Letter | Published:

Related amino acid sequences in neurofilaments and non-neuronal intermediate filaments

Nature volume 296, pages 448450 (01 April 1982) | Download Citation

Abstract

The major constituents of mammalian neurofilaments are the three triplet proteins of molecular weight 200,000 (200K), 145K and 68K, which also co-migrate in slow axonal transport1–5. Partial amino acid sequence data6 and chemical cleavage patterns7,8 indicate that various cell-specific non-neuronal intermediate filament proteins having molecular weights between 40,000 and 70,000 are structurally related, consistent with a common filament morphology. Here we extend this principle to the neurofilament 68K triplet protein, NF68. We show that NF68, muscle-specific desmin (52K) and mesenchymally derived vimentin (55K) are related proteins. Direct amino acid sequence analysis of a uniquely positioned marker peptide (5K) shows that in this region, NF68 shows 42% sequence identity with vimentin and desmin, which have 70% identity. These results are discussed with respect to neurofilament organization.

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Author information

Affiliations

  1. Max-Planck Institute for Biophysical Chemistry, D-3400 Göttingen, FRG

    • Norbert Geisler
    • , Uwe Plessmann
    •  & Klaus Weber

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https://doi.org/10.1038/296448a0

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