Natively unfolded tubulin polymerization promoting protein TPPP/p25 is a common marker of alpha-synucleinopathies

Gábor G. Kovács, Lajos László, János Kovács, Poul Henning Jensen, Evo Lindersson, Gergo Botond, Tamás Molnár, András Perczel, Ferenc Hudecz, Gábor Mezo, Anna Erdei, László Tirián, Attila Lehotzky, Ellen Gelpi, Herbert Budka, Judit Ovádi

Research output: Article

100 Citations (Scopus)


The novel basic, heat-stable tubulin polymerization promoting protein TPPP/p25 is associated with microtubules in vitro and can induce the formation of aberrant microtubule assemblies. We show by 1H-NMR spectroscopy that TPPP/p25 is natively unfolded. Antisera against peptide 186GKGKAGRVDLVDESG 200NH 2 (186a-200) are highly specific to TPPP/p25. Immunohistochemistry and confocal microscopy demonstrates that TPPP/p25 is enriched in filamentous alpha-synuclein bearing Lewy bodies of Parkinson's (PD) and diffuse Lewy body disease (DLBD), as well as glial inclusions of multiple system atrophy (MSA). There is a correlation between TPPP/p25 and alpha-synuclein immunoreactivity in Western blot. In contrast, TPPP/p25 is not associated with abnormally phosphorylated tau in various inclusions of Pick's disease (PiD), progressive supranuclear palsy (PSP), and corticobasal degeneration (CBD). However, electron microscopy confirms clusters of TPPP/p25 immunoreactivity along filaments of unstructured but not compact neurofibrillary tangles in Alzheimer's disease (AD). TPPP/p25 seems to be a novel marker of alpha-synucleinopathies.

Original languageEnglish
Pages (from-to)155-162
Number of pages8
JournalNeurobiology of Disease
Issue number2
Publication statusPublished - nov. 1 2004

ASJC Scopus subject areas

  • Neurology

Fingerprint Dive into the research topics of 'Natively unfolded tubulin polymerization promoting protein TPPP/p25 is a common marker of alpha-synucleinopathies'. Together they form a unique fingerprint.

  • Cite this