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Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein
Published on: May 30, 2015
Threonine 53 in alpha-synuclein is conserved in long-living non-primate animals
Knud Larsen1, Claus Hedegaard, Mads Frost Bertelsen
1Department of Genetics and Biotechnology, Faculty of Agricultural Sciences, University of Aarhus, Blichers Alle 20, Tjele, Denmark. Knud.Larsen@agrsci.dk
Abstract:
Alpha-synuclein is the main constituent of Lewy bodies in familial and sporadic cases of Parkinson's disease (PD). Autosomal dominant point mutations, gene duplications or triplications in the alpha-synuclein (SNCA) gene cause hereditary forms of PD. One of the alpha-synuclein point mutations, Ala53Thr, is associated with increased oligomerization toxicity leading to familial early-onset PD in humans. The amino acid in position 53 in alpha-synuclein is an alanine in humans, great apes and Old World primates. However, this amino acid is a threonine in the alpha-synuclein of all other examined species, including New World monkeys. Here, we present DNA sequence analysis of SNCA and the deduced amino acid sequences of alpha-synuclein cloned from various different species, ranging from fish to mammals, which are known for their long-living potential. In all these investigated species the 53Thr is found. We conclude that 53Thr is not a molecular adaptation for long-living animals to minimize the risk of developing PD.
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