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

Nature

Volumn 480, Issue 7376, 2011, Pages

  Jaworski, Tomasz ^a   Dewachter, Ilse ^a,d   Lechat, Benoit ^a   Gees, Maarten ^a,e   Kremer, Anna ^a   Demedts, David ^a   Borghgraef, Peter ^a   Devijver, Herman ^a   Kügler, Seb ^b   Patel, Satish ^c   Woodgett, Jim R ^c   Van Leuven, Fred ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

^b UNIVERSITY OF GÖTTINGEN   (Germany)

^c MOUNT SINAI HOSPITAL   (Canada)

^d UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

^e LABORATORY OF MOLECULAR AND CELLULAR SIGNALING   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AMYLOID PRECURSOR PROTEIN; GLYCOGEN SYNTHASE KINASE 3ALPHA; GLYCOGEN SYNTHASE KINASE 3BETA; ISOENZYME; VIRUS VECTOR;

ENZYME ACTIVITY; EXPERIMENTAL STUDY; MOLECULAR ANALYSIS;

ENZYME ACTIVITY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN SYNTHESIS; SHORT SURVEY;

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; ANIMALS; GLYCOGEN SYNTHASE KINASE 3;

EID: 83055188883     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10615     Document Type: Short Survey

References (13)

1. Phiel, C. J., Wilson, C. A., Lee, V. M. & Klein, P. S. GSK-3a regulates production of Alzheimer's disease amyloid-b peptides. Nature 423, 435-439 (2003). (Pubitemid 36626994)
2. Ishiguro, K. et al. Glycogen synthase kinase 3b is identical to tau protein kinase I generating several epitopes of paired helical filaments. FEBS Lett. 325, 167-172 (1993). (Pubitemid 23186470)
3. Spittaels, K. et al. GSK3b phosphorylates protein tau and rescues the axonopathy in the central nervous system of human four-repeat tau transgenic mice. J. Biol. Chem. 275, 41340-41349 (2000). (Pubitemid 32054968)
4. Takashima, A. GSK-3 is essential in the pathogenesis of Alzheimer's disease. J. Alzheimers Dis. 9 (Suppl.), 309-317 (2006). (Pubitemid 44253325)
5. Terwel, D. et al. Amyloid activates GSK-3b to aggravate neuronal tauopathy in bigenic mice. Am. J. Pathol. 172, 786-798 (2008). (Pubitemid 351354550)
6. Kaidanovich-Beilin, O. et al. Abnormalities in brain structure and behavior in GSK-3a mutant mice. Mol Brain. 2, 35 (2009).
7. Dewachter, I. et al. Neuronal deficiency of presenilin 1 inhibits amyloid plaque formation and corrects hippocampal long-term potentiation but not a cognitive defect of amyloid precursor protein [V717I] transgenic mice. J. Neurosci. 22, 3445-3453 (2002). (Pubitemid 37465750)
8. Perez-Costas, E., Gandy, J. C., Melendez-Ferro, M., Roberts, R. C. & Bijur, G. N. Light and electron microscopy study of glycogen synthase kinase-3b in the mouse brain. PLoS ONE 5, e8911 (2010).
9. Jaworski, T. et al. AAV-tau mediates pyramidal neurodegeneration by cell-cycle reentry without neurofibrillary tangle formation in wild-type mice. PLoS ONE 4, e7280 (2009).
10. De Strooper, B. et al. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 391, 387-390 (1998). (Pubitemid 28093512)
11. Moechars, D. et al. Early phenotypic changes in transgenic mice that overexpress different mutants of amyloid precursor protein in brain. J. Biol. Chem. 274, 6483-6492 (1999). (Pubitemid 29111064)
12. Tanghe, A. et al.Pathological hallmarks, clinical parallels, and value for drug testing in Alzheimer's disease of the APP[V717I] London transgenic mouse model. Int. J. Alzheimers Dis. 2010, 417314 (2010).
13. Jaworski, T. et al. Alzheimer's disease: old problem, newviews fromtransgenic and viral models. Biochim. Biophys. Acta 1802, 808-818 (2010).