Cited by 440Alzheimer's disease research and treatmentsMitochondrial Function and PathologyAntioxidant Activity and Oxidative Stress

The DOI matches its Crossref record.

Impairment of Glucose and Glutamate Transport and Induction of Mitochondrial Oxidative Stress and Dysfunction in Synaptosomes by Amyloid β‐Peptide: Role of the Lipid Peroxidation Product 4‐Hydroxynonenal

Keller, Jeffrey N., Pang, Zheng, Geddes, James W., Begley, James G., Germeyer, Ariane, Waeg, Georg, Mattson, Mark P.·1997·Journal of Neurochemistry

DOI 10.1046/j.1471-4159.1997.69010273.x

Open this paper in CoChat — free account

Abstract

Deposits of amyloid beta-peptide (A beta), reduced glucose uptake into brain cells, oxidative damage to cellular proteins and lipids, and excitotoxic mechanisms have all been suggested to play roles in the neurodegenerative process in Alzheimer's disease. Synapse loss is closely correlated with cognitive impairments in Alzheimer's disease, suggesting that the synapse may be the site at which degenerative mechanisms are initiated and propagated. We report that A beta causes oxyradical-mediated impairment of glucose transport, glutamate transport, and mitochondrial function in rat neocortical synaptosomes. A beta induced membrane lipid peroxidation in synaptosomes that occurred within 1 h of exposure; significant decreases in glucose transport occurred within 1 h of exposure to A beta and decreased further with time. The lipid peroxidation product 4-hydroxynonenal conjugated to synaptosomal proteins and impaired glucose transport; several antioxidants prevented A beta-induced impairment of glucose transport, indicating that lipid peroxidation was causally linked to this adverse action of A beta. FeSO4 (an initiator of lipid peroxidation), A beta, and 4-hydroxynonenal each induced accumulation of mitochondrial reactive oxygen species, caused concentration-dependent decreases in 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide reduction, and reduced cellular ATP levels significantly. A beta also impaired glutamate transport, an effect blocked by antioxidants. These data suggest that A beta induces membrane lipid peroxidation, which results in impairment of the function of membrane glucose and glutamate transporters, altered mitochondrial function, and a deficit in ATP levels; 4-hydroxynonenal appears to be a mediator of these actions of A beta. These data suggest that oxidative stress occurring at synapses may contribute to the reduced glucose uptake and synaptic degeneration that occurs in Alzheimer's disease patients. They further suggest a sequence of events whereby oxidative stress promotes excitotoxic synaptic degeneration and neuronal cell death in a variety of different neurodegenerative disorders.

Integrity signals

Registry

Crossref · 10.1046/j.1471-4159.1997.69010273.x

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Sorted by citations

Items 301–400 of 440

Stimulation of Insulin Signaling and Inhibition of JNK-AP1 Activation Protect Cells from Amyloid-β-Induced Signaling Dysregulation and Inflammatory Response
Bamji‐Mirza, M., Callaghan, D., Najem, D., Shen, S., Hasim, M. S., Yang, Z., & Zhang, W. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131949 · Cited by 26
“Short term exposure of A to cerebral synaptosomes from Sprague-Dawley rats resulted in lipid peroxidation and a significant decrease in glucose transport [7] suggesting that impairments in insulin signaling and glucose utilization occur during the early stages of AD, prior to significant A plaque burden.”
Background
Combination antiretroviral therapy (cART)-induced hippocampal disorders: Highlights on therapeutic potential of Naringenin and Quercetin
Akang, E. N., Dosumu, O. O., Afolayan, O. O., Fagoroye, A. M., Osiagwu, D. D., Usman, I. T., Oremosu, A. A., & Akanmu, S. A. (2019) · IBRO Reports · doi:10.1016/j.ibror.2019.04.002 · Cited by 26
“It has been reported that the byproducts of lipid peroxidation have high affinity for amino acids, hampering glutamate and sugar uptake blocking neurotransmitters and activating c-Jun and MAP kinase pathways to invoke cellular apoptosis (Keller et al., 1997).”
Background
Activation of phosphatidylcholine signalling during oxidative stress in synaptic endings
Mateos, M. V., Uranga, R. M., Salvador, G. A., & Giusto, N. M. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.07.005 · Cited by 26
“The methods employed in the present study are similar to those described by Keller and co workers (Keller et al., 1997a,b).”
Membrane Disordering Effects of β-Amyloid Peptides
Eckert, G. P., Wood, W. G., & Müller, W. E. G. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_16 · Cited by 26
Impact of common ALDH2 inactivating mutation and alcohol consumption on Alzheimer’s disease
Seike, T., Chen, C., & Mochly‐Rosen, D. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1223977 · Cited by 28
“4-HNE leads to dysfunction of glucose and glutamate transporters, mitochondrial dysfunction, and reduced adenosine triphosphate (ATP) levels, and is involved in synaptic degeneration (Keller et al., 1997).”
Background
G Protein and cAMP-Dependent Protein Kinase Mediate Amyloid β-Peptide Inhibition of Neuronal Glucose Uptake
Prapong, T., Uemura, E., & Hsu, W. H. (2001) · Experimental Neurology · doi:10.1006/exnr.2000.7519 · Cited by 25
Mitochondria and the Repurposing of Diabetes Drugs for Off-Label Health Benefits
Yip, J., Chiang, G. S. H., Lee, I. C. J., Lehming-Teo, R., Dai, K., Dongol, L., Wang, L. Y.-T., Teo, D. W. X., Seah, G. T., & Lehming, N. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26010364 · Cited by 30
Cellular mechanisms of brain hypoglycemia
Исаев, Н. К., Stelmashook, E. V., & Zorov, D. B. (2007) · Biochemistry (Moscow) · doi:10.1134/s0006297907050021 · Cited by 24
Diabetes, Insulin and Alzheimer's Disease
Craft, S., & Christen, Y. (2010) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-04300-0 · Cited by 24
Metabolic regulation of aging and age-related disease
Hamrick, M. W., & Stranahan, A. M. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101175 · Cited by 27
From the Mind to the Spine: The Intersecting World of Alzheimer’s and Osteoporosis
Margetts, T. J., Wang, H. S., Karnik, S. J., Plotkin, L. I., Movilă, A., Oblak, A. L., Fehrenbacher, J. C., & Kacena, M. A. (2024) · Current Osteoporosis Reports · doi:10.1007/s11914-023-00848-w · Cited by 26
“Oxidative damage has been implicated in the impairment of glucose and glutamate transport and mitochondrial dysfunction induced by Aβ in synaptosomes [119].”
Background
Increase in Molecular Rigidity of the Protein Conformation of Brain Na+-K+-ATPase by Modification with 4-Hydroxy-2-nonenal
Miyake, H., Kadoya, A., & Ohyashiki, T. (2003) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.26.1652 · Cited by 23
Mutant presenilin 2 increased oxidative stress and p53 expression in neuronal cells
Nguyen, H. N., Lee, M. S., Hwang, D. Y., et al. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.03.119 · Cited by 22
Brain Damage - Bridging Between Basic Research and Clinics
González-Quevedo, A. (2012) · InTech eBooks · doi:10.5772/2174 · Cited by 21
Effect of Oxidative Stress on the Uptake of GABA and Glutamate in Synaptosomes Isolated from Diabetic Rat Brain
Duarte, A. I., Santos, M. S., Seiça, R. M. F., & Oliveira, C. R. (2000) · Neuroendocrinology · doi:10.1159/000054585 · Cited by 21
Distinct Glycolysis Inhibitors Determine Retinal Cell Sensitivity to Glutamate-Mediated Injury
Rego, A. C., Areias, F. M., Santos, M. S., et al. (1999) · Neurochemical Research · doi:10.1023/a:1020977331372 · Cited by 21
Naproxen-induced oxidative stress in the isolated perfused rat liver
Yokoyama, H., Horie, T., & Awazu, S. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.01.003 · Cited by 21
β-Amyloid overload does not directly correlate with SAPK/JNK activation and tau protein phosphorylation in the cerebellar cortex of Ts65Dn mice
Lomoio, S., Scherini, E., & Necchi, D. (2009) · Brain Research · doi:10.1016/j.brainres.2009.08.052 · Cited by 20
Oxidative Alterations in Neurodegenerative Diseases
Markesbery, W. R., Montine, T. J., & Lovell, M. A. (2001) · Humana Press eBooks · doi:10.1007/978-1-59259-106-0_2 · Cited by 27
“impairing the function of, membrane ion-motive ATPases, glucose transporters, and glutamate transporters (Mark et al., 1995, 1997a, b; Keller et al., 1997).”
Background
Influence of vitamin E succinate on retinal cell survival
Rego, A. C., Santos, M. S., Proença, M. T., et al. (1998) · Toxicology · doi:10.1016/s0300-483x(98)00054-7 · Cited by 20
“…of the retinal cells submitted to vitamin E succinate supplementation was analyzed by the release of LDH, which is indicative of irreversible membrane disruption and cell death, and by the reduction of MTT, suggested to be a measure of the mitochondria activity (Mosmann, 1983; Keller et al., 1997).”
BackgroundMethodInfluential
The mitochondria-targeted small molecule SS31 delays progression of behavioral deficits by attenuating β-amyloid plaque formation and mitochondrial/synaptic deterioration in APP/PS1 mice
Jia, Y., Wang, W., Han, N., Sun, H.-L., Dong, F., Song, Y., Feng, R.-F., & Wang, J.-H. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.02.076 · Cited by 19
Mind Gaps and Bone Snaps: Exploring the Connection Between Alzheimer’s Disease and Osteoporosis
Wang, H. S., Karnik, S. J., Margetts, T. J., Plotkin, L. I., Movilă, A., Fehrenbacher, J. C., Kacena, M. A., & Oblak, A. L. (2024) · Current Osteoporosis Reports · doi:10.1007/s11914-023-00851-1 · Cited by 24
Contributions of impaired hippocampal plasticity and neurodegeneration to age-related deficits in hormonal pulsatility
Stranahan, A. M., Lee, K. M., & Mattson, M. P. (2008) · Ageing Research Reviews · doi:10.1016/j.arr.2007.12.004 · Cited by 19
Self-citation
Curcumin and β-caryophellene attenuate cadmium quantum dots induced oxidative stress and lethality in Caenorhabditis elegans model system
Srivastava, S., Pant, A., Trivedi, S., et al. (2016) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2016.01.001 · Cited by 19
In Vivo Assessment of Lipid Peroxidation Products Associated with Age-Related Neurodegenerative Diseases
Ou, J. J., Zhang, Y., & Montine, T. J. (2002) · Experimental Neurology · doi:10.1006/exnr.2002.7923 · Cited by 19
4-Hydroxynonenal disrupts zinc export in primary rat cortical cells
SMITH, J., Xiong, S., & Lovell, M. A. (2005) · NeuroToxicology · doi:10.1016/j.neuro.2005.05.009 · Cited by 19
Molecular structure of tetraaqua adenosine 5′-triphosphate aluminium(III) complex: A study involving Raman spectroscopy, theoretical DFT and potentiometry
Tenório, T. D. S., Silva, A. M., Ramos, J. M., Buarque, C. D., & Felcman, J. (2012) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2012.12.019 · Cited by 18
Citalopram attenuated neurobehavioral, biochemical, and metabolic alterations in transient middle cerebral artery occlusion model of stroke in male Wistar rats
Gupta, S., Upadhayay, D., Sharma, U., Jagannathan, N. R., & Gupta, Y. K. (2018) · Journal of Neuroscience Research · doi:10.1002/jnr.24226 · Cited by 18
“Lipid peroxidation is also reported to induce apoptosis by generation of 4-hydroxynonenal, which impairs the functioning of membrane transporters such as Na(1) ATPase, K(1) ATPase, glucose, and Glu (Keller et al., 1997).”
Background
Mitochondrial SIRT3 Deficiency Results in Neuronal Network Hyperexcitability, Accelerates Age-Related Aβ Pathology, and Renders Neurons Vulnerable to Aβ Toxicity
Perone, I., Ghena, N., Wang, J., Mackey, C. D., Wan, R., Malla, S., Gorospe, M., Cheng, A., & Mattson, M. P. (2022) · NeuroMolecular Medicine · doi:10.1007/s12017-022-08713-2 · Cited by 20
“Data from studies of cultured neurons and transgenic mice that develop Aβ plaques have shown Aβ aggregation on neuronal membranes where the Aβ impairs the function of ion-motive ATPases and glucose transporters, rendering neurons vulnerable to cellular calcium overload, and excitotoxicity (Keller et al., 1997; Mark et…”
BackgroundSelf-citation
Mitochondria-sequestered Aβ renders synaptic mitochondria vulnerable in the elderly with a risk of Alzheimer disease
Jia, K., Tian, J., Wang, T., Guo, L., Xuan, Z., Swerdlow, R. H., & Du, H. (2023) · JCI Insight · doi:10.1172/jci.insight.174290 · Cited by 20
The morphological changes and molecular biomarker responses in the liver of fluoride-exposed Bufo gargarizans larvae
Bo, X., Mu, D., Wu, M., Xiao, H., & Wang, H. (2018) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2018.01.027 · Cited by 16
Role of Metals in Neuronal Apoptosis: Challenges Associated with Neurodegeneration
Ravid, R., & Rao, K. S. J. (2006) · Current Alzheimer Research · doi:10.2174/156720506778249399 · Cited by 18
Multidrug Resistance-Associated Protein 2 (MRP2) Enhances 4-Hydroxynonenal-Induced Toxicity in Madin−Darby Canine Kidney II Cells
Ji, B., Ito, K., & Horie, T. (2004) · Chemical Research in Toxicology · doi:10.1021/tx034067m · Cited by 17
Research progress on ferroptosis in the pathogenesis and treatment of neurodegenerative diseases
Wang, L., Fang, X., Ling, B., Wang, F., Xia, Y., Zhang, W., Zhong, T., & Wang, X. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1359453 · Cited by 18
Cryopreservation of rat cortical synaptosomes and analysis of glucose and glutamate transporter activities, and mitochondrial function
Begley, J. G., Butterfield, D. A., Keller, J. N., et al. (1998) · Brain Research Protocols · doi:10.1016/s1385-299x(98)00024-5 · Cited by 16
Self-citation
Glimepiride reduces mononuclear activation of the redox‐sensitive transcription factor nuclear factor‐kappa B
Schiekofer, S., Rudofsky, G., Andrassy, M., Schneider, J. G., Chen, J., Isermann, B., Kanitz, M., Elsenhans, S., Heinle, H., Balletshofer, B. M., et al. (2003) · Diabetes Obesity and Metabolism · doi:10.1046/j.1463-1326.2003.00270.x · Cited by 16
Excitatory amino acid transporters as emerging targets for central nervous system therapeutics
Dunlop, J., Zaleska, M. M., Eliasof, S. D., & Moyer, J. A. (1999) · Emerging Therapeutic Targets · doi:10.1517/14728222.3.4.543 · Cited by 16
Estrés oxidativo, péptido β-amiloide y enfermedad de Alzheimer
Manzano‐León, N., & Mas‐Oliva, J. (2006) · Gaceta Médica de México · Cited by 16
Comparison of the effects of hydrogen peroxide, 4-hydroxy-2-nonenal and β-amyloid (25–35) upon calcium signalling
Fowler, C. J., Ando, Y., & Tiger, G. (1998) · Neurochemistry International · doi:10.1016/s0197-0186(98)00013-8 · Cited by 15
Quantitative autoradiography of Na+-dependent [3H]l-aspartate binding to l-glutamate transporters in rat brain: structure-activity studies using l-trans-pyrrolidine-2,4-dicarboxylate (l-t-PDC) and 2-(carboxycyclopropyl)-glycine (CCG)
Lieb, I., Chebib, M., Cooper, B., Dias, L. S., & Balcar, V. J. (2000) · Neurochemistry International · doi:10.1016/s0197-0186(99)00140-0 · Cited by 15
REMOVED: Protein kinase inhibitors in traumatic brain injury and repair: New roles of nanomedicine
Sharma, H. S., Sahib, S., Tian, Z. R., Muresanu, D. F., Nozari, A., Lafuente, J. V., Wiklund, L., & Sharma, A. (2020) · Progress in brain research · doi:10.1016/bs.pbr.2020.09.009 · Cited by 14
Susceptibility to β-Amyloid-Induced Toxicity Is Decreased in Goto-Kakizaki Diabetic Rats: Involvement of Oxidative Stress
Pereira, C., Moreira, P. I., Seiça, R. M. F., et al. (2000) · Experimental Neurology · doi:10.1006/exnr.1999.7270 · Cited by 14
The pyrrolopyrimidine U101033E is a potent free radical scavenger and prevents Fe(II)-induced lipid peroxidation in synaptosomal membranes
Lauderback, C. M., Breier, A. M., Hackett, J. M., Varadarajan, S., Goodlett-Mercer, J., & Butterfield, D. A. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00015-6 · Cited by 13
Glutamate Receptors in Aging and Alzheimer's Disease
Mishizen-Eberz, A. J., Ikonomović, M. D., & Armstrong, D. M. (2001) · Elsevier eBooks · doi:10.1016/b978-012351830-9/50022-6 · Cited by 18
4-Hydroxyhexenal (HHE) Impairs Glutamate Transport in Astrocyte Cultures
Lovell, M. A., Bradley‐Whitman, M. A., & Fister, S. X. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120409 · Cited by 15
“modified by exposure to A [25, 35, 63–66] or alde-”
Assemblages of prion fragments: novel model systems for understanding amyloid toxicity
Satheeshkumar, K., Murali, J., & Rajadas, J. (2004) · Journal of Structural Biology · doi:10.1016/j.jsb.2004.05.006 · Cited by 13
Insight into the anti-amyloidogenic activity of polyphenols and its application in virtual screening of phytochemical database
Chakraborty, S., & Basu, S. (2014) · Medicinal Chemistry Research · doi:10.1007/s00044-014-1081-2 · Cited by 11
“exposure of synapses to Ab impairs the function of membrane ion channels, glutamate transporters, and compromises mitochondrial function mediated by oxidative stress (Keller et al., 1997).”
Background
Prevention and Therapy of Neurodegenerative Disorders: Role of Nutritional Antioxidants
Matteo, V. D., Pierucci, M., Giovanni, G. D., & Esposito, E. (2007) · Elsevier eBooks · doi:10.1016/b978-044452809-4/50168-x · Cited by 11
Effects of the novel cyclosporine derivative PSC833 on glucose metabolism in rat primary cultures of neuronal and glial cells11Abbreviations: CsA, cyclosporine A; DMEM, Dulbecco’s modified Eagle’s medium; FBS, fetal bovine serum; LDH, l-lactate dehydrogenase (EC 1.1.1.27); MDR, multidrug resistance, PC, pyruvate carboxylase (EC 1.2.4.1); PDH, pyruvate dehydrogenase complex (EC 1.2.4.1, 1.8.1.4. 2.3.1.12, 3.1.3.43); and TCA, tricarboxylic acid.
Cruz, F., & Wolf, A. (2001) · Biochemical Pharmacology · doi:10.1016/s0006-2952(01)00642-6 · Cited by 10
A multi‐ingredient dietary supplement abolishes large‐scale brain cell loss, improves sensory function, and prevents neuronal atrophy in aging mice
Lemon, J. A., Aksenov, V., Samigullina, R., Aksenov, S., Rodgers, W. H., Rollo, C. D., & Boreham, D. R. (2016) · Environmental and Molecular Mutagenesis · doi:10.1002/em.22019 · Cited by 12
Repeated addition of insulin for dynamic control of apoptosis in serum-free culture of Chinese hamster ovary cells
Yun, Z., Takagi, M., & Yoshida, T. (2003) · Journal of Bioscience and Bioengineering · doi:10.1016/s1389-1723(03)90097-1 · Cited by 10
Mechanisms and Prevention of Noise-Induced Hearing Loss
Miller, J. M., Yamashita, D., Minami, S., Yamasoba, T., & Prell, C. G. L. (2006) · Otology Japan · doi:10.11289/otoljpn1991.16.139 · Cited by 9
The role of mitochondrial uncoupling in the regulation of mitostasis after traumatic brain injury
Hubbard, W. B., Velmurugan, G. V., & Sullivan, P. G. (2024) · Neurochemistry International · doi:10.1016/j.neuint.2024.105680 · Cited by 10
Adventures in Neural Plasticity, Aging, and Neurodegenerative Disorders Aboard the CWC Beagle
Mattson, M. P. (2003) · Neurochemical Research · doi:10.1023/a:1026000703290 · Cited by 8
Self-citation
Opposite in vivo effects of agents that stimulate or inhibit the glutamate/cysteine exchanger system on the inhibition of hippocampal LTP by Aß
Zhang, D., Jin, B., Ondrejčák, T., & Rowan, M. J. (2016) · Hippocampus · doi:10.1002/hipo.22667 · Cited by 8
“Reducing glutamate receptor activation with receptor antagonists (Hu et al., 2009; Klyubin et al., 2011; Rammes et al., 2011; Ronicke et al., 2011; Hu et al., 2014), or by enhancing glutamate clearance (Li et al., 2009; Takahashi et al., 2015; Varga et al., 2015; Zumkehr et al., 2015) has been…”
Background
Adaptative responses of spinal astrocytes to oxidative stress
Cassina, P., Peluffo, H., & Barbeito, L. (2001) · Progress in brain research · doi:10.1016/s0079-6123(01)32092-7 · Cited by 8
Chapter 9 The Role of Mitochondrial Genome Mutations in Neurodegenerative Disease
Glazner, G. W. (1999) · Advances in cell aging and gerontology · doi:10.1016/s1566-3124(08)60029-2 · Cited by 7
Oxidation of 4-hydroxynonenal in rat brain slices
Murphy, T. C., Amarnath, V., & Picklo, M. J. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00182-5 · Cited by 7
How an increase in the copy number of HSV-1 during latency can cause Alzheimer’s disease: the viral and cellular dynamics according to the microcompetition model
Polansky, H., & Goral, B. (2021) · Journal of NeuroVirology · doi:10.1007/s13365-021-01012-9 · Cited by 9
“With an increased oxidative stress, energy metabolism is impaired, eventually leading to neuronal damage, neurodegeneration pathologies, and AD (Keller et al. 1997; Manczak et al. 2006).”
Background
Oxidative and Inflammatory Properties of Aluminum: Possible Relevance in Alzheimer’s Disease
Bondy, S. C., & Campbell, A. (2001) · Elsevier eBooks · doi:10.1016/b978-044450811-9/50041-0 · Cited by 7
Cholinergic Neurotransmission, Amyloid-β Peptide and the Pathogenesis of Alzheimer's Disease
Liu, L. (2003) · Cited by 7
Synaptic-mitochondrial transport: mechanisms in neural adaptation and degeneration
Ding, Y., Yang, H., Gao, J., Tang, C. L., Peng, Y.-Y., Ma, X., Li, S., Wang, H., Lu, X., & Wang, Y. (2025) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-025-05209-y · Cited by 7
The Unified Theory of Neurodegeneration Pathogenesis Based on Axon Deamidation
Joseph, D. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26094143 · Cited by 6
“According to Keller et al. [116], HNE disrupts glucose and glutamate transport by impairing the glucose transporter type-3 and glutamate transporter 1 (GLT-1).”
REMOVED: Nanodelivery of traditional Chinese Gingko Biloba extract EGb-761 and bilobalide BN-52021 induces superior neuroprotective effects on pathophysiology of heat stroke
Sahib, S., Sharma, A., Muresanu, D. F., Zhang, Z., Li, C., Tian, Z. R., Buzoianu, A. D., Lafuente, J. V., Nozari, A., Patnaik, R., et al. (2021) · Progress in brain research · doi:10.1016/bs.pbr.2021.06.007 · Cited by 6
Expression of chaperonin 60 in the hippocampus of the streptozotocin diabetic rat
Yuan, J., Young, B. J., & Martinus, R. D. (2006) · Neuroreport · doi:10.1097/01.wnr.0000201503.15632.06 · Cited by 6
“Such increases produce impaired mitochondrial function in brain synaptosomes [13], and more generally, exacerbate oxidative stress, mitochondrial dysfunction and neuronal death [14].”
Background
Expression Analysis of 4-Hydroxynonenal Modified Proteins in Schizophrenia Brain; Relevance to Involvement in Redox Dysregulation
Manzoor, S., Ayesha, K., Hasan, B., Mushtaq, S., & Ahmed, N. (2021) · Current Proteomics · doi:10.2174/1570164618666210121151004 · Cited by 5
Repeated Glucose Deprivation/Reperfusion Induced PC-12 Cell Death through the Involvement of FOXO Transcription Factor
Han, N., Kim, Y. J., Park, S. M., Kim, S. M., Lee, J., Jung, H. S., Lee, E. J., Kim, T. K., Kim, T. N., Kwon, M. J., et al. (2016) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2016.40.5.396 · Cited by 5
“Amyloid β-peptidecaused Alzheimer’s disease inhibits glucose transport, which in turn triggers the glucose deprivation apoptotic cascade in the cortex and hippocampus [27,28].”
Background
Molecular Mechanisms of Acute Brain Injury and Ensuing Neurodegeneration
Francisco, J., Jose, M., Mahy, N., & Manuel, J. (2012) · InTech eBooks · doi:10.5772/37401 · Cited by 5
Preserving Function in Acute Nervous System Injury
Hall, E. D., & Sullivan, P. G. (2005) · Elsevier eBooks · doi:10.1016/b978-012738903-5/50004-7 · Cited by 5
Analysis of HNE metabolism in CNS models
Kubátová, A., Honzátko, A., Brichac, J., et al. (2007) · Redox Report · doi:10.1179/135100007x162149 · Cited by 5
Effect of Glucose Deprivation and Acute Glutamate Exposure in Cultured Retinal Cells
Rego, A. C., Areias, F. M., Santos, M. S., et al. (1998) · Experimental Neurology · doi:10.1006/exnr.1998.6865 · Cited by 5
“1) and a decrement in the cellular redox efficacy, probably related with changes in mitochondrial function (11, 16), as determined by the MTT method (Table 1).”
Method
Insights into the promising prospect of medicinal chemistry studies against neurodegenerative disorders
Rahman, M. M., Islam, M. R., Tumpa, M. A. A., Shohag, S., shuvo, S. K., Ferdous, J., Kajol, S. A., Aljohani, A. S. M., Abdulmonem, W. A., Rauf, A., et al. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110375 · Cited by 4
Free Radicals and Neuroprotection in Traumatic Brain and Spinal Cord Injury
Hall, E. D. (2008) · Springer eBooks · doi:10.1007/978-0-387-30375-8_10 · Cited by 4
Inflammation, Free Radicals, Glycation, Metabolism and Apoptosis, and Heavy Metals
Mattson, M. P. (2001) · Elsevier eBooks · doi:10.1016/b978-012351830-9/50025-1 · Cited by 5
Self-citation
Structure, function and regulation of glutamate transporters
Levy, L. M. (2001) · Pharmaceutical science series · doi:10.1201/9780203299388.pt5 · Cited by 4
Oxidative Stress and Metals in Alzheimer’s Disease
Fathima, S. A., Maurya, R., & Naqvi, S. (2023) · Springer eBooks · doi:10.1007/978-981-99-6038-5_2 · Cited by 5
Carbonyl Stress, Aging Mechanisms, and The Up-stream Molecular Etiology of Alzheimer′s Disease*
Yin, D., & Liu, W. (2012) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2012.00316 · Cited by 3
Insulin-Mediated Neuroplasticity in the Central Nervous System
Reagan, L. P. (2010) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-04300-0_3 · Cited by 3
“In this regard, the glial glutamate transporter GLT-1 is a target of HNE protein conjugation, which may be responsible for HNE-mediated decreases in glutamate transport in primary astrocytic cultures (Blanc et al. 1998) and in rat cortical synaptosomal fractions ( Keller et al. 1997 ).”
Background
Aging of the Nervous System
Wolkow, C. A., Zou, S., & Mattson, M. P. (2009) · Springer eBooks · doi:10.1007/978-90-481-3465-6_14 · Cited by 3
Self-citation
Addressing the Complex Etiology of Alzheimer‘s Disease: the Role of P25/Cdk5
Mungenast, A. E., & Tsai, L. (2011) · Future Neurology · doi:10.2217/fnl.11.22 · Cited by 3
Aβ 42 oligomers impair the bioenergetic activity in hippocampal synaptosomes derived from APP-KO mice
Beckert, B., Acker‐Palmer, A., & Volknandt, W. (2018) · Biological Chemistry · doi:10.1515/hsz-2017-0238 · Cited by 3
Potentiometric, Raman spectroscopy and DFT study of pentaaqua glycine aluminum(III) complex in aqueous solution
Tenório, T. D. S., & Tenório, A. (2015) · Vibrational Spectroscopy · doi:10.1016/j.vibspec.2015.06.005 · Cited by 3
PS1/gamma-secretase acts as rogue chaperone of glutamate transporter EAAT2/GLT-1 in Alzheimer’s disease
Perrin, F., Anderson, L. C., Mitchell, S. P. C., Sinha, P., Turchyna, Y., Maesako, M., Houser, M. C., Zhang, C. M., Wagner, S. L., Tanzi, R. E., et al. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01876-y · Cited by 6
Mitochondrial oxidative stress and metabolic alterations in neurodegenerative disorders
Keller, J. N., & Glazner, G. W. (2001) · Advances in cell aging and gerontology · doi:10.1016/s1566-3124(01)07020-1 · Cited by 2
Self-citation
Experimental and theoretical investigation of [Al(PCr)(H2O)] complex in aqueous solution
Tenório, T. D. S., Lopes, D. C. N., Silva, A. M., Ramos, J. M., & Buarque, C. D. (2013) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2013.08.073 · Cited by 2
Role of Nutritional Antioxidants in the Prevention and Treatment of Neurodegenerative Disorders
Esposito, E. (2006) · Nutrition and disease prevention · doi:10.1201/9781420019131.ch5 · Cited by 2
Overview: Membrane lipid peroxidation
Montine, K. S., Quinn, J. F., & Montine, T. J. (2003) · Advances in cell aging and gerontology · doi:10.1016/s1566-3124(03)12002-0 · Cited by 2
Cellular and Molecular Mechanisms Underlying Synaptic Degeneration and Neuronal Death in Alzheimer's Disease
Mattson, M. P., Pedersen, W. A., & Culmsee, C. (2001) · Humana Press eBooks · doi:10.1007/978-1-59259-106-0_6 · Cited by 2
Self-citation
Glutamate regulates the viability of retinal cells in culture
Rego, A. C., Santos, M. S., Areias, F. M., et al. (2001) · Vision Research · doi:10.1016/s0042-6989(00)00309-6 · Cited by 2
In Vivo Imaging of Alzheimer Pathology in Transgenic Mice using Multiphoton Microscopy
Bacskai, B. J., Klunk, W. E., Hickey, G. A., Skoch, J. M., Kajdasz, S. T., McLellan, M. E., Frosch, M. P., Debnath, M. L., Holt, D. P., Wang, Y., et al. (2004) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-59300-0_4 · Cited by 2
Contribution of Dietary Carbohydrates in Induction of Oxidative Stress
Farooqui, A. A. (2014) · Springer eBooks · doi:10.1007/978-3-319-04111-7_8 · Cited by 2
Dementia: The Significance of Cerebral Metabolic Disturbances in Alzheimer's Disease. Relation to Parkinson's Disease
Hoyer, S., & Frölich, L. (2007) · Springer eBooks · doi:10.1007/978-0-387-30377-2_12 · Cited by 2
Oxidative stress in neurodegenerative diseases
Javaid, M., Arain, F. M., & Javaid, M. D. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-18807-7.00011-9 · Cited by 2
The role of ALDH2 rs671 polymorphism and C-reactive protein in the phenotypes of male ALS patients
Huang, L., Liu, M., Tang, J., Gong, Z., Li, Z., Yang, Y., & Zhang, M. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1397991 · Cited by 1
The Aβcentric Pathway of Alzheimer’s Disease
Villemagne, V. L., Cappai, R., Barnham, K. J., Cherny, R. A., Opazo, C., Novakovic, K. E., Rowe, C. C., & Masters, C. L. (2006) · Springer eBooks · doi:10.1007/978-1-84628-440-3_2 · Cited by 4
Pharmacological Therapies for Concussions
Hall, E. D., Park, E., & BAKER, A. J. (2022) · Springer eBooks · doi:10.1007/978-3-030-93813-0_9 · Cited by 1
Gut–Brain Axis in Alzheimer’s Disease: Interplay Between Cholecystokinin, Dysbiosis, and Brain-Derived Neurotrophic Factor
Ouerdane, Y., El-Nahas, Z. S., Ouerdane, F., Hamam, K. M., & Ebada, M. A. (2022) · Springer eBooks · doi:10.1007/978-981-16-7606-2_12 · Cited by 4
Stabilizing Calcium Homeostasis
Mattson, M. P. (2002) · Handbook of experimental pharmacology · doi:10.1007/978-3-662-06274-6_5 · Cited by 1
Self-citation
Chapter 10 Excitotoxicity and Oxidative Stress in Pathogenesis of Amyotrophic Lateral Sclerosis/Motor Neuron Disease
Damme, P. V., Bosch, L. V. D., & Robberecht, W. (2003) · Blue books of practical neurology · doi:10.1016/s1877-3419(09)70111-4 · Cited by 1
Chapter 1 Genetic Contributions to the Pathogenesis of Alzheimer's Disease
Mattson, M. P. (1999) · Advances in cell aging and gerontology · doi:10.1016/s1566-3124(08)60021-8 · Cited by 1
Self-citation

Authors: Keller, J. N., Pang, Z., Geddes, J. W., Begley, J. G., Germeyer, A., Waeg, G., & Mattson, M. P.
Affiliations: University of Kentucky (US)
University of Graz (AT)
Corresponding author: Mattson, Mark P.
ORCID: Keller, Jeffrey N.
Geddes, James W.
Germeyer, Ariane
Mattson, Mark P.
Venue: Journal of Neurochemistry
Publisher: Wiley
Published: 1997-07
Volume: 69
Issue: 1
Pages: 273-284
ISSN: 0022-3042 (ISSN-L)
1471-4159
DOI: 10.1046/j.1471-4159.1997.69010273.x
OpenAlex: W2069303994
Cited by: 439
References: 0
Citations by year: 2025: 3 · 2024: 8 · 2023: 11 · 2022: 8 · 2021: 8 · 2020: 9 · 2019: 10 · 2018: 14 · 2017: 4 · 2016: 20 · 2015: 10 · 2014: 8 · 2013: 12 · 2012: 15
FWCI: 19.53
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 1966 d)
Locations: Journal of Neurochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01ns030583-04)
National Institute on Aging (P50AG005144, AG-05144, P01AG010836, AG 10836)
National Institute of Neurological Disorders and Stroke (NS30583)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
Keywords: amyloid-beta, Alzheimer's disease, 4-hydroxynonenal, lipid peroxidation, glucose transport, glutamate uptake, mitochondrial dysfunction, oxidative stress, synaptosomes, reactive oxygen species, ATP depletion, synaptic degeneration, excitotoxicity, antioxidants, neurodegeneration
MeSH terms: Aldehydes, Animals, Biological Transport, Cell Membrane, Cross-Linking Reagents, Energy Metabolism, Female, Glucose, Mitochondria, Synapses, Synaptosomes, Lipid Peroxidation, Amyloid beta-Peptides, Rats, Sprague-Dawley, Reactive Oxygen Species, Oxidative Stress, Glutamic Acid, Rats

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

Impairment of Glucose and Glutamate Transport and Induction of Mitochondrial Oxidative Stress and Dysfunction in Synaptosomes by Amyloid β‐Peptide: Role of the Lipid Peroxidation Product 4‐Hydroxynonenal

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cited by

Related

Metadata

Record

About these checks