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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Evidence that formation of an intermediate filament-protein complex plays a primary role in aggregation of neurofilaments, glial fibrillary acidic protein (GFAP)-filaments and vimentin-filaments by 2,5-hexanedione.

Using a variety of cell types in culture, we have investigated the relevance of intermolecular crosslinking involving intermediate filament proteins (IF-proteins) to the changes in distribution of intermediate filaments induced by the neurotoxicant, 2,5-hexanedione (2,5HD). Aggregation of vimentin-filaments (vimentin-IF), glial fibrillary acidic protein (GFAP)-IF and neurofilaments was preceded by appearance on immunoblots of a high molecular weight complex (IF-complex) labeled by antibodies against the IF-protein of the cell type: pV-170 from human skin fibroblasts and pV-130 from 3T3 mouse fibroblasts, which were labeled by anti-vimentin and, from cultures of dissociated mouse spinal cord and dorsal root ganglia, pNFH-300 labeled by antibody against the 200 kDa neurofilament protein (NF-200 or NF-H) and a doublet labeled by antiserum to GFAP (pGFAP-145).pV-170 was detected in human skin fibroblasts within one hour of exposure to 2,5HD and the amount of both pV-170 and pNFH-300 was related to the concentration of 2,5HD and the duration of exposure. Intermediate filament-complexes were not detected in PtK1 epithelial cells by labeling of transblots with anti-cytokeratin, nor are keratin-IF aggregated by 2,5HD. Intermediate filament-complexes were not detected in fibroblasts with IF-aggregates secondary to disruption of microtubules by colchicine or in fibroblasts from patients with giant axonal neuropathy.[1]


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