GSK-3α/β kinases and amyloid production in vivo

Tomasz Jaworski, Ilse Dewachter, Benoit Lechat, Maarten Gees, Anna Kremer, David Demedts, Peter Borghgraef, Herman Devijver, Seb Kügler, Satish Patel, Jim R. Woodgett and Fred Van Leuven ()
Additional contact information
Tomasz Jaworski: Experimental Genetics Group
Ilse Dewachter: Experimental Genetics Group
Benoit Lechat: Experimental Genetics Group
Maarten Gees: Experimental Genetics Group
Anna Kremer: Experimental Genetics Group
David Demedts: Experimental Genetics Group
Peter Borghgraef: Experimental Genetics Group
Herman Devijver: Experimental Genetics Group
Seb Kügler: Georg-August-University
Satish Patel: Samuel Lunenfeld Research Institute, Mount Sinai Hospital
Jim R. Woodgett: Samuel Lunenfeld Research Institute, Mount Sinai Hospital
Fred Van Leuven: Experimental Genetics Group

Nature, 2011, vol. 480, issue 7376, E4-E5

Abstract: Abstract Arising from C. J. Phiel, C. A. Wilson, V. M.-Y. Lee & P. S. Klein Nature 423, 435–439 (2003)10.1038/nature01640 A major unresolved issue in Alzheimer’s disease is identifying the mechanisms that regulate proteolytic processing of amyloid precursor protein (APP)—glycogen synthase kinase-3 (GSK-3) isozymes are thought to be important in this regulation. Phiel et al.1 proposed that GSK-3α, but not GSK-3β, controls production of amyloid1. We analysed the proteolytic processing of mouse and human APP in mouse brain in vivo in five different genetic and viral models. Our data do not yield evidence for either GSK-3α-mediated or GSK-3β-mediated control of APP processing in brain in vivo.

Date: 2011
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DOI: 10.1038/nature10615

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