A New Splice Variant of Glial Fibrillary Acidic Protein, GFAPε, Interacts with the Presenilin Proteins*

By A. Nielsen, I. Holm, M. Johansen, B. Bonven, Poul Jørgensen, A. Jørgensen. Journal of Biological Chemistry, 2002

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We describe a new human isoform, GFAPε, of the intermediary filament protein GFAP (glial fibrillary acidic protein). GFAPε mRNA is the result of alternative splicing and a new polyadenylation signal, and thus GFAPε has a new C-terminal protein sequence. This provides GFAPε with the capacity for specific binding of presenilin proteins in yeast and in vitro. Our observations suggest a direct link between the presenilins and the cytoskeleton where GFAPε is incorporated. Mutations in GFAP and presenilins are associated with Alexander disease and Alzheimer's disease, respectively. Accordingly, GFAPε should be taken into consideration when studying neurodegenerative diseases.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/a5c6fe5e3b2ef40d98a37dbe9030f5261afd3ff5

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Citations in the corpus

• Proinflammatory cytokine synthesis in the injured mouse spinal cord: Multiphasic expression pattern and identification of the cell types involved (2007, background): “1H, lane 4), which apparently is a proteolytic fragment of the protein or an alternate transcript from the GFAP gene (Nielsen et al., 2002).”