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J. Biol. Chem., Vol. 277, Issue 33, 29983-29991, August 16, 2002

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

Anders Lade Nielsen^§¶, Ida E. Holm, Marianne Johansen, Bjarne Bonven^§, Poul Jørgensen^§, and Arne Lund Jørgensen

From the  Department of Human Genetics and the ^§ Department of Molecular Biology, University of Aarhus and the  Department of Neurology, Aarhus University Hospital, DK-8000 Aarhus C, Denmark

We describe a new human isoform, GFAP, of the intermediary filament protein GFAP (glial fibrillary acidic protein). GFAP mRNA is the result of alternative splicing and a new polyadenylation signal, and thus GFAP has a new C-terminal protein sequence. This provides GFAP 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 GFAP is incorporated. Mutations in GFAP and presenilins are associated with Alexander disease and Alzheimer's disease, respectively. Accordingly, GFAP should be taken into consideration when studying neurodegenerative diseases.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AJ306447.

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				J. Blechingberg, S. Lykke-Andersen, T. H. Jensen, A. L. Jorgensen, and A. L. Nielsen Regulatory mechanisms for 3'-end alternative splicing and polyadenylation of the Glial Fibrillary Acidic Protein, GFAP, transcript Nucleic Acids Res., December 3, 2007; 35(22): 7636 - 7650. [Abstract] [Full Text] [PDF]

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