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FK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53T.
- Source :
-
Journal of Neurochemistry . Jul2008, Vol. 106 Issue 1, p121-133. 13p. 2 Black and White Photographs, 1 Diagram, 2 Charts, 5 Graphs. - Publication Year :
- 2008
-
Abstract
- Aggregation of alpha-synuclein (α-SYN) plays a key role in Parkinson’s disease. We have previously shown that aggregation of α-SYN in vitro is accelerated by addition of FK506 binding proteins (FKBP) and that this effect can be counteracted by FK506, a specific inhibitor of these enzymes. In this paper, we investigated in detail the effect of FKBP12 on early aggregation and on fibril formation of wild-type, A53T and A30P α-SYN. FKBP12 has a much smaller effect on the fibril formation of these two clinical mutants α-SYN. Using an inactive enzyme, we were able to discriminate between catalytic and non-catalytic effects that differentially influence the two processes. A model explaining non-linear concentration dependencies is proposed. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00223042
- Volume :
- 106
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Journal of Neurochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 32593233
- Full Text :
- https://doi.org/10.1111/j.1471-4159.2008.05342.x