Amino acid sequence data on glial fibrillary acidic protein (GFA); implications for the subdivision of intermediate filaments into epithelial and non-epithelial members.
AUTOR(ES)
Geisler, N
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=555409Documentos Relacionados
- Sequence of a cDNA clone encoding mouse glial fibrillary acidic protein: structural conservation of intermediate filaments.
- Mice lacking glial fibrillary acidic protein display astrocytes devoid of intermediate filaments but develop and reproduce normally.
- Structure of the mouse glial fibrillary acidic protein gene: implications for the evolution of the intermediate filament multigene family.
- Long term neurotoxicity of styrene. A quantitative study of glial fibrillary acidic protein (GFA) and S-100.
- Comparison of commercially available cytokeratin antibodies in normal and neoplastic adult epithelial and non-epithelial tissues.