Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

Parkinson's disease alpha-synuclein mutations exhibit defective axonal transport in cultured neurons

Saha, Anirban R., Hill, Josephine, Utton, Michelle A., Asuni, Ayodeji A., Ackerley, Steven, Grierson, Andrew J., Miller, Christopher C., Davies, Alun M., Buchman, Vladimir, Anderton, Brian H. and Hanger, Diane P. 2004. Parkinson's disease alpha-synuclein mutations exhibit defective axonal transport in cultured neurons. Journal of Cell Science 117 (Pt 7) , pp. 1017-1024. 10.1242/jcs.00967

Full text not available from this repository.

Abstract

?-Synuclein is a major protein constituent of Lewy bodies and mutations in -synuclein cause familial autosomal dominant Parkinson's disease. One explanation for the formation of perikaryal and neuritic aggregates of ?-synuclein, which is a presynaptic protein, is that the mutations disrupt ?-synuclein transport and lead to its proximal accumulation. We found that mutant forms of ?-synuclein, either associated with Parkinson's disease (A30P or A53T) or mimicking defined serine, but not tyrosine, phosphorylation states exhibit reduced axonal transport following transfection into cultured neurons. Furthermore, transfection of A30P, but not wild-type, ?-synuclein results in accumulation of the protein proximal to the cell body. We propose that the reduced axonal transport exhibited by the Parkinson's disease-associated ?-synuclein mutants examined in this study might contribute to perikaryal accumulation of ?-synuclein and hence Lewy body formation and neuritic abnormalities in diseased brain.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Subjects: R Medicine > R Medicine (General)
Uncontrolled Keywords: Synuclein ; Axonal transport ; Lewy body ; Parkinson's disease ; Aggregation ; Neurodegeneration
ISSN: 0021-9533
Last Modified: 04 Jun 2017 01:37
URI: http://orca.cf.ac.uk/id/eprint/1003

Citation Data

Cited 123 times in Scopus. View in Scopus. Powered By Scopus® Data

Cited 93 times in Web of Science. View in Web of Science.

Actions (repository staff only)

Edit Item Edit Item