Human α-Synuclein-Harboring Familial Parkinson's Disease-Linked Ala-53 → Thr Mutation Causes Neurodegenerative Disease with α-Synuclein Aggregation in Transgenic Mice

Mutations in α-synuclein (α-Syn) cause Parkinson's disease (PD) in a small number of pedigrees with familial PD. Moreover, α-Syn accumulates as a major component of Lewy bodies and Lewy neurites, intraneuronal inclusions that are neuropathological hallmarks of PD. To better understand the patho...

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Published in:Proceedings of the National Academy of Sciences - PNAS 2002-06, Vol.99 (13), p.8968-8973
Main Authors: Lee, Michael K., Stirling, Wanda, Xu, Yanqun, Xu, Xueying, Qui, Dike, Mandir, Allen S., Dawson, Ted M., Copeland, Neal G., Jenkins, Nancy A., Price, Don L.
Format: Article
Language:English
Subjects:
Alanine - genetics
alpha-Synuclein
Animals
Biological Sciences
Brain
Humans
Messenger RNA
Mice
Mice, Transgenic
Mutation
Nerve Tissue Proteins - chemistry
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Nervous system diseases
Neurodegenerative diseases
Neurons
Parkinson Disease - genetics
Parkinson Disease - pathology
Parkinson's disease
Pathology
Reverse Transcriptase Polymerase Chain Reaction
Rodents
Synucleins
Threonine - genetics
Transgenes
Transgenic animals
Ubiquitins
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container_issue 13
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container_title Proceedings of the National Academy of Sciences - PNAS
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creator Lee, Michael K.
Stirling, Wanda
Xu, Yanqun
Xu, Xueying
Qui, Dike
Mandir, Allen S.
Dawson, Ted M.
Copeland, Neal G.
Jenkins, Nancy A.
Price, Don L.
description Mutations in α-synuclein (α-Syn) cause Parkinson's disease (PD) in a small number of pedigrees with familial PD. Moreover, α-Syn accumulates as a major component of Lewy bodies and Lewy neurites, intraneuronal inclusions that are neuropathological hallmarks of PD. To better understand the pathogenic relationship between alterations in the biology of α-Syn and PD-associated neurodegeneration, we generated multiple lines of transgenic mice expressing high levels of either wild-type or familial PD-linked Ala-30 → Pro (A30P) or Ala-53 → Thr (A53T) human α-Syns. The mice expressing the A53T human α-Syn, but not wild-type or the A30P variants, develop adult-onset neurodegenerative disease with a progressive motoric dysfunction leading to death. Pathologically, affected mice exhibit neuronal abnormalities (in perikarya and neurites) including pathological accumulations of α-Syn and ubiquitin. Consistent with abnormal neuronal accumulation of α-Syn, brain regions with pathology exhibit increases in detergent-insoluble α-Syn and α-Syn aggregates. Our results demonstrate that the A53T mutant α-Syn causes significantly greater in vivo neurotoxicity as compared with other α-Syn variants. Further, α-Syn-dependent neurodegeneration is associated with abnormal accumulation of detergent-insoluble α-Syn.
doi_str_mv 10.1073/pnas.132197599
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Our results demonstrate that the A53T mutant α-Syn causes significantly greater in vivo neurotoxicity as compared with other α-Syn variants. 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E-mail: mklee@jhmi.edu.</notes><notes>Edited by Solomon H. Snyder, Johns Hopkins University School of Medicine, Baltimore, MD, and approved May 2, 2002</notes><abstract>Mutations in α-synuclein (α-Syn) cause Parkinson's disease (PD) in a small number of pedigrees with familial PD. Moreover, α-Syn accumulates as a major component of Lewy bodies and Lewy neurites, intraneuronal inclusions that are neuropathological hallmarks of PD. To better understand the pathogenic relationship between alterations in the biology of α-Syn and PD-associated neurodegeneration, we generated multiple lines of transgenic mice expressing high levels of either wild-type or familial PD-linked Ala-30 → Pro (A30P) or Ala-53 → Thr (A53T) human α-Syns. The mice expressing the A53T human α-Syn, but not wild-type or the A30P variants, develop adult-onset neurodegenerative disease with a progressive motoric dysfunction leading to death. Pathologically, affected mice exhibit neuronal abnormalities (in perikarya and neurites) including pathological accumulations of α-Syn and ubiquitin. Consistent with abnormal neuronal accumulation of α-Syn, brain regions with pathology exhibit increases in detergent-insoluble α-Syn and α-Syn aggregates. Our results demonstrate that the A53T mutant α-Syn causes significantly greater in vivo neurotoxicity as compared with other α-Syn variants. Further, α-Syn-dependent neurodegeneration is associated with abnormal accumulation of detergent-insoluble α-Syn.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>12084935</pmid><doi>10.1073/pnas.132197599</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
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subjects Alanine - genetics
alpha-Synuclein
Animals
Biological Sciences
Brain
Humans
Messenger RNA
Mice
Mice, Transgenic
Mutation
Nerve Tissue Proteins - chemistry
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Nervous system diseases
Neurodegenerative diseases
Neurons
Parkinson Disease - genetics
Parkinson Disease - pathology
Parkinson's disease
Pathology
Reverse Transcriptase Polymerase Chain Reaction
Rodents
Synucleins
Threonine - genetics
Transgenes
Transgenic animals
Ubiquitins
title Human α-Synuclein-Harboring Familial Parkinson's Disease-Linked Ala-53 → Thr Mutation Causes Neurodegenerative Disease with α-Synuclein Aggregation in Transgenic Mice
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