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Polyglutamine Domain Proteins with Expanded Repeats Bind Neurofilament, Altering the Neurofilament Network
Author(s) -
NAGAI YOSHITAKA,
ONODERA OSAMU,
STRITTMATTER WARREN J.,
BURKE JAMES R.
Publication year - 1999
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1999.tb07826.x
Subject(s) - neurofilament , microbiology and biotechnology , cytoplasm , fusion protein , biology , green fluorescent protein , gene , genetics , immunology , immunohistochemistry , recombinant dna
Proteins with expanded polyglutamine (polyQ) repeats cause eight inherited neurodegenerative diseases. Nuclear and cytoplasmic polyQ protein is a common feature of these diseases, but its role in cell death remains debatable. Since the neuronal intermediate filament network is composed of neurofilament (NF) and NF abnormalities occur in neurodegenerative diseases, we examined whether pathologic‐length polyQ domain proteins interact with NF. We expressed polyQ‐green fluorescent fusion proteins (GFP) in a neuroblast cell line, TR1. Pathologic‐length polyQ‐GFP fusion proteins form large cytoplasmic aggregates surrounded by neurofilament. Immunoisolation of pathologic‐length polyQ proteins co‐isolated 68 kD NF protein demonstrating molecular interaction. These observations suggest that polyQ interaction with NF is important in the pathogenesis of the polyglutamine repeat diseases.