Cited by 399Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsPhagocytosis and Immune Regulation

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CD36, a Class B Scavenger Receptor, Is Expressed on Microglia in Alzheimer's Disease Brains and Can Mediate Production of Reactive Oxygen Species in Response to β-Amyloid Fibrils

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Coraci, Indra Sethy, Husemann, Jens, Berman, Joan W., Hulette, Christine, Dufour, Jennifer H., Campanella, Gabriele K., Luster, Andrew D., Silverstein, Samuel C., El Khoury, Joseph B.·2002·The American Journal of Pathology

DOI 10.1016/s0002-9440(10)64354-4PMC PMC1867121

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Abstract

A pathological hallmark of Alzheimer's disease is the senile plaque, composed of beta-amyloid fibrils, microglia, astrocytes, and dystrophic neurites. We reported previously that class A scavenger receptors mediate adhesion of microglia and macrophages to beta-amyloid fibrils and oxidized low-density lipoprotein (oxLDL)-coated surfaces. We also showed that CD36, a class B scavenger receptor and an oxLDL receptor, promotes H(2)O(2) secretion by macrophages adherent to oxLDL-coated surfaces. Whether CD36 is expressed on microglia, and whether it plays a role in secretion of H(2)O(2) by microglia interacting with fibrillar beta-amyloid is not known. Using fluorescence-activated cell sorting analysis and immunohistochemistry, we found that CD36 is expressed on human fetal microglia, and N9-immortalized mouse microglia. We also found that CD36 is expressed on microglia and on vascular endothelial cells in the brains of Alzheimer's disease patients. Bowes human melanoma cells, which normally do not express CD36, gained the ability to specifically bind to surfaces coated with fibrillar beta-amyloid when transfected with a cDNA encoding human CD36, suggesting that CD36 is a receptor for fibrillar beta-amyloid. Furthermore, two different monoclonal antibodies to CD36 inhibited H(2)O(2) production by N9 microglia and human macrophages adherent to fibrillar beta-amyloid by approximately 50%. Our data identify a role for CD36 in fibrillar beta-amyloid-induced H(2)O(2) production by microglia, and imply that CD36 can mediate binding to fibrillar beta-amyloid. We propose that similar to their role in the interaction of macrophages with oxLDL, class A scavenger receptors and CD36 play complimentary roles in the interactions of microglia with fibrillar beta-amyloid.

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Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.
Lorenzo, A., & Yankner, B. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12243 · Cited by 1,324
Activation of microglial cells by β-amyloid protein and interferon-γ
Meda, L., Cassatella, M. A., Szendrei, G. I., Otvos, L., Baron, P., Villalba, M., Ferrari, D., & Rossi, F. (1995) · Nature · doi:10.1038/374647a0 · Cited by 1,314
CD36 is a receptor for oxidized low density lipoprotein
Endemann, G., Stanton, L. W., Madden, K. S., Bryant, C. M., White, R. T., & Protter, A. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50272-1 · Cited by 1,282
A role for macrophage scavenger receptors in atherosclerosis and susceptibility to infection
Suzuki, H. I., Kurihara, Y., Takeya, M., Kamada, N., Kataoka, M., Jishage, K., Ueda, O., Sakaguchi, H., Higashi, T., Suzuki, T., et al. (1997) · Nature · doi:10.1038/386292a0 · Cited by 1,226
Targeted disruption of the class B scavenger receptor CD36 protects against atherosclerotic lesion development in mice
Febbraio, M., Podrez, E. A., Smith, J. D., Hajjar, D. P., Hazen, S. L., Hoff, H. F., Sharma, K., & Silverstein, R. L. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9259 · Cited by 1,037
Scavenger receptor-mediated adhesion of microglia to β-amyloid fibrils
Khoury, J. E., Hickman, S. E., Thomas, C. A., Cao, L., Silverstein, S. C., & Loike, J. D. (1996) · Nature · doi:10.1038/382716a0 · Cited by 727
Self-citation
β-Amyloid-mediated vasoactivity and vascular endothelial damage
Thomas, T., Thomas, G., McLendon, C., Sutton, T., & Mullan, M. (1996) · Nature · doi:10.1038/380168a0 · Cited by 703
Isolation and direct characterization of resident microglial cells from the normal and inflamed central nervous system.
Sedgwick, J. D., Schwender, S., Imrich, H., Dörries, R., Butcher, G. W., & ter Meulen, V. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.16.7438 · Cited by 691
Diversity of function is inherent in matricellular proteins: an appraisal of thrombospondin 1.
Bornstein, P. (1995) · The Journal of cell biology · doi:10.1083/jcb.130.3.503 · Cited by 666
Microglial Cells Internalize Aggregates of the Alzheimer's Disease Amyloid β-Protein Via a Scavenger Receptor
Paresce, D. M., Ghosh, R. N., & Maxfield, F. R. (1996) · Neuron · doi:10.1016/s0896-6273(00)80187-7 · Cited by 663

Show all 56 references

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Yang, C.-N., Shiao, Y.-J., Shie, F.-S., Guo, B.-S., Chen, P.-H., Cho, C.-Y., Chen, Y.-J., Huang, F.-L., & Tsay, H.-J. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.005 · Cited by 117
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Takeuchi, H., & Suzumura, A. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00189 · Cited by 127
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Downregulation of CD36 results in reduced phagocytic ability of peritoneal macrophages of women with endometriosis
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Mallick, R., Basak, S., & Duttaroy, A. K. (2021) · Progress in Lipid Research · doi:10.1016/j.plipres.2021.101116 · Cited by 126
Roles of Microglial and Monocyte Chemokines and Their Receptors in Regulating Alzheimer's Disease-Associated Amyloid-β and Tau Pathologies
Guedes, J. R., Lao, T., Cardoso, A. L., & El Khoury, J. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00549 · Cited by 115
CD36 Signals to the Actin Cytoskeleton and Regulates Microglial Migration via a p130Cas Complex
Stuart, L. M., Bell, S. A., Stewart, C. R., Silver, J. M., Richard, J., Goss, J. L., Tseng, A. A., Zhang, A., Khoury, J. B. E., & Moore, K. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702887200 · Cited by 112
Immunopathogenesis of brain abscess.
Kielian, T. (2004) · Journal of Neuroinflammation · doi:10.1186/1742-2094-1-16 · Cited by 111
Complement receptor 3 mediates NADPH oxidase activation and dopaminergic neurodegeneration through a Src-Erk-dependent pathway
Hou, L., Wang, K., Zhang, C., Sun, F., Che, Y., Zhao, X., Zhang, D., Li, H., & Wang, Q. (2018) · Redox Biology · doi:10.1016/j.redox.2017.09.017 · Cited by 104
Role of transient receptor potential ankyrin 1 channels in Alzheimer’s disease
Lee, K.-I., Lee, H., Lin, H., Tsay, H.-J., Tsai, F.-C., Shyue, S., & Lee, T. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0557-z · Cited by 113
Extracellular aggregated Cu/Zn superoxide dismutase activates microglia to give a cytotoxic phenotype
Roberts, K., Zeineddine, R., Corcoran, L., Li, W., Campbell, I. L., & Yerbury, J. J. (2012) · Glia · doi:10.1002/glia.22444 · Cited by 107
MicroRNA-146a switches microglial phenotypes to resist the pathological processes and cognitive degradation of Alzheimer's disease
Liang, C., Zou, T., Zhang, M., Fan, W., Zhang, T., Jiang, Y., Cai, Y., Chen, F., Chen, X., Sun, Y., et al. (2021) · Theranostics · doi:10.7150/thno.53418 · Cited by 106
Blood–brain barrier and blood–cerebrospinal fluid barrier in normal and pathological conditions
Ueno, M., Chiba, Y., Murakami, R., Matsumoto, K., Kawauchi, M., & Fujihara, R. (2016) · Brain Tumor Pathology · doi:10.1007/s10014-016-0255-7 · Cited by 106
Microglia-targeting nanotherapeutics for neurodegenerative diseases
Zhao, N., Francis, N. L., Calvelli, H. R., & Moghe, P. V. (2020) · APL Bioengineering · doi:10.1063/5.0013178 · Cited by 104
Oxidative insults to neurons and synapse are prevented by aged garlic extract and S-allyl-l-cysteine treatment in the neuronal culture and APP-Tg mouse model
Ray, B., Chauhan, N. B., & Lahiri, D. K. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07145.x · Cited by 104
Alpha-synuclein and beta-amyloid – different targets, same players: calcium, free radicals and mitochondria in the mechanism of neurodegeneration
Angelova, P. R., & Abramov, A. Y. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.07.103 · Cited by 98
A key role for the microglial NADPH oxidase in APP-dependent killing of neurons
Qin, B., Cartier, L., Dubois‐Dauphin, M., Li, B., Serrander, L., & Krause, K. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.036 · Cited by 99
Amyloid-β Induces Hepatic Insulin Resistance by Activating JAK2/STAT3/SOCS-1 Signaling Pathway
Zhang, Y., Zhou, B., Zhang, F., Wu, J., Hu, Y., Liu, Y., & Zhai, Q. (2012) · Diabetes · doi:10.2337/db11-0499 · Cited by 92
The Role of Neurovascular System in Neurodegenerative Diseases
Ahmad, A., Patel, V., Xiao, J., & Khan, M. M. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02023-z · Cited by 97
A High Content Drug Screen Identifies Ursolic Acid as an Inhibitor of Amyloid β Protein Interactions with Its Receptor CD36
Wilkinson, K., Boyd, J. D., Glicksman, M. A., Moore, K. J., & Khoury, J. B. E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.232116 · Cited by 90
Suppression of iNOS expression by fucoidan is mediated by regulation of p38 MAPK, JAK/STAT, AP-1 and IRF-1, and depends on up-regulation of scavenger receptor B1 expression in TNF-α- and IFN-γ-stimulated C6 glioma cells
Do, H., Pyo, S., & Sohn, E. (2009) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2009.03.013 · Cited by 88
Transforming growth factor‐β stimulates β amyloid uptake by microglia through Smad3‐dependent mechanisms
Tichauer, J. E., & Rommy von Bernhardi, M. (2012) · Journal of Neuroscience Research · doi:10.1002/jnr.23082 · Cited by 91
The Multifunctionality of CD36 in Diabetes Mellitus and Its Complications—Update in Pathogenesis, Treatment and Monitoring
Puchałowicz, K., & Rać, M. E. (2020) · Cells · doi:10.3390/cells9081877 · Cited by 88
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Driscoll, W. S., Vaisar, T., Tang, J., Wilson, C. L., & Raines, E. W. (2013) · Circulation Research · doi:10.1161/circresaha.112.300683 · Cited by 87
Metabolic regulation of microglial phagocytosis: Implications for Alzheimer's disease therapeutics
Lepiarz-Raba, I., Gbadamosi, I., Florea, R., Paolicelli, R. C., & Jawaid, A. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00382-w · Cited by 90
CXCL1 Contributes to β-Amyloid-Induced Transendothelial Migration of Monocytes in Alzheimer’s Disease
Zhang, K., Li, T. X., Liu, L., Feng, Y., Dong, Y.-B., Li, B., Shang, D., Fang, W., Cao, Y., & Chen, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072744 · Cited by 89
Blood‐brain barrier damage in vascular dementia
Ueno, M., Chiba, Y., Matsumoto, K., Murakami, R., Fujihara, R., Kawauchi, M., Miyanaka, H., & Nakagawa, T. (2015) · Neuropathology · doi:10.1111/neup.12262 · Cited by 90
Neurotoxicity by microglia: Mechanisms and potential therapeutic strategy
Takeuchi, H. (2010) · Clinical and Experimental Neuroimmunology · doi:10.1111/j.1759-1961.2009.00001.x · Cited by 88
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Fanlo-Ucar, H., Picón-Pagès, P., Herrera-Fernández, V., ILL‐Raga, G., & Muñoz, F. J. (2024) · Antioxidants · doi:10.3390/antiox13101208 · Cited by 94
CD36 in Alzheimer’s Disease: An Overview of Molecular Mechanisms and Therapeutic Targeting
Dobri, A.-M., Dudău, M., Enciu, A., & Hinescu, M. E. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.11.003 · Cited by 83
Genetic deletion of CD36 enhances injury after acute neonatal stroke
Woo, M., Wang, X., Faustino, J. V., Derugin, N., Wendland, M. F., Zhou, P., Iadecola, C., & Vexler, Z. S. (2012) · Annals of Neurology · doi:10.1002/ana.23727 · Cited by 82
The Evolving Biology of Microglia in Alzheimer's Disease
Malm, T. M., Jay, T. R., & Landreth, G. E. (2015) · Neurotherapeutics · doi:10.1007/s13311-014-0316-8 · Cited by 85
Activation of Human Platelets by Misfolded Proteins
Herczenik, E., Bouma, B., Korporaal, S. J. A., Strangi, R. D., Zeng, Q., Gros, P., Eck, M. V., van Berkel, T. J. C., Gebbink, M. F. B. G., & Akkerman, J. N. (2007) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.107.143479 · Cited by 86
Migration of blood cells to β-amyloid plaques in Alzheimer's disease
Hohsfield, L. A., & Humpel, C. (2015) · Experimental Gerontology · doi:10.1016/j.exger.2015.03.002 · Cited by 79
Microglia as a critical player in both developmental and late-life CNS pathologies
Derecki, N. C., Katzmarski, N., Kipnis, J., & Meyer-Luehmann, M. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1321-z · Cited by 78
Menopause leads to elevated expression of macrophage-associated genes in the aging frontal cortex: rat and human studies identify strikingly similar changes
Sárvári, M., Hrabovszky, E., Kalló, I., Solymosi, N., Likó, I., Berchtold, N. C., Cotman, C. W., & Liposits, Z. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-264 · Cited by 81
β−Amyloid exacerbates inflammation in astrocytes lacking fatty acid amide hydrolase through a mechanism involving PPAR‐α, PPAR‐γ and TRPV1, but not CB1 or CB2 receptors
Benito, C., Tolón, R. M., Castillo, A. I., Ruiz‐Valdepeñas, L., Martínez-Orgado, J. A., Fernández, J., Vázquez, C., Cravatt, B. F., & Romero, J. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.01889.x · Cited by 81
Systemic Immune Responses in Alzheimer's Disease: In Vitro Mononuclear Cell Activation and Cytokine Production
Pellicanò, M., Bulati, M., Buffa, S., Barbagallo, M., Di Prima, A., Misiano, G., Picone, P., Di Carlo, M., Nuzzo, D., Candore, G., et al. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-091714 · Cited by 86
Improving outcomes in intracerebral hemorrhage through microglia/macrophage-targeted IL-10 delivery with phosphatidylserine liposomes
Han, R., Lan, X., Han, Z., Ren, H., Aafreen, S., Wang, W., Hou, Z., Zhu, T., Qian, A., Han, X., et al. (2023) · Biomaterials · doi:10.1016/j.biomaterials.2023.122277 · Cited by 80
Untangling the role of amyloid in atherosclerosis
Howlett, G. J., & Moore, K. J. (2006) · Current Opinion in Lipidology · doi:10.1097/01.mol.0000245260.63505.4f · Cited by 79
Desacyl‐ghrelin and synthetic GH‐secretagogues modulate the production of inflammatory cytokines in mouse microglia cells stimulated by β‐amyloid fibrils
Bulgarelli, I., Tamiazzo, L., Bresciani, E., Rapetti, D., Caporali, S., Lattuada, D., Locatelli, V., & Torsello, A. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22088 · Cited by 78
Microglial cells in neurodegenerative disorders.
Wojtera, M., Sikorska, B., Sobów, T., & Liberski, P. P. (2005) · PubMed · Cited by 78
Gut Microbiota Disorder, Gut Epithelial and Blood–Brain Barrier Dysfunctions in Etiopathogenesis of Dementia: Molecular Mechanisms and Signaling Pathways
Welcome, M. O. (2019) · NeuroMolecular Medicine · doi:10.1007/s12017-019-08547-5 · Cited by 77
Cholesterol-related genes in Alzheimer's disease
Wollmer, M. A. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2010.05.009 · Cited by 78
Misfolded Truncated Protein τ Induces Innate Immune Response via MAPK Pathway
Kovac, A., Zilka, N., Kazmerova, Z., Cente, M., Zilkova, M., & Novak, M. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100216 · Cited by 75
Dyslipidemia and Dementia: Current Epidemiology, Genetic Evidence, and Mechanisms Behind the Associations
Reitz, C. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110599 · Cited by 76
Fatty acid transporting proteins: Roles in brain development, aging, and stroke
Zhang, W., Chen, R., Yang, T., Xu, N., Chen, J., Gao, Y., & Stetler, R. A. (2017) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2017.04.004 · Cited by 79
Danger-Sensing/Patten Recognition Receptors and Neuroinflammation in Alzheimer’s Disease
Chiarini, A., Armato, U., Hu, P., & Prà, I. D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239036 · Cited by 77
Innate Immunity in Alzheimer’s Disease: A Complex Affair
Guillot‐Sestier, M., & Town, T. (2013) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527311312050008 · Cited by 72
Microglia Ontology and Signaling
ElAli, A., & Rivest, S. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00072 · Cited by 75
Interaction of neurons and astrocytes underlies the mechanism of Aβ-induced neurotoxicity
Angelova, P. R., & Abramov, A. Y. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140153 · Cited by 71
Analysis of Protein Levels of 24 Cytokines in Scrapie Agent-Infected Brain and Glial Cell Cultures from Mice Differing in Prion Protein Expression Levels
Tribouillard‐Tanvier, D., Striebel, J. F., Peterson, K. E., & Chesebro, B. W. (2009) · Journal of Virology · doi:10.1128/jvi.01413-09 · Cited by 73
Proprotein Convertase Subtilisin/Kexin Type 9, Brain Cholesterol Homeostasis and Potential Implication for Alzheimer’s Disease
Adorni, M. P., Ruscica, M., Ferri, N., Bernini, F., & Zimetti, F. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00120 · Cited by 67
The Participation of Microglia in Neurogenesis: A Review
Pérez-Rodríguez, D. R., Blanco‐Luquin, I., & Mendióroz, M. (2021) · Brain Sciences · doi:10.3390/brainsci11050658 · Cited by 74
CD36 overexpression in human brain correlates with β-amyloid deposition but not with Alzheimer's disease
Ricciarelli, R., d'Abramo, C., Zingg, J.-M., Giliberto, L., Markesbery, W., Azzi, A., Marinari, U. M., Pronzato, M. A., & Tabaton, M. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.01.007 · Cited by 66
Therapeutic Potential of Ursolic Acid to Manage Neurodegenerative and Psychiatric Diseases
Ramos-Hryb, A. B., Pazini, F. L., Kaster, M. P., & Rodrigues, A. L. S. (2017) · CNS Drugs · doi:10.1007/s40263-017-0474-4 · Cited by 66
Modulation of β-Amyloid Fibril Formation in Alzheimer’s Disease by Microglia and Infection
Brown, M. R., Radford, S. E., & Hewitt, E. W. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.609073 · Cited by 67
Calprotectin in microglia from frontal cortex is up‐regulated in schizophrenia: evidence for an inflammatory process?
Foster, F., Kandanearatchi, A., Beasley, C. L., Williams, B. P., Khan, N., Fagerhol, M. K., & Everall, I. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.05219.x · Cited by 62
Functional and Phenotypic Diversity of Microglia: Implication for Microglia-Based Therapies for Alzheimer’s Disease
Xu, Y., Au, N. P. B., & Ma, C. H. E. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.896852 · Cited by 68
Microglial Activation in Metal Neurotoxicity: Impact in Neurodegenerative Diseases
Martínez-Hernández, M. I., Acosta‐Saavedra, L. C., Hernández‐Kelly, L. C., Loaeza‐Loaeza, J., & Ortega, A. (2023) · BioMed Research International · doi:10.1155/2023/7389508 · Cited by 63
A novel phosphodiesterase-5 Inhibitor: Yonkenafil modulates neurogenesis, gliosis to improve cognitive function and ameliorates amyloid burden in an APP/PS1 transgenic mice model
Zhu, L., Yang, J., Xue, X., Dong, Y., Liu, Y., Miao, F.-R., Wang, Y., Xue, H., & Wu, C. (2015) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2015.07.002 · Cited by 59
Presenilin 2 Is the Predominant γ-Secretase in Microglia and Modulates Cytokine Release
Jayadev, S., Case, A., Eastman, A. J., Nguyen, H., Pollak, J., Wiley, J. C., Möller, T., Morrison, R. S., & Garden, G. A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015743 · Cited by 60
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McKimmie, C. S., Roy, D., Forster, T., & Fazakerley, J. K. (2006) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2006.03.012 · Cited by 51
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Tedeschi, P., Nigro, M., Travagli, A., Catani, M., Cavazzini, A., Merighi, S., & Gessi, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23136950 · Cited by 61
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Qin, M., Wang, L., Li, F., Yang, M., Song, L., Tian, F., Yukht, A., Shah, P. K., Rothenberg, M. E., & Sharifi, B. G. (2017) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2017.05.011 · Cited by 58
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CD36 in the periphery and brain synergizes in stroke injury in hyperlipidemia
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Macrophage Scavenger Receptor A Mediates Adhesion to Apolipoproteins A-I and E
Neyen, C. D., Plüddemann, A., Roversi, P., Thomas, B., Cai, L., van der Westhuyzen, D. R., Sim, R. B., & Gordon, S. (2009) · Biochemistry · doi:10.1021/bi9013769 · Cited by 56
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“This receptor has been reported to act as an inflammatory conductor for Aß, leading to the production of ROS and proinflammatory cytokines upon the interaction of fibrillar Aß with microglial or macrophage CD36 (Coraci et al., 2002; Bamberger et al., 2003; El Khoury et al., 2003; Demers et al., 2004).”
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Authors: Coraci, I. S., Husemann, J., Berman, J. W., Hulette, C., Dufour, J. H., Campanella, G. K., Luster, A. D., Silverstein, S. C., & El Khoury, J. B.
Affiliations: Columbia University Irving Medical Center (US)
Albert Einstein College of Medicine (US)
Duke University (US)
Harvard University (US)
ORCID: Berman, Joan W.
Luster, Andrew D.
Venue: The American Journal of Pathology
Publisher: Elsevier BV
Published: 2002-01
Volume: 160
Issue: 1
Pages: 101-112
ISSN: 0002-9440 (ISSN-L)
DOI: 10.1016/s0002-9440(10)64354-4
PMC: PMC1867121
OpenAlex: W2096519700
Cited by: 398
References: 56
Citations by year: 2026: 6 · 2025: 18 · 2024: 13 · 2023: 10 · 2022: 16 · 2021: 18 · 2020: 29 · 2019: 17 · 2018: 10 · 2017: 16 · 2016: 16 · 2015: 18 · 2014: 29 · 2013: 18 · 2012: 33
FWCI: 7.59
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: American Journal Of Pathology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of Neurological Disorders and Stroke
National Heart, Lung, and Blood Institute (PO1-AG02219, P50-AG05138)
Alzheimer's Association (R37-AI 20516)
National Institute of Allergy and Infectious Diseases (HL43310)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
Keywords: CD36, scavenger receptor class B, microglia, Alzheimer's disease, amyloid-beta fibrils, reactive oxygen species, hydrogen peroxide production, amyloid plaques, vascular endothelial cells, monoclonal antibody inhibition
MeSH terms: Alzheimer Disease, Animals, Antibodies, Brain, Cell Adhesion, Cell Line, Cell Line, Transformed, Fetus, Humans, Macrophages, Membrane Proteins, Peptide Fragments, Peroxides, Phagocytes, Receptors, Immunologic, Amyloid beta-Peptides, Reactive Oxygen Species, Microglia, Receptors, Lipoprotein, CD36 Antigens, Receptors, Scavenger, Scavenger Receptors, Class A, Scavenger Receptors, Class B, Mice, Rats

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CD36, a Class B Scavenger Receptor, Is Expressed on Microglia in Alzheimer's Disease Brains and Can Mediate Production of Reactive Oxygen Species in Response to β-Amyloid Fibrils

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