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Synthetic filaments assembled from C‐terminally truncated α‐synuclein
Author(s) -
Crowther R.Anthony,
Jakes Ross,
Spillantini Maria Grazia,
Goedert Michel
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01146-6
Subject(s) - proteolysis , alpha synuclein , antibody , intermediate filament , biology , chemistry , parkinson's disease , microbiology and biotechnology , pathology , medicine , genetics , biochemistry , disease , cytoskeleton , cell , enzyme
Recently two point mutations in the α‐synuclein gene have been found in familial Parkinson's disease. The characteristic fibrous neuropathological lesions of Parkinson's and other neurodegenerative diseases have been shown to stain strongly with antibodies against α‐synuclein and extracted filaments have been labelled with anti‐α‐synuclein antibodies. In view of the close involvement of α‐synuclein filaments with pathology, it was important to establish an in vitro assembly system. We report here that C‐terminally truncated recombinant α‐synuclein readily assembles into filaments resembling those isolated from diseased brain and suggest that truncation by proteolysis may play a role in the pathological process.