Phiel et al. reply

Christopher J. Phiel, Christina A. Wilson, Virginia M.-Y. Lee and Peter S. Klein ()
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Christopher J. Phiel: Center for Molecular and Human Genetics, The Research Institute at Nationwide Children’s Hospital
Christina A. Wilson: 3 West Gates Building, University of Pennsylvania School of Medicine
Virginia M.-Y. Lee: Center for Neurodegenerative Disease Research, 3rd Floor Maloney Building, University of Pennsylvania School of Medicine
Peter S. Klein: University of Pennsylvania School of Medicine

Nature, 2011, vol. 480, issue 7376, E6-E6

Abstract: Abstract Replying to T. Jaworski et al. Nature 480, doi:10.1038/nature10615 (2011) GSK-3 has been implicated in the pathogenesis of Alzheimer’s disease through regulation of tau phosphorylation, cellular responses to amyloid-β and processing of amyloid precursor protein (APP) to amyloid-β. We previously reported1 that inhibition of GSK-3 reduces the accumulation of Aβ40 and Aβ42 (amyloid-ß peptides of 40 and 42 amino acids) in mouse brain and cell culture and that knockdown of Gsk3a reduces amyloid-β accumulation in CHO cells, indicating that Gsk3a contributes to the processing of APP in this context1. At about the same time, others reported that knockdown of Gsk3b reduces amyloid-β production and overexpression of active Gsk3b enhances amyloid-β production2,3,4. A reasonable explanation for these findings, as suggested previously2,5,6, was that both of these highly similar enzymes contribute to APP processing and their respective contributions depend on cell type, relative abundance and assay conditions. Jaworski et al.7 now show that APP can be processed in mouse brain in the absence of either Gsk3a or neuronal Gsk3b.

Date: 2011
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DOI: 10.1038/nature10616

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