Modulation of α-Synuclein Aggregation by Dopamine: A Review
Parkinson’s disease (PD) is a progressive neurodegenerative disorder that is characterized by (1) the selective loss of dopaminergic neurons in the substantia nigra and (2) the deposition of misfolded α-synuclein (α-syn) as amyloid fibrils in the intracellular Lewy bodies in various region of the br...
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Veröffentlicht in: | Neurochemical research 2009-10, Vol.34 (10), p.1838-1846 |
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description | Parkinson’s disease (PD) is a progressive neurodegenerative disorder that is characterized by (1) the selective loss of dopaminergic neurons in the substantia nigra and (2) the deposition of misfolded α-synuclein (α-syn) as amyloid fibrils in the intracellular Lewy bodies in various region of the brain. Current thinking suggests that an interaction between α-syn and dopamine (DA) leads to the selective death of neuronal cells and the accumulation of misfolded α-syn. However, the exact mechanism by which this occurs is not fully defined. DA oxidation could play a key role is the pathogenesis of PD by causing oxidative stress, mitochondria dysfunction and impairment of protein metabolism. Here, we review the literature on the role of DA and its oxidative intermediates in modulating the aggregation pathways of α-syn. |
doi_str_mv | 10.1007/s11064-009-9986-8 |
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Current thinking suggests that an interaction between α-syn and dopamine (DA) leads to the selective death of neuronal cells and the accumulation of misfolded α-syn. However, the exact mechanism by which this occurs is not fully defined. DA oxidation could play a key role is the pathogenesis of PD by causing oxidative stress, mitochondria dysfunction and impairment of protein metabolism. 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Current thinking suggests that an interaction between α-syn and dopamine (DA) leads to the selective death of neuronal cells and the accumulation of misfolded α-syn. However, the exact mechanism by which this occurs is not fully defined. DA oxidation could play a key role is the pathogenesis of PD by causing oxidative stress, mitochondria dysfunction and impairment of protein metabolism. Here, we review the literature on the role of DA and its oxidative intermediates in modulating the aggregation pathways of α-syn.</description><subject>alpha-Synuclein - metabolism</subject><subject>alpha-Synuclein - physiology</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cell Biology</subject><subject>Cell Death - physiology</subject><subject>Dopamine - metabolism</subject><subject>Dopamine - physiology</subject><subject>Humans</subject><subject>Neurochemistry</subject><subject>Neurology</subject><subject>Neurons - metabolism</subject><subject>Neurons - pathology</subject><subject>Neurons - physiology</subject><subject>Neurosciences</subject><subject>Oxidative Stress - physiology</subject><subject>Parkinson Disease - etiology</subject><subject>Parkinson Disease - metabolism</subject><subject>Parkinson Disease - pathology</subject><subject>Protein Folding</subject><subject>Review Article</subject><issn>0364-3190</issn><issn>1573-6903</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtKw0AYhQdRbK0-gBvJSlfRfy6Zi7gp9QoVwct6mCSTkJJkaqZR-li-iM_klBTcdTX8nO8chg-hUwyXGEBceYyBsxhAxUpJHss9NMaJoDFXQPfRGGhIKVYwQkfeLwBCi-BDNMKKMcZBjNHNs8v72qwq10auiH5_4rd122e1rdpoWpadLYcsXUe3bmmaqrXX0TR6tV-V_T5GB4WpvT3ZvhP0cX_3PnuM5y8PT7PpPM6oYKtY5KAolpJCwTlRGeMGsMxTzLARAkieS1uQzFqSsoJKw1mBeTgwiASSnNAJuhh2l5377K1f6abyma1r01rXey0opUQymgTyfCdJwk-CGx5APIBZ57zvbKGXXdWYbq0x6I1cPcjVQa7eyNUydM62433a2Py_sbUZADIAPkRtaTu9cH3XBjU7Vv8ABC6DCw</recordid><startdate>20091001</startdate><enddate>20091001</enddate><creator>Leong, Su Ling</creator><creator>Cappai, Roberto</creator><creator>Barnham, Kevin Jeffrey</creator><creator>Pham, Chi Le Lan</creator><general>Springer US</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7X8</scope></search><sort><creationdate>20091001</creationdate><title>Modulation of α-Synuclein Aggregation by Dopamine: A Review</title><author>Leong, Su Ling ; Cappai, Roberto ; Barnham, Kevin Jeffrey ; Pham, Chi Le Lan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c374t-7d09318830f6629c46a018db141a7702dd8ef2cee2b4f38a64f16e2b107505d23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>alpha-Synuclein - metabolism</topic><topic>alpha-Synuclein - physiology</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cell Biology</topic><topic>Cell Death - physiology</topic><topic>Dopamine - metabolism</topic><topic>Dopamine - physiology</topic><topic>Humans</topic><topic>Neurochemistry</topic><topic>Neurology</topic><topic>Neurons - metabolism</topic><topic>Neurons - pathology</topic><topic>Neurons - physiology</topic><topic>Neurosciences</topic><topic>Oxidative Stress - physiology</topic><topic>Parkinson Disease - etiology</topic><topic>Parkinson Disease - metabolism</topic><topic>Parkinson Disease - pathology</topic><topic>Protein Folding</topic><topic>Review Article</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leong, Su Ling</creatorcontrib><creatorcontrib>Cappai, Roberto</creatorcontrib><creatorcontrib>Barnham, Kevin Jeffrey</creatorcontrib><creatorcontrib>Pham, Chi Le Lan</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Neurochemical research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leong, Su Ling</au><au>Cappai, Roberto</au><au>Barnham, Kevin Jeffrey</au><au>Pham, Chi Le Lan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Modulation of α-Synuclein Aggregation by Dopamine: A Review</atitle><jtitle>Neurochemical research</jtitle><stitle>Neurochem Res</stitle><addtitle>Neurochem Res</addtitle><date>2009-10-01</date><risdate>2009</risdate><volume>34</volume><issue>10</issue><spage>1838</spage><epage>1846</epage><pages>1838-1846</pages><issn>0364-3190</issn><eissn>1573-6903</eissn><abstract>Parkinson’s disease (PD) is a progressive neurodegenerative disorder that is characterized by (1) the selective loss of dopaminergic neurons in the substantia nigra and (2) the deposition of misfolded α-synuclein (α-syn) as amyloid fibrils in the intracellular Lewy bodies in various region of the brain. 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subjects | alpha-Synuclein - metabolism alpha-Synuclein - physiology Animals Biochemistry Biomedical and Life Sciences Biomedicine Cell Biology Cell Death - physiology Dopamine - metabolism Dopamine - physiology Humans Neurochemistry Neurology Neurons - metabolism Neurons - pathology Neurons - physiology Neurosciences Oxidative Stress - physiology Parkinson Disease - etiology Parkinson Disease - metabolism Parkinson Disease - pathology Protein Folding Review Article |
title | Modulation of α-Synuclein Aggregation by Dopamine: A Review |
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