Threonine 53 in α-synuclein is conserved in long-living non-primate animals

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Knud Larsen
  • Claus Hedegaard, Denmark
  • Mads Frost Bertelsen, Copenhagen Zoo, Denmark
  • Christian Bendixen, Denmark
  • Molekylær Genetik og Systembiologi
  • Department of Genetics and Biotechnology
α-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 α-synuclein (SNCA) gene cause hereditary forms of PD. One of the α-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 α-synuclein is an alanine in humans, great apes and Old World primates. However, this amino acid is a threonine in the α-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 α-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
Original languageEnglish
JournalBiochemical and Biophysical Research Communications
Pages (from-to)602-605
Number of pages4
Publication statusPublished - 2009

    Research areas

  • α-Synuclein, Mutation, Parkinson’s disease, SNCA

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