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. 1983;2(11):2059-63.
doi: 10.1002/j.1460-2075.1983.tb01700.x.

Amino acid sequence data on glial fibrillary acidic protein (GFA); implications for the subdivision of intermediate filaments into epithelial and non-epithelial members

N Geisler, K Weber

Amino acid sequence data on glial fibrillary acidic protein (GFA); implications for the subdivision of intermediate filaments into epithelial and non-epithelial members

N Geisler et al. EMBO J. 1983.

Abstract

Determination of 50% of the sequence of the astrocyte-specific intermediate filament (IF) protein documents the hypervariable regions as well as parts of the coiled-coil array of glial fibrillary acidic protein (GFA). The results show that the four non-epithelial IF proteins (myogenic desmin, mesenchymal vimentin, GFA and neurofilament 68 K protein) known to form homopolymers are much more closely related than the epithelial keratins, which seem to form heteropolymers only. Of the four non-epithelial proteins, desmin and vimentin are the most closely related, since GFA has a shorter non-alpha-helical array at the amino terminus. We discuss the possibility that the non-alpha-helical terminal arrays, because of their sequence and length variability, are responsible for differences of distinct IF with respect to physical-chemical properties such as the low ionic strength-induced depolymerization into protofilaments.

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References

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