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Role of Tau Protein in Both Physiological and Pathological Conditions
Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), Facultad de Ciencias, Campus de Cantoblanco, Madrid, Spain Avila, Jesús, José J. Lucas, Mar Pérez, and Félix Hernández. Role of Tau Protein in Both Physiological and Pathological Conditions. Physiol Rev 84: 361384, 2004; 10.1152/phys...
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Published in: | Physiological reviews 2004-04, Vol.84 (2), p.361-384 |
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Avila, Jesús, José J. Lucas, Mar Pérez, and Félix Hernández. Role of Tau Protein in Both Physiological and Pathological Conditions. Physiol Rev 84: 361384, 2004; 10.1152/physrev.00024.2003.The morphology of a neuron is determined by its cytoskeletal scaffolding. Thus proteins that associate with the principal cytoskeletal compo-nents such as the microtubules have a strong influence on both the morphology and physiology of neurons. Tau is a microtubule-associated protein that stabilizes neuronal microtubules under normal physiological conditions. However, in certain pathological situations, tau protein may undergo modifications, mainly through phosphorylation, that can result in the generation of aberrant aggregates that are toxic to neurons. This process occurs in a number of neurological disorders collectively known as tauopathies, the most commonly recognized of which is Alzheimer's disease. The purpose of this review is to define the role of tau protein under normal physiological conditions and to highlight the role of the protein in different tauopathies.
Address for reprint requests and other correspondence: J. Avila, Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), Facultad de Ciencias, Campus de Cantoblanco, Universidad Autónoma de Madrid, 28049 Madrid, Spain (E-mail: ). |
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Avila, Jesús, José J. Lucas, Mar Pérez, and Félix Hernández. Role of Tau Protein in Both Physiological and Pathological Conditions. Physiol Rev 84: 361384, 2004; 10.1152/physrev.00024.2003.The morphology of a neuron is determined by its cytoskeletal scaffolding. Thus proteins that associate with the principal cytoskeletal compo-nents such as the microtubules have a strong influence on both the morphology and physiology of neurons. Tau is a microtubule-associated protein that stabilizes neuronal microtubules under normal physiological conditions. However, in certain pathological situations, tau protein may undergo modifications, mainly through phosphorylation, that can result in the generation of aberrant aggregates that are toxic to neurons. This process occurs in a number of neurological disorders collectively known as tauopathies, the most commonly recognized of which is Alzheimer's disease. The purpose of this review is to define the role of tau protein under normal physiological conditions and to highlight the role of the protein in different tauopathies.
Address for reprint requests and other correspondence: J. Avila, Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), Facultad de Ciencias, Campus de Cantoblanco, Universidad Autónoma de Madrid, 28049 Madrid, Spain (E-mail: ).</description><identifier>ISSN: 0031-9333</identifier><identifier>EISSN: 1522-1210</identifier><identifier>DOI: 10.1152/physrev.00024.2003</identifier><identifier>PMID: 15044677</identifier><identifier>CODEN: PHREA7</identifier><language>eng</language><publisher>United States: Am Physiological Soc</publisher><subject>Anatomy & physiology ; Animals ; Disease Models, Animal ; Humans ; Microtubules - physiology ; Neurons - pathology ; Neurons - physiology ; Pathology ; Protein Processing, Post-Translational - physiology ; Proteins ; tau Proteins - chemistry ; tau Proteins - genetics ; tau Proteins - physiology ; Tauopathies - pathology ; Tauopathies - physiopathology</subject><ispartof>Physiological reviews, 2004-04, Vol.84 (2), p.361-384</ispartof><rights>COPYRIGHT 2004 American Physiological Society</rights><rights>Copyright American Physiological Society Apr 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c584t-6a70e546d913055c68f343550a9ba6017af9a6045a0143a9048bec86e57414053</citedby><cites>FETCH-LOGICAL-c584t-6a70e546d913055c68f343550a9ba6017af9a6045a0143a9048bec86e57414053</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15044677$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>AVILA, JESUS</creatorcontrib><creatorcontrib>LUCAS, JOSE J</creatorcontrib><creatorcontrib>PEREZ, MAR</creatorcontrib><creatorcontrib>HERNANDEZ, FELIX</creatorcontrib><title>Role of Tau Protein in Both Physiological and Pathological Conditions</title><title>Physiological reviews</title><addtitle>Physiol Rev</addtitle><description>Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), Facultad de Ciencias, Campus de Cantoblanco, Madrid, Spain
Avila, Jesús, José J. Lucas, Mar Pérez, and Félix Hernández. Role of Tau Protein in Both Physiological and Pathological Conditions. Physiol Rev 84: 361384, 2004; 10.1152/physrev.00024.2003.The morphology of a neuron is determined by its cytoskeletal scaffolding. Thus proteins that associate with the principal cytoskeletal compo-nents such as the microtubules have a strong influence on both the morphology and physiology of neurons. Tau is a microtubule-associated protein that stabilizes neuronal microtubules under normal physiological conditions. However, in certain pathological situations, tau protein may undergo modifications, mainly through phosphorylation, that can result in the generation of aberrant aggregates that are toxic to neurons. This process occurs in a number of neurological disorders collectively known as tauopathies, the most commonly recognized of which is Alzheimer's disease. The purpose of this review is to define the role of tau protein under normal physiological conditions and to highlight the role of the protein in different tauopathies.
Address for reprint requests and other correspondence: J. Avila, Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), Facultad de Ciencias, Campus de Cantoblanco, Universidad Autónoma de Madrid, 28049 Madrid, Spain (E-mail: ).</description><subject>Anatomy & physiology</subject><subject>Animals</subject><subject>Disease Models, Animal</subject><subject>Humans</subject><subject>Microtubules - physiology</subject><subject>Neurons - pathology</subject><subject>Neurons - physiology</subject><subject>Pathology</subject><subject>Protein Processing, Post-Translational - physiology</subject><subject>Proteins</subject><subject>tau Proteins - chemistry</subject><subject>tau Proteins - genetics</subject><subject>tau Proteins - physiology</subject><subject>Tauopathies - pathology</subject><subject>Tauopathies - physiopathology</subject><issn>0031-9333</issn><issn>1522-1210</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNp1kV1rFDEYhYModq3-AS9k8MKbMtu8-Zy5bJdWhYJLWa9Ddiazk5JN1mRG3X_f7JeFUknghTfPOTlwEPoIeArAyeWm36Zofk8xxoRNCcb0FZrkB1ICAfwaTfIGyppSeobepfSQOc4Ff4vOgGPGhJQTdHMfnClCVyz0WMxjGIz1Rb7XYeiLef7ABhdWttGu0L4t5nro_y1mwbd2sMGn9-hNp10yH47zHP28vVnMvpV3P75-n13dlQ2v2FAKLbHhTLQ10BylEVVHGeUc63qpBQapuzpPxjUGRnWNWbU0TSUMlwwY5vQcfTn4bmL4NZo0qLVNjXFOexPGpECKuiIAGfz8DHwIY_Q5myIgWCWF3LmVB2ilnVHWd2GIulkZb6J2wZvO5vUVAKs4Z5RkfvoCn09r1rZ5UUAOgiaGlKvq1CbatY5bBVjtKlTHCtW-QrWrMIs-HaOPy7VpnyTHzjIgD0BvV_0fG83eZd_TVt2Ozi3M3-HkXGVXRQWoTdtl5cX_lacoJwV9BCMbugo</recordid><startdate>20040401</startdate><enddate>20040401</enddate><creator>AVILA, JESUS</creator><creator>LUCAS, JOSE J</creator><creator>PEREZ, MAR</creator><creator>HERNANDEZ, FELIX</creator><general>Am Physiological Soc</general><general>American Physiological Society</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>7QP</scope><scope>7TK</scope><scope>7TS</scope></search><sort><creationdate>20040401</creationdate><title>Role of Tau Protein in Both Physiological and Pathological Conditions</title><author>AVILA, JESUS ; LUCAS, JOSE J ; PEREZ, MAR ; HERNANDEZ, FELIX</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c584t-6a70e546d913055c68f343550a9ba6017af9a6045a0143a9048bec86e57414053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Anatomy & physiology</topic><topic>Animals</topic><topic>Disease Models, Animal</topic><topic>Humans</topic><topic>Microtubules - physiology</topic><topic>Neurons - pathology</topic><topic>Neurons - physiology</topic><topic>Pathology</topic><topic>Protein Processing, Post-Translational - physiology</topic><topic>Proteins</topic><topic>tau Proteins - chemistry</topic><topic>tau Proteins - genetics</topic><topic>tau Proteins - physiology</topic><topic>Tauopathies - pathology</topic><topic>Tauopathies - physiopathology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>AVILA, JESUS</creatorcontrib><creatorcontrib>LUCAS, JOSE J</creatorcontrib><creatorcontrib>PEREZ, MAR</creatorcontrib><creatorcontrib>HERNANDEZ, FELIX</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Physical Education Index</collection><jtitle>Physiological reviews</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>AVILA, JESUS</au><au>LUCAS, JOSE J</au><au>PEREZ, MAR</au><au>HERNANDEZ, FELIX</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of Tau Protein in Both Physiological and Pathological Conditions</atitle><jtitle>Physiological reviews</jtitle><addtitle>Physiol Rev</addtitle><date>2004-04-01</date><risdate>2004</risdate><volume>84</volume><issue>2</issue><spage>361</spage><epage>384</epage><pages>361-384</pages><issn>0031-9333</issn><eissn>1522-1210</eissn><coden>PHREA7</coden><abstract>Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), Facultad de Ciencias, Campus de Cantoblanco, Madrid, Spain
Avila, Jesús, José J. Lucas, Mar Pérez, and Félix Hernández. Role of Tau Protein in Both Physiological and Pathological Conditions. Physiol Rev 84: 361384, 2004; 10.1152/physrev.00024.2003.The morphology of a neuron is determined by its cytoskeletal scaffolding. Thus proteins that associate with the principal cytoskeletal compo-nents such as the microtubules have a strong influence on both the morphology and physiology of neurons. Tau is a microtubule-associated protein that stabilizes neuronal microtubules under normal physiological conditions. However, in certain pathological situations, tau protein may undergo modifications, mainly through phosphorylation, that can result in the generation of aberrant aggregates that are toxic to neurons. This process occurs in a number of neurological disorders collectively known as tauopathies, the most commonly recognized of which is Alzheimer's disease. The purpose of this review is to define the role of tau protein under normal physiological conditions and to highlight the role of the protein in different tauopathies.
Address for reprint requests and other correspondence: J. Avila, Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), Facultad de Ciencias, Campus de Cantoblanco, Universidad Autónoma de Madrid, 28049 Madrid, Spain (E-mail: ).</abstract><cop>United States</cop><pub>Am Physiological Soc</pub><pmid>15044677</pmid><doi>10.1152/physrev.00024.2003</doi><tpages>24</tpages></addata></record> |
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subjects | Anatomy & physiology Animals Disease Models, Animal Humans Microtubules - physiology Neurons - pathology Neurons - physiology Pathology Protein Processing, Post-Translational - physiology Proteins tau Proteins - chemistry tau Proteins - genetics tau Proteins - physiology Tauopathies - pathology Tauopathies - physiopathology |
title | Role of Tau Protein in Both Physiological and Pathological Conditions |
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