Varadarajan, S., Yatin, S., Aksenova, M., & Butterfield, D. A. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4274 · Cited by 735 · see citing works
Abramov, A. Y., Canevari, L., & Duchen, M. R. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.006 · Cited by 223 · see citing works
Oxidant/Antioxidant Imbalance in Alzheimer’s Disease: Therapeutic and Diagnostic Prospects
Wojsiat, J., Zoltowska, K. M., Laskowska-Kaszub, K., & Wojda, U. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/6435861 · Cited by 221 · see citing works
Centella Asiatica Improves Memory and Promotes Antioxidative Signaling in 5XFAD Mice
Matthews, D. G., Caruso, M., Murchison, C. F., Zhu, J. Y., Wright, K. M., Harris, C. J., Gray, N. E., Quinn, J. F., & Soumyanath, A. (2019) · Antioxidants · doi:10.3390/antiox8120630 · Cited by 86 · see citing works
Yoo, C.-H., Kim, J., Baek, H.-M., Chang, K.-A., & Choe, B.-Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065073 · Cited by 13 · see citing works
- Authors
- Cecchi, C., Latorraca, S., Sorbi, S., Iantomasi, T., Favilli, F., Vincenzini, M. T., & Liguri, G.
- Affiliations
- University of Florence (IT)
- Corresponding author
- Liguri, Gianfranco
- Venue
- Neuroscience Letters
- Publisher
- Elsevier BV
- Published
- 1999-11
- Volume
- 275
- Issue
- 2
- Pages
- 152-154
- ISSN
- 0304-3940 (ISSN-L)
- OpenAlex
- W2088881207
- Cited by
- 101
- References
- 20
- Citations by year
- 2024: 2 · 2023: 1 · 2022: 1 · 2021: 4 · 2020: 2 · 2019: 4 · 2018: 2 · 2017: 3 · 2016: 3 · 2015: 4 · 2014: 6 · 2013: 1 · 2012: 8
- FWCI
- 1.89
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuroscience Letters (publishedVersion)
- PubMed (publishedVersion)
- Florence Research (University of Florence) (submittedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Keywords
- glutathione, glutathione disulfide, gamma-glutamylcysteine synthetase, familial Alzheimer's disease, presenilin mutations, amyloid precursor protein mutations, lymphoblasts, oxidative stress, glutamate, glutathione metabolism
- MeSH terms
- Alzheimer Disease, Glutamate-Cysteine Ligase, Glutathione, Humans, Lymphocyte Activation, Lymphocytes, Membrane Proteins, Oxidation-Reduction, Amyloid beta-Protein Precursor, Glutamic Acid, Glutathione Disulfide, Presenilin-1
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review