Cited by 477Parkinson's Disease Mechanisms and TreatmentsNuclear Receptors and SignalingDeep Brain Stimulation and Movement Disorders

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Parkin-deficient mice are not a robust model of parkinsonism

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Perez, Francisco A., Palmiter, Richard D.·2005·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0409598102PMC PMC548311

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Abstract

Mutations in the human parkin gene cause autosomal recessive juvenile parkinsonism, a heritable form of Parkinson's disease (PD). To determine whether mutations in the mouse parkin gene ( Park2 ) also result in a parkinsonian phenotype, we generated mice with a targeted deletion of parkin exon 2. Using an extensive behavioral screen, we evaluated neurological function, motor ability, emotionality, learning, and memory in aged Parkin-deficient mice. The behavioral profile of Parkin-deficient mice on a B6;129S4 genetic background was strikingly similar to that of control mice, and most differences were not reproducible by using coisogenic mice on a 129S4 genetic background. Moreover, catecholamine levels in the striatum, olfactory bulb, and spinal cord of Parkin-deficient mice were normal. In contrast to previous studies using independently generated Parkin-deficient mice, we found no evidence for nigrostriatal, cognitive, or noradrenergic dysfunction. Understanding why Parkin-deficient mice do not exhibit robust signs of parkinsonism could advance knowledge and treatment of PD.

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Guide for the Care and Use of Laboratory Animals: Eighth Edition
(2011) · doi:10.17226/12910 · Cited by 16,199
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
Controlling the false discovery rate in behavior genetics research
Benjamini, Y., Drai, D., Elmer, G., Kafkafi, N., & Golani, I. (2001) · Behavioural Brain Research · doi:10.1016/s0166-4328(01)00297-2 · Cited by 4,146
Mitochondrial Dysfunction and Oxidative Damage in parkin-deficient Mice
Palacino, J. J., Sagi, D., Goldberg, M. S., Krauss, S., Motz, C., Wacker, M., Klose, J., & Shen, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401135200 · Cited by 995
Parkin functions as an E2-dependent ubiquitin– protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
Zhang, Y., Gao, J., Chung, K. K. K., Huang, H., Dawson, V. L., & Dawson, T. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.240347797 · Cited by 982
Parkin-deficient Mice Exhibit Nigrostriatal Deficits but Not Loss of Dopaminergic Neurons
Goldberg, M. S., Fleming, S. M., Palacino, J. J., Cepeda, C., Lam, H. A., Bhatnagar, A., Meloni, E. G., Wu, N., Ackerson, L. C., Klapstein, G. J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308947200 · Cited by 913
Gene-targeting studies of mammalian behavior: is it the mutation or the background genotype?
Gerlai, R. (1996) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)20020-7 · Cited by 881
Behavioral and functional analysis of mouse phenotype: SHIRPA, a proposed protocol for comprehensive phenotype assessment
Rogers, D. C., Fisher, E. M. C., Brown, S. D. M., Peters, J., Hunter, A. J., & Martin, J. E. (1997) · Mammalian Genome · doi:10.1007/s003359900551 · Cited by 795
Parkin Suppresses Unfolded Protein Stress-induced Cell Death through Its E3 Ubiquitin-protein Ligase Activity
Imai, Y., Soda, M., & Takahashi, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000447200 · Cited by 766
Genetic variation among 129 substrains and its importance for targeted mutagenesis in mice
Simpson, E. M., Linder, C. C., Sargent, E. E., Davisson, M. T., Mobraaten, L. E., & Sharp, J. J. (1997) · Nature Genetics · doi:10.1038/ng0597-19 · Cited by 684

Show all 45 references

Research works printed but not linked: 3

Schrag, A. (2004) J. Neurol. 251, 795-804.15258780
Ralph, R. J., Paulus, M. P. & Geyer, M. A. (2001) J. Pharmacol. Exp. Ther. 298, 148-155.11408536
Flaherty, L. (1981) in The Mouse in Biomedical Research, eds. Foster, H. L., Small, J. D. & Fox, J. G. (Academic, New York), Vol. 1, pp. 215-222.

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Authors: Perez, F. A., & Palmiter, R. D.
Affiliations: Howard Hughes Medical Institute (US)
ORCID: Perez, Francisco A.
Palmiter, Richard D.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2005-01-31
Volume: 102
Issue: 6
Pages: 2174-2179
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0409598102
PMC: PMC548311
OpenAlex: W2129698492
Cited by: 477
References: 45
Citations by year: 2026: 6 · 2025: 9 · 2024: 18 · 2023: 18 · 2022: 31 · 2021: 33 · 2020: 29 · 2019: 18 · 2018: 24 · 2017: 18 · 2016: 19 · 2015: 17 · 2014: 26 · 2013: 21 · 2012: 27
FWCI: 19.69
Type: journal article
Language: en
Open access: green
europepmc.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
Health Sciences › Medicine › Clinical Neurology › Deep Brain Stimulation and Movement Disorders
Keywords: Parkin, PARK2, juvenile parkinsonism, autosomal recessive juvenile parkinsonism, Parkinson's disease, exon 2 deletion, behavioral phenotypes, motor function, emotionality, learning and memory, catecholamine levels, noradrenergic dysfunction, genetic background effects, B6
MeSH terms: Amphetamines, Animals, Behavior, Animal, Disease Models, Animal, Emotions, Genotype, Humans, Learning, Memory, Mice, Inbred C57BL, Motor Activity, Nerve Tissue, Parkinson Disease, Phenotype, Mice, Knockout, Ubiquitin-Protein Ligases, Mice

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Parkin-deficient mice are not a robust model of parkinsonism

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