GSK-3α regulates production of Alzheimer's disease amyloid-β peptides

Nature

Volumn 423, Issue 6938, 2003, Pages 435-439

  Phiel, Christopher J ^a   Wilson, Christina A ^a   Lee, Virginia M Y ^a   Klein, Peter S ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BRAIN MODELS; CATALYSIS; LITHIUM; NEUROLOGY; PATHOLOGY; POLYPEPTIDES; PROTEINS;

AMYLOID PRECURSOR PROTEIN (APP);

DISEASE CONTROL;

ALPHA CATENIN; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; ASPARTIC PROTEINASE; BETA CATENIN; GAMMA SECRETASE; GLYCOGEN SYNTHASE KINASE 3BETA; KENPAULLONE; LITHIUM; NICASTRIN; NONSTEROID ANTIINFLAMMATORY AGENT; NOTCH RECEPTOR; PRESENILIN 1; ROSCOVITINE; BACE1 PROTEIN, MOUSE; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3 ALPHA; MEMBRANE PROTEIN; PEPTIDE FRAGMENT; PROTEINASE; SECRETASE;

MEDICINE;

ALZHEIMER DISEASE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CONTROLLED STUDY; MOUSE; NEUROFIBRILLARY TANGLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN SYNTHESIS; SENILE PLAQUE; ANIMAL; BRAIN; CELL CULTURE; CHO CELL; DRUG ANTAGONISM; DRUG EFFECT; HAMSTER; METABOLISM; NERVE CELL; PATHOLOGY; PHOSPHORYLATION;

ANIMALIA;

ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; AMYLOID PRECURSOR PROTEIN SECRETASES; ANIMALS; ASPARTIC ENDOPEPTIDASES; BRAIN; CELLS, CULTURED; CHO CELLS; CRICETINAE; ENDOPEPTIDASES; GLYCOGEN SYNTHASE KINASE 3; LITHIUM; MEMBRANE PROTEINS; MICE; NEURONS; PEPTIDE FRAGMENTS; PHOSPHORYLATION; RECEPTORS, NOTCH;

EID: 0038187674     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01640     Document Type: Article

References (30)

1. Selkoe, D. J. Presenilin, Notch, and the genesis and treatment of Alzheimer's disease. Proc. Natl Acad. Sci. USA 98, 11039-11041 (2001).
2. Vassar, R. et al. β-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286, 735-741 (1999).
3. De Strooper, B. et al. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 391, 387-390 (1998).
4. Esler, W. P. et al. Activity-dependent isolation of the presenilin-γ-secretase complex reveals nicastrin and a γ secretase substrate. Proc. Natl Acad. Sci. USA 99, 2720-2725 (2002).
5. Edbauer, D., Winkler, E., Haass, C. & Steiner, H. Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation. Proc. Natl Acad. Sci. USA 99, 8666-8671 (2002).
6. Francis, R. et al. aph-1 and pen-2 are required for Notch pathway signalling, γ-secretase cleavage of βAPP, and presenilin protein accumulation. Dev. Cell 3, 85-97 (2002).
7. Soriano, S. et al. Presenilin 1 negatively regulates β-catenin/T cell factor/lymphoid enhancer factor-1 signalling independently of β-amyloid precursor protein and notch processing. J. Cell Biol. 152, 785-794 (2001).
8. Yu, G. et al. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature 407, 48-54 (2000).
9. Takashima, A. et al. Presenilin 1 associates with glycogen synthase kinase-3β and its substrate tau. Proc. Natl Acad. Sci. USA 95, 9637-9641 (1998).
10. Kang, D. E. et al. Presenilin 1 facilitates the constitutive turnover of β-catenin: differential activity of Alzheimer's disease-linked PS1 mutants in the β-catenin-signalling pathway. J. Neurosci. 19, 4229-4237 (1999).
11. Kang, D. E. et al. Presenilin couples the paired phosphorylation of β-catenin independent of axin: implications for β-catenin activation in tumorigenesis. Cell 110, 751-762 (2002).
12. Phiel, C. I. & Klein, P. S. Molecular targets of lithium action. Annu. Rev. Pharmacol. Toxicol. 41, 789-813 (2001).
13. Klein, P. S. & Melton, D. A. A molecular mechanism for the effect of lithium on development. Proc. Natl Acad. Sci. USA 93, 8455-8459 (1996).
14. Sun, X. et al. Lithium inhibits amyloid secretion in COS7 cells transfected with amyloid precursor protein C100. Neurosci. Lett. 321, 61-64 (2002).
15. De Strooper, B. et al. A presenilin-I-dependent γ-secretase-like protease mediates release of Notch intracellular domain. Nature 398, 518-522 (1999).
16. Wolfe, M. S. et al. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 398, 513-517 (1999).
17. Schroeter, E. H., Kisslinger, J. A. & Kopan, R. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature 393, 382-386 (1998).
18. Bain, J., McLaughlan, H., Elliott, M. & Cohen, P. The specificities of protein kinase inhibitors-an update. Biochem. J. 371, 199-204 (2003).
19. Elbashir, S. M. et al. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411, 494-498 (2001).
20. Hoeflich, K. P. et al. Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation. Nature 406, 86-90 (2000).
21. Siman, R. et al. Presenilin-1 P264L knock-in mutation: differential effects on Aβ production, amyloid deposition, and neuronal vulnerability. J. Neurosci. 20, 8717-8726 (2000).
22. Kirschenbaum, F., Hsu, S. C., Cordell, B. & McCarthy, J. V. Substitution of a glycogen synthase kinase-3β phosphorylation site in presenilin 1 separates presenilin function from β-catenin signaling. J. Biol. Chem. 276, 7366-7375 (2001).
23. Weggen, S. et al. A subset of NSA1Ds lower amyloidogenic Aβ42 independently of cyclooxygenase activity. Nature 414, 212-216 (2001).
24. Alvarez, G. et al. Regulation of tau phosphorylation and protection against β-amyloid-induced neurodegeneration by lithium. Possible implications for Alzheimer's disease. Bipolar Disord. 4, 153-165 (2002).
25. Forman, M. S., Cook, D. G., Leight, S., Doms, R. W. & Lee, V. M.-Y. Differential effects of the Swedish mutant amyloid precursor protein on β-amyloid accumulation and secretion in neurons and nonneuronal cells. J. Biol. Chem. 272, 32247-32253 (1997).
26. Pleasure, S. J., Page, C. & Lee, V. M.-Y. Pure, postmitotic, polarized human neurons derived from NTera 2 cells provide a system for expressing exogenous proteins in terminally differentiated neurons. J. Neurosci. 12, 1802-1815 (1992).
27. Suzuki, N. et al. An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (βAPPTI7) mutants. Science 264, 1336-1340 (1994).
28. Turner, R. S., Suzuki, N., Chyung, A. S., Younkin, S. G. & Lee, V. M.-Y. Amyloids β40 and β42 are generated intracellularly in cultured human neurons and their secretion increases with maturation. J. Biol. Chem. 271, 8966-8970 (1996).
29. Cook, D. G. et al. Alzheimer's Aβ(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nature Med. 3, 1021-1023 (1997).
30. Wilson, C. A., Doms, R. W., Zheng, H. & Lee, V. M.-Y. Presenilins are not required for Aβ42 production in the early secretory pathway. Nature Neurosci. 5, 849-855 (2002).