Ceruloplasmin dysfunction and therapeutic potential for Parkinson disease

Basal Lipid Peroxidation in Substantia Nigra Is Increased in Parkinson's Disease

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C ERULOPLASMIN M ETABOLISM AND F UNCTION

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Iron-Export Ferroxidase Activity of β-Amyloid Precursor Protein Is Inhibited by Zinc in Alzheimer's Disease

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The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum.

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Genetic or Pharmacological Iron Chelation Prevents MPTP-Induced Neurotoxicity In Vivo

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Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export

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The A53T α-Synuclein Mutation Increases Iron-Dependent Aggregation and Toxicity

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Ceruloplasmin regulates iron levels in the CNS and prevents free radical injury

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Individual dopaminergic neurons show raised iron levels in Parkinson disease

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Sequestration of iron by Lewy bodies in Parkinson's disease

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Ceruloplasmin replacement therapy ameliorates neurological symptoms in a preclinical model of aceruloplasminemia

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Restless Legs Syndrome and Parkinson Disease: A Causal Relationship Between the Two Disorders?

Ferini‐Strambi, L., Carli, G., Casoni, F. M., & Galbiati, A. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00551 · Cited by 57

Ferroptosis Is Regulated by Mitochondria in Neurodegenerative Diseases

Zhou, J.-P., Jin, Y., Lei, Y.-H., Liu, T., Wan, Z., Meng, H., & Wang, H. (2020) · Neurodegenerative Diseases · doi:10.1159/000510083 · Cited by 57

Prognostic Value of Elevated Serum Ceruloplasmin Levels in Patients With Heart Failure

Hammadah, M., Fan, Y., Wu, Y., Hazen, S. L., & Tang, W. H. W. (2014) · Journal of Cardiac Failure · doi:10.1016/j.cardfail.2014.08.001 · Cited by 55

Copper and ceruloplasmin dyshomeostasis in serum and cerebrospinal fluid of multiple sclerosis subjects

Riccardis, L. D., Buccolieri, A., Muci, M., Pitotti, E., Robertis, F. D., Trianni, G., Manno, D. E., & Maffia, M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.03.007 · Cited by 56

Inhibition of ACSL4 Alleviates Parkinsonism Phenotypes by Reduction of Lipid Reactive Oxygen Species

Tang, F., Zhou, L.-Y., Li, P., Jiao, L., Chen, K., Guo, Y., Ding, X., He, S., Dong, B., Xu, R., et al. (2023) · Neurotherapeutics · doi:10.1007/s13311-023-01382-4 · Cited by 53

Reactivity of copper–α-synuclein peptide complexes relevant to Parkinson’s disease

Dell’Acqua, S., Pirota, V., Anzani, C., Rocco, M. M., Nicolis, S., Valensin, D., Monzani, E., & Casella, L. (2015) · Metallomics · doi:10.1039/c4mt00345d · Cited by 51

A Proposed Mechanism for Neurodegeneration in Movement Disorders Characterized by Metal Dyshomeostasis and Oxidative Stress

Trist, B. G., Hare, D. J., & Double, K. L. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.05.004 · Cited by 51

Overdosing on iron: Elevated iron and degenerative brain disorders

D’Mello, S. R., & Kindy, M. S. (2020) · Experimental Biology and Medicine · doi:10.1177/1535370220953065 · Cited by 49

The iron regulatory capability of the major protein participants in prevalent neurodegenerative disorders

Wong, B. X. W., & Duce, J. A. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00081 · Cited by 50

Serum microRNA-133b is associated with low ceruloplasmin levels in Parkinson's disease

Zhao, N., Jin, L., Fei, G., Zheng, Z.-Y., & Zhong, C. (2014) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2014.08.016 · Cited by 48

The Ferroxidase Hephaestin But Not Amyloid Precursor Protein is Required for Ferroportin-Supported Iron Efflux in Primary Hippocampal Neurons

Ji, C., Steimle, B. L., Bailey, D. K., & Kosman, D. J. (2017) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-017-0568-z · Cited by 50

Iron Dysregulation in Parkinson’s Disease: Focused on the Autophagy–Lysosome Pathway

Chen, L., Huang, Y., Cui, J., Song, N., & Xie, J. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00390 · Cited by 47

Correlation of Ferroptosis and Other Types of Cell Death in Neurodegenerative Diseases

Dang, X., Huan, X., Du, X., Chen, X., Bi, M., Yan, C., Jiao, Q., & Jiang, H. F. (2022) · Neuroscience Bulletin · doi:10.1007/s12264-022-00861-6 · Cited by 46

Research progress in the molecular mechanism of ferroptosis in Parkinson's disease and regulation by natural plant products

Yang, K., Zeng, L., Zeng, J., Deng, Y., Wang, S., Xu, H., He, Q., Yuan, M., Luo, Y., Ge, A., et al. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102063 · Cited by 46

Evidence for disrupted copper availability in human spinal cord supports CuII(atsm) as a treatment option for sporadic cases of ALS

Hilton, J. B. W., Kysenius, K., Liddell, J. R., Mercer, S. W., Paul, B. T., Beckman, J. S., McLean, C., White, A. R., Donnelly, P. S., Bush, A. I., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-55832-w · Cited by 45

Serotonergic markers in Parkinson's disease and levodopa‐induced dyskinesias

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Ceruloplasmin functional changes in Parkinson’s disease-cerebrospinal fluid

Barbariga, M., Curnis, F., Andolfo, A., Zanardi, A., Lazzaro, M., Conti, A., Magnani, G., Volonté, M. A., Ferrari, L. D., Comı, G., et al. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0055-2 · Cited by 47

Alpha-synuclein inhibits Snx3–retromer-mediated retrograde recycling of iron transporters in S. cerevisiae and C. elegans models of Parkinson’s disease

Patel, D., Xu, C., Nagarajan, S., Liu, Z., Hemphill, W. O., Shi, R., Uversky, V. N., Caldwell, G. A., Caldwell, K. A., & Witt, S. N. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy059 · Cited by 44

Association of metals with the risk and clinical characteristics of Parkinson's disease

Kim, M., Oh, S.-B., Kim, J., Kim, K., Ryu, H., Kim, M. S., Ayton, S., Bush, A. I., Lee, J., & Chung, S. J. (2018) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2018.05.022 · Cited by 44

Widespread Decreases in Cerebral Copper Are Common to Parkinson's Disease Dementia and Alzheimer's Disease Dementia

Scholefield, M., Church, S. J., Xu, J., Patassini, S., Roncaroli, F., Hooper, N. M., Unwin, R. D., & Cooper, G. J. S. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.641222 · Cited by 44

Biomarkers in diabetic neuropathy

Adki, K. M., & Kulkarni, Y. A. (2020) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2020.1837183 · Cited by 42

Transferrin protects against Parkinsonian neurotoxicity and is deficient in Parkinson’s substantia nigra

Ayton, S., Lei, P., McLean, C., Bush, A. I., & Finkelstein, D. I. (2016) · Signal Transduction and Targeted Therapy · doi:10.1038/sigtrans.2016.15 · Cited by 42

Ferroptosis in Neurological Disease

David, S., Ryan, F., Jhelum, P., & Kroner, A. (2022) · The Neuroscientist · doi:10.1177/10738584221100183 · Cited by 43

Mitochondrial ferritin suppresses MPTP-induced cell damage by regulating iron metabolism and attenuating oxidative stress.

You, L., Li, Z., Duan, X.-L., Zhao, B.-L., Chang, Y.-Z., & Shi, Z.-H. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.023 · Cited by 38

Alpha-synuclein-induced oxidative stress correlates with altered superoxide dismutase and glutathione synthesis in human neuroblastoma SH-SY5Y cells

Perfeito, R., Ribeiro, M., & Rego, A. C. (2016) · Archives of Toxicology · doi:10.1007/s00204-016-1788-6 · Cited by 41

Ceruloplasmin, a Potential Therapeutic Agent for Alzheimer's Disease

Zhao, Y., Zhang, L.-H., Yu, P.-P., Gou, Y.-J., Zhao, J., You, L., Wang, Z., Zheng, X., Yan, L., Yu, P., et al. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6883 · Cited by 42

Shared perturbations in the metallome and metabolome of Alzheimer’s, Parkinson’s, Huntington’s, and dementia with Lewy bodies: A systematic review

Scholefield, M., Unwin, R. D., & Cooper, G. J. S. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101152 · Cited by 39

Ferroptosis—A Novel Mechanism With Multifaceted Actions on Stroke

Fang, X., Ding, S.-Y., Du, X., Wang, J.-H., & Li, X. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.881809 · Cited by 42

Cerebrospinal fluid ceruloplasmin levels predict cognitive decline and brain atrophy in people with underlying β-amyloid pathology

Diouf, I., Bush, A. I., & Ayton, S. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104810 · Cited by 38

Inhibition of copper transporter 1 prevents α-synuclein pathology and alleviates nigrostriatal degeneration in AAV-based mouse model of Parkinson's disease

Gou, D.-H., Huang, T., Li, W., Gao, X.-D., Haikal, C., Wang, X.-H., Song, D., Liang, X., Zhu, L., Tang, Y. C., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101795 · Cited by 40

Ferroptosis-Related Genes in Neurodevelopment and Central Nervous System

Kim, S.-W., Kim, S.-W., Kim, Y.-J., & An, J. (2021) · Biology · doi:10.3390/biology10010035 · Cited by 40

The divergent effects of astrocyte ceruloplasmin on learning and memory function in young and old mice

Li, Z., Li, H., Kang, S., Cui, Y., Zheng, H., Wang, P., Han, K., Yu, P., & Chang, Y. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05459-4 · Cited by 38

Parkinson Disease Signaling Pathways, Molecular Mechanisms, and Potential Therapeutic Strategies: A Comprehensive Review

Khan, M. S., Nasiripour, S., & Bopassa, J. C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26136416 · Cited by 48

Cp/Heph mutant mice have iron‐induced neurodegeneration diminished by deferiprone

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Insight Into the Role of Ferroptosis in Non-neoplastic Neurological Diseases

Lei, J., Chen, Z., Song, S., Sheng, C., Song, S., & Zhu, J. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00231 · Cited by 37

Copper homeostasis and the ubiquitin proteasome system

Zhang, B., & Burke, R. (2023) · Metallomics · doi:10.1093/mtomcs/mfad010 · Cited by 36

Oxidation-induced Structural Changes of Ceruloplasmin Foster NGR Motif Deamidation That Promotes Integrin Binding and Signaling

Barbariga, M., Curnis, F., Spitaleri, A., Andolfo, A., Zucchelli, C., Lazzaro, M., Magnani, G., Musco, G., Corti, A., & Alessio, M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.520981 · Cited by 35

Effects of hemochromatosis and transferrin gene mutations on peripheral iron dyshomeostasis in mild cognitive impairment and Alzheimer's and Parkinson's diseases

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Occupational Metal Exposure and Parkinsonism

Caudle, W. M. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-60189-2_7 · Cited by 35

Effects of Neonatal Iron Feeding and Chronic Clioquinol Administration on the Parkinsonian Human A53T Transgenic Mouse

Billings, J. L., Hare, D. J., Nurjono, M., Volitakis, I., Cherny, R. A., Bush, A. I., Adlard, P. A., & Finkelstein, D. I. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00305 · Cited by 35

Ferroptosis-related factors in the substantia nigra are associated with Parkinson’s disease

Liu, L., Cui, Y., Chang, Y., & Yu, P. (2023) · Scientific Reports · doi:10.1038/s41598-023-42574-4 · Cited by 39

Combined chronic copper exposure and aging lead to neurotoxicity in vivo

González-Alcocer, A., Gopar‐Cuevas, Y., Soto‐Domínguez, A., Castillo-Velázquez, U., Loera‐Arias, M. D. J., Cárdenas, O. S., Montes‐de‐Oca‐Luna, R., García‐García, A., & Rodríguez‐Rocha, H. (2023) · NeuroToxicology · doi:10.1016/j.neuro.2023.02.002 · Cited by 33

Signaling Integration of Hydrogen Sulfide and Iron on Cellular Functions

Arif, H. M., Qian, Z., & Wang, R. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0203 · Cited by 33

Switching on Endogenous Metal Binding Proteins in Parkinson’s Disease

McLeary, F. A., Rcom-H'cheo-Gauthier, A. N., Goulding, M., Radford, R. A. W., Okita, Y., Faller, P., Chung, R. S., & Pountney, D. L. (2019) · Cells · doi:10.3390/cells8020179 · Cited by 31

A comparison of ceruloplasmin to biological polyanions in promoting the oxidation of Fe2+ under physiologically relevant conditions

Wong, B. X. W., Ayton, S., Lam, L. Q., Lei, P., Adlard, P. A., Bush, A. I., & Duce, J. A. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.08.006 · Cited by 32

Copper toxicity and deficiency: the vicious cycle at the core of protein aggregation in ALS

Min, J.-H., Sarlus, H., & Harris, R. A. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1408159 · Cited by 31

The role of iron transporters and regulators in Alzheimer’s disease and Parkinson’s disease: Pathophysiological insights and therapeutic prospects

Tian, S., Wang, B., Ding, Y., Zhang, Y. L., Yu, P., Chang, Y.-Z., & Gao, G. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117419 · Cited by 29

Analogues of desferrioxamine B designed to attenuate iron-mediated neurodegeneration: synthesis, characterisation and activity in the MPTP-mouse model of Parkinson's disease

Gotsbacher, M. P., Telfer, T. J., Witting, P. K., Double, K. L., Finkelstein, D. I., & Codd, R. (2017) · Metallomics · doi:10.1039/c7mt00039a · Cited by 28

Correction: Iron Accumulates in Huntington’s Disease Neurons: Protection by Deferoxamine

Chen, J., Marks, E. S., Lai, B. C. H., Zhang, Z., Duce, J. A., Lam, L. Q., Volitakis, I., Bush, A. I., Hersch, S. M., & Fox, J. H. (2013) · PLoS ONE · doi:10.1371/annotation/67f555f5-35b7-4468-8bab-26d518942803 · Cited by 29

Impaired skeletal muscle health in Parkinsonian syndromes: clinical implications, mechanisms and potential treatments

Murphy, K. T., & Lynch, G. S. (2023) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13312 · Cited by 27

Interrogating Parkinson's disease associated redox targets: Potential application of CRISPR editing

Artyukhova, M. A., Tyurina, Y. Y., Chu, C. T., Zharikova, T. M., Bayır, H., Kagan, V. E., & Timashev, P. S. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.06.007 · Cited by 26

Bioavailable Trace Metals in Neurological Diseases

Poujois, A., Devedjian, J.-C., Moreau, C., Devos, D., Chaine, P., Woimant, F., & Duce, J. A. (2016) · Current Treatment Options in Neurology · doi:10.1007/s11940-016-0426-1 · Cited by 26

Biomaterial and tissue-engineering strategies for the treatment of brain neurodegeneration

Martinez, B., & Peplow, P. V. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.336132 · Cited by 28

Copper increases the ability of 6‐hydroxydopamine to generate oxidative stress and the ability of ascorbate and glutathione to potentiate this effect: potential implications in Parkinson's disease

Cruces‐Sande, A., Méndez‐Álvarez, E., & Soto‐Otero, R. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14019 · Cited by 26

The role of ACSL4 in stroke: mechanisms and potential therapeutic target

Zhuo, B., Qin, C., Deng, S., Jiang, H., Si, S., Tao, F., Cai, F., & Meng, Z. (2024) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-024-05150-6 · Cited by 25

Metals in Alzheimer’s and Parkinson’s Disease: Relevance to Dementia with Lewy Bodies

McAllum, E. J., & Finkelstein, D. I. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0809-5 · Cited by 24

Ceruloplasmin is an endogenous protectant against kainate neurotoxicity

Shin, E., Jeong, J. H., Chung, C. K., Kim, D.-J., Wie, M., Park, E. S., Chung, Y. H., Nam, Y., Tran, T.-V., Lee, S. Y., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.03.031 · Cited by 24

New Insights into the Crosstalk between NMDARs and Iron: Implications for Understanding Pathology of Neurological Diseases

Xu, H., Jiang, H. F., & Xie, J. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00071 · Cited by 25

Predictive association of copper metabolism proteins with Alzheimer’s disease and Parkinson’s disease: a preliminary perspective

Pal, A., Kumar, A., & Prasad, R. (2014) · BioMetals · doi:10.1007/s10534-013-9702-7 · Cited by 23

Copper chelation and interleukin-6 proinflammatory cytokine effects on expression of different proteins involved in iron metabolism in HepG2 cell line

Bella, L. M. D., Alampi, R., Biundo, F., Toscano, G., & Felice, M. R. (2017) · BMC Biochemistry · doi:10.1186/s12858-017-0076-2 · Cited by 23

Neuroprotective approaches to halt Parkinson's disease progression

Sola, P., Krishnamurthy, P. T., Kumari, M., Byran, G., Gangadharappa, H. V., & Garikapati, K. K. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105380 · Cited by 21

Downregulation of thioredoxin reductase 1 expression in the substantia nigra pars compacta of Parkinson's disease mice.

Liu, Z., Jing, Y., Yin, J., Mu, J.-Y., Yao, T., & Gao, L. (2013) · PubMed Central · doi:10.3969/j.issn.1673-5374.2013.35.002 · Cited by 22

Effects of Excess Iron on the Retina: Insights From Clinical Cases and Animal Models of Iron Disorders

Shahandeh, A., Bui, B. V., Finkelstein, D. I., & Nguyen, C. T. O. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.794809 · Cited by 21

Unscrambling the Role of Redox-Active Biometals in Dopaminergic Neuronal Death and Promising Metal Chelation-Based Therapy for Parkinson’s Disease

González-Alcocer, A., Duarte-Jurado, A. P., Soto‐Domínguez, A., Loera‐Arias, M. D. J., Villarreal‐Silva, E. E., Cárdenas, O. S., Montes‐de‐Oca‐Luna, R., García‐García, A., & Rodríguez‐Rocha, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021256 · Cited by 22

Ceruloplasmin is Involved in the Nigral Iron Accumulation of 6-OHDA-Lesioned Rats

Wang, J., Bi, M., & Xie, J. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0161-2 · Cited by 22

Nutrient copper signaling promotes protein turnover by allosteric activation of ubiquitin E2D conjugasesPreprint

Opazo, C. M., Lotan, A., Xiao, Z., Zhang, B., Greenough, M. A., Lim, C. M., Trytell, H., Ramírez, A., Ukuwela, A. A., Mawal, C. H., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.15.431211 · Cited by 21

Therapeutic potential of iron modulating drugs in a mouse model of multiple system atrophy

Shukla, J. J., Stefanova, N., Bush, A. I., McColl, G., Finkelstein, D. I., & McAllum, E. J. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105509 · Cited by 19

Metal dyshomeostasis in the substantia nigra of patients with Parkinson's disease or multiple sclerosis

Carmona, A., Carboni, E., Gomes, L. C., Roudeau, S., Maass, F., Lenz, C., Ortega, R., & Lingor, P. (2024) · Journal of Neurochemistry · doi:10.1111/jnc.16040 · Cited by 20

Metallomics Applied to the Study of Neurodegenerative and Mental Diseases

Sussulini, A., & Hauser‐Davis, R. A. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-90143-5_2 · Cited by 21

The Compound ATH434 Prevents Alpha-Synuclein Toxicity in a Murine Model of Multiple System Atrophy

Finkelstein, D. I., Shukla, J. J., Cherny, R. A., Billings, J. L., Saleh, E., Stefanova, N., Barnham, K. J., & Adlard, P. A. (2021) · Journal of Parkinson s Disease · doi:10.3233/jpd-212877 · Cited by 20

What Is the Role of Ferroptosis in Neurodegeneration?

Benarroch, E. E. (2023) · Neurology · doi:10.1212/wnl.0000000000207730 · Cited by 26

An Unrecognized Fundamental Relationship between Neurotransmitters: Glutamate Protects against Catecholamine Oxidation

Wang, W., Wu, X., Yang, C. S., & Zhang, J. (2021) · Antioxidants · doi:10.3390/antiox10101564 · Cited by 23

The expression of ceruloplasmin in astrocytes is essential for postnatal myelination and myelin maintenance in the adult brain

Cheli, V. T., Sekhar, M., González, D. A. S., Angeliu, C. G., Denaroso, G., Smith, Z., Wang, C., & Paez, P. M. (2023) · Glia · doi:10.1002/glia.24424 · Cited by 18

Ferroptosis as a Therapeutic Target in Neurodegenerative Diseases: Exploring the Mechanisms and Potential of Treating Alzheimer's Disease and Parkinson's Disease

Zhong, H., Liu, H., & Fu, Q. (2024) · Protein and Peptide Letters · doi:10.2174/0109298665333926240927074528 · Cited by 21

Iron on trial: recasting the role of iron in neurodegeneration

Ayton, S., Moreau, C., Devos, D., & Bush, A. I. (2025) · Brain · doi:10.1093/brain/awaf398 · Cited by 18

Research progress on ferroptosis in the pathogenesis and treatment of neurodegenerative diseases

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Serum Ceruloplasmin Depletion is Associated With Magnetic Resonance Evidence of Widespread Accumulation of Brain Iron in Parkinson's Disease

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