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The abnormal intraneuronal accumulations of \u03b1\u2010Syn in Lewy bodies (LBs) and Lewy neurites (LNs) have implicated defects in axonal transport of \u03b1\u2010Syn in the \u03b1\u2010synucleinopathies. Using human (Hu) \u03b1\u2010Syn transgenic (Tg) mice, we have examined whether familial PD (FPD)\u2010linked mutations (A30P and A53T) alter axonal transport of Hu\u03b1\u2010Syn. Our studies using peripheral nerves show that Hu\u03b1\u2010Syn and Mo\u03b1\u2010Syn are almost exclusively transported in the slow component (SC) of axonal transport and that the FPD\u2010linked \u03b1\u2010Syn mutations do not have obvious effects on the axonal transport of \u03b1\u2010Syn. Moreover, older pre\u2010symptomatic A53T Hu\u03b1\u2010Syn Tg mice do not show gross alterations in the axonal transport of \u03b1\u2010Syn and other proteins in the SC, indicating that the early stages of \u03b1\u2010synucleinopathy in A53T \u03b1\u2010Syn Tg mice are not associated with gross alterations in the slow axonal transport. However, the axonal transport of \u03b1\u2010Syn slows significantly with aging. Because the rate of axonal transport affects the stability and accumulation of proteins in axons, age\u2010dependent\u2010slowing \u03b1\u2010Syn is a likely contributor to axonal aggregation of \u03b1\u2010Syn in \u03b1\u2010synucleinopathy.<\/jats:p>","DOI":"10.1046\/j.1471-4159.2003.02166.x","type":"journal-article","created":{"date-parts":[[2010,7,16]],"date-time":"2010-07-16T06:31:32Z","timestamp":1279261892000},"page":"401-410","source":"Crossref","is-referenced-by-count":62,"title":["Axonal transport of human \u03b1\u2010synuclein slows with aging but is not affected by familial Parkinson's disease\u2010linked mutations"],"prefix":"10.1111","volume":"88","author":[{"given":"Wenxue","family":"Li","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paul N.","family":"Hoffman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wanda","family":"Stirling","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Donald L.","family":"Price","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael K.","family":"Lee","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2003,12,12]]},"reference":[{"key":"e_1_2_15_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0896-6273(00)80886-7"},{"key":"e_1_2_15_3_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M102981200"},{"key":"e_1_2_15_4_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1077209"},{"key":"e_1_2_15_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0896-6273(00)80974-5"},{"key":"e_1_2_15_6_1","doi-asserted-by":"publisher","DOI":"10.1006\/nbdi.1998.0178"},{"key":"e_1_2_15_7_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1471-4159.2001.00021.x"},{"key":"e_1_2_15_8_1","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-4547(19991001)58:1<120::AID-JNR12>3.0.CO;2-E"},{"key":"e_1_2_15_9_1","doi-asserted-by":"publisher","DOI":"10.1097\/00019052-200108000-00001"},{"key":"e_1_2_15_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0002-9440(10)64781-5"},{"key":"e_1_2_15_11_1","doi-asserted-by":"publisher","DOI":"10.1093\/jnen\/59.9.830"},{"key":"e_1_2_15_12_1","first-page":"679","volume-title":"Merritt's Neurology","author":"Fahn S.","year":"2000"},{"key":"e_1_2_15_13_1","doi-asserted-by":"publisher","DOI":"10.1038\/35006074"},{"key":"e_1_2_15_14_1","doi-asserted-by":"crossref","first-page":"2093","DOI":"10.1046\/j.1471-4159.1999.02093.x","article-title":"\u03b1\u2010Synuclein immunoisolation of glial inclusions from multiple system atrophy brain tissue reveals multiprotein components","volume":"73","author":"Gai W. 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