Localization of α-, ß-, and γ-synuclein during neuronal development and alterations associated with the neuronal response to axonal trauma

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Title Localization of α-, ß-, and γ-synuclein during neuronal development and alterations associated with the neuronal response to axonal trauma
Author Quilty, M.C.; Gai, W-P; Pountney, Dean Louis; West, A.K.; Vickers, J.C.
Journal Name Experimental Neurology
Year Published 2003
Place of publication Ireland
Publisher Academic Press
Abstract Genetic and protein studies have indicated abnormalities in α-synuclein in neurodegenerative diseases. However, the developmental localization and cellular role of synuclein isoforms is contentious. We investigated the cellular localization of α-, ß-, and γ-synuclein in developing cultured rat neurons and following axonal transection of relatively mature neurons, a model that disrupts the axonal cytoskeleton and results in regenerative sprouting. Cortical neurons were grown up to 21 days in vitro (DIV). Axon bundles at 21 DIV were transected and cellular changes examined at 4 and 24 h post-injury. Immunohistochemistry demonstrated that α- and ß-synuclein were localized to cellular cytosol and growth cones at 3DIV, with accumulating puncta-like labeling within axons and growth cones by 10-21DIV. In contrast, γ-synuclein immunoreactivity was limited at all time points. By 21DIV, α- and ß-synuclein were present in the same neurons but largely in separate subregions, only 26% of puncta contained both α- and ß-synuclein immunoreactivity. Less than 20% of α-, ß-, and pan-synuclein immunoreactive puncta directly colocalized to synaptophysin profiles at 10DIV, decreasing to 10% at 21DIV. Both α- and ß-synuclein accumulated substantially within damaged axons at 21DIV and were localized to cytoskeletal abnormalities. At latter time points post-injury, α- and ß-synuclein immunoreactive puncta were localized to growth cone-like structures in regenerating neurites. This study shows that α- and ß-synuclein have a precise localization within cortical neurons and are generally nonoverlapping in their distribution within individual neurons. In addition, synuclein proteins accumulate rapidly in damaged axons and may have a role in regenerative sprouting.
Peer Reviewed Yes
Published Yes
Publisher URI http://www.elsevier.com/locate/yexnr
Alternative URI http://dx.doi.org/10.1016/S0014-4886(03)00108-0
Volume 182
Issue Number 1
Page from 195
Page to 207
ISSN 0014-4886
Date Accessioned 2006-07-26
Date Available 2009-01-13T07:10:57Z
Language en_AU
Research Centre Griffith Health Institute
Faculty Griffith Health Faculty
Subject PRE2009-Cell Neurochemistry
URI http://hdl.handle.net/10072/21001
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1x

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