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Identification of multiple post-translational modifications in the porcine brain specific p25α

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

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  • Anne J. Kjeinnijenhuis, Syddansk Universitet, Netherlands Organisation for Applied Scientific Research
    • ,
  • Claus Hedegaard, Institute of Genetics and Biotechnology
    • ,
  • Ditte Lundvig
    • ,
  • Sabrina Sundbye
    • ,
  • Olaf Georg Issinger, Syddansk Universitet
    • ,
  • Ole Nørregaard Jensen
  • Poul Henning Jensen

P25α is a protein normally expressed in oligodendrocytes and subcellular relocalization of p25α occurs in multiple system atrophy, Parkinson's disease and Lewy body dementia along with ectopic expression in neurons. Moreover, it accumulates in Lewy body inclusions with aggregated α-synuclein and is a potent stimulator of α-synuclein aggregation. P25α is a phosphoprotein and post-transla- tional modifications (PTMs) may play a role in its disease- related abnormalities. To investigate the spectrum of PTMs on p25α we cloned porcine p25α and isolated the protein from porcine brain. Using several complementary tandem mass spectrometry techniques for peptide mass analysis and amino acid sequencing, a comprehensive analysis of the PTMs on porcine p25α was performed. It was found that porcine p25α is heavily modified with a variety of modifications: phosphorylation, di- and trimethylation, citrullination and a HexNAc group. The modifications are localized within p25α's unfolded terminal domains and suggest that their functional states are regulated. This comprehensive mapping of p25α's PTMs will form the basis for future functional studies and investigations of p25α's potential role as a biomarker.

OriginalsprogEngelsk
TidsskriftJournal of Neurochemistry
Vol/bind106
Nummer2
Sider (fra-til)925-933
Antal sider9
ISSN0022-3042
DOI
StatusUdgivet - jul. 2008

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