Analysis of in vivo turnover of tau in a mouse model of tauopathy

Molecular Neurodegeneration

Volumn 10, Issue 1, 2015, Pages

  Yamada, Kaoru ^a   Patel, Tirth K ^b   Hochgräfe, Katja ^c   Mahan, Thomas E ^b   Jiang, Hong ^b   Stewart, Floy R ^b   Mandelkow, Eva Maria ^c,d,e   Holtzman, David M ^b  

^a UNIVERSITY OF TOKYO   (Japan)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c DESY   (Germany)

^d GERMAN CENTER FOR NEURODEGENERATIVE DISEASES DZNE   (Germany)

^e CENTER OF ADVANCED EUROPEAN STUDIES AND RESEARCH CAESAR   (Germany)

Author keywords

Alzheimer's disease; Clearance; Extracellular tau; Half life; Tauopathy model

Indexed keywords

EXTRACELLULAR TAU PROTEIN; INSOLUBLE TAU PROTEIN; INTRACELLULAR TAU PROTEIN; PHOSPHORYLATED TAU PROTEIN; PROLINE; SOLUBLE TAU PROTEIN; TAU PROTEIN; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BETA SHEET; CLEARANCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME LINKED IMMUNOSORBENT ASSAY; FEMALE; GENE MUTATION; HALF LIFE TIME; IN VIVO STUDY; MALE; MICRODIALYSIS; MOUSE; NONHUMAN; PROLINE RICH PROTEIN DOMAIN; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN METABOLISM; PROTEIN PHOSPHORYLATION; TAUOPATHY; TRANSGENIC MOUSE; TURNOVER TIME; ANIMAL; BRAIN; DISEASE MODEL; FRONTOTEMPORAL DEMENTIA; GENETICS; MEMORY; METABOLISM; MUTATION; PHYSIOLOGY;

ANIMALS; BRAIN; DISEASE MODELS, ANIMAL; FRONTOTEMPORAL DEMENTIA; MEMORY; MICE; MICE, TRANSGENIC; MUTATION; TAU PROTEINS; TAUOPATHIES;

EID: 84945293479     PISSN: None     EISSN: 17501326     Source Type: Journal    
DOI: 10.1186/s13024-015-0052-5     Document Type: Article

References (31)

1. De Calignon A, Polydoro M, Suárez-Calvet M, William C, Adamowicz DH, Kopeikina KJ, et al. Propagation of tau pathology in a model of early Alzheimer's disease. Neuron. 2012;73:685-97.
2. Clavaguera F, Bolmont T, Crowther RA, Abramowski D, Frank S, Probst A, et al. Transmission and spreading of tauopathy in transgenic mouse brain. Nat Cell Biol. 2009;11:909-13.
3. Frost B, Jacks RL, Diamond MI. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem. 2009;284:12845-52.
4. Liu L, Drouet V, Wu JW, Witter MP, Small SA, Clelland C, et al. Trans-synaptic spread of tau pathology in vivo. PLoS One. 2012;7:e31302.
5. Iba M, Guo JL, McBride JD, Zhang B, Trojanowski JQ, Lee VM-Y. Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy. J Neurosci. 2013;33:1024-37.
6. Van der Jeugd A, Hochgräfe K, Ahmed T, Decker JM, Sydow A, Hofmann A, et al. Cognitive defects are reversible in inducible mice expressing pro-aggregant full-length human Tau. Acta Neuropathol. 2012;123:787-805.
7. Roberson ED, Scearce-Levie K, Palop JJ, Yan F, Cheng IH, Wu T, et al. Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model. Science. 2007;316(80-):750-4.
8. Santacruz K, Lewis J, Spires T, Paulson J, Kotilinek L, Ingelsson M, et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science. 2005;309:476-81.
9. David DC, Layfield R, Serpell L, Narain Y, Goedert M, Spillantini MG. Proteasomal degradation of tau protein. J Neurochem. 2002;83:176-85.
10. Lim J, Balastik M, Lee TH, Nakamura K, Liou Y, Sun A, et al. Pin1 has opposite effects on wild-type and P301L tau stability and tauopathy. J Clin Invest. 2008;118:1877-89.
11. Carrettiero DC, Hernandez I, Neveu P, Papagiannakopoulos T, Kosik KS. The cochaperone BAG2 sweeps paired helical filament- insoluble tau from the microtubule. J Neurosci. 2009;29:2151-61.
12. Min S-W, Cho S-H, Zhou Y, Schroeder S, Haroutunian V, Seeley WW, et al. Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron. 2010;67:953-66.
13. Dickey CA, Kamal A, Lundgren K, Klosak N, Bailey RM, Dunmore J, et al. The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. J Clin Invest. 2007;117:648-58.
14. Shimura H, Schwartz D, Gygi SP, Kosik KS. CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J Biol Chem. 2004;279:4869-76.
15. Hochgräfe K, Sydow A, Mandelkow E-M. Regulatable transgenic mouse models of Alzheimer disease: onset, reversibility and spreading of Tau pathology. FEBS J. 2013;280:4371-81.
16. Eckermann K, Mocanu M-M, Khlistunova I, Biernat J, Nissen A, Hofmann A, et al. The beta-propensity of Tau determines aggregation and synaptic loss in inducible mouse models of tauopathy. J Biol Chem. 2007;282:31755-65.
17. Von Bergen M, Barghorn S, Li L, Marx A, Biernat J, Mandelkow E-M, et al. Mutations of Tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local {beta}-structure. J Biol Chem. 2001;276:48165-74.
18. Van Swieten JC, Bronner IF, Azmani A, Severijnen L-A, Kamphorst W, Ravid R, et al. The DeltaK280 mutation in MAP tau favors exon 10 skipping in vivo. J Neuropathol Exp Neurol. 2007;66:17-25.
19. Momeni P, Pittman A, Lashley T, Vandrovcova J, Malzer E, Luk C, et al. Clinical and pathological features of an Alzheimer's disease patient with the MAPT delta K280 mutation. Neurobiol Aging. 2009;30:388-93.
20. Yamada K, Holth JK, Liao F, Stewart FR, Mahan TE, Jiang H, et al. Neuronal activity regulates extracellular tau in vivo. J Exp Med. 2014;211:387-93.
21. Yamada K, Cirrito JR, Stewart FR, Jiang H, Finn MB, Holmes BB, et al. In vivo microdialysis reveals Age-dependent decrease of brain interstitial fluid Tau levels in P301S human Tau transgenic mice. J Neurosci. 2011;31:13110-7.
22. Andorfer C, Kress Y, Espinoza M, De Silva R, Tucker KL, Barde Y-A, et al. Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms. J Neurochem. 2003;86:582-90.
23. Castellano JM, Kim J, Stewart FR, Jiang H, DeMattos RB, Patterson BW, et al. Human apoE isoforms differentially regulate brain amyloid-β peptide clearance. Sci Transl Med. 2011;3:89ra57.
24. Poppek D, Keck S, Ermak G, Jung T, Stolzing A, Ullrich O, et al. Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress. Biochem J. 2006;400:511-20.
25. Ling S-C, Albuquerque CP, Han JS, Lagier-Tourenne C, Tokunaga S, Zhou H, et al. ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS. Proc Natl Acad Sci U S A. 2010;107:13318-23.
26. Li W, Lesuisse C, Xu Y, Troncoso JC, Price DL, Lee MK. Stabilization of alpha-synuclein protein with aging and familial parkinson's disease-linked A53T mutation. J Neurosci. 2004;24:7400-9.
27. Price JC, Guan S, Burlingame A, Prusiner SB, Ghaemmaghami S. Analysis of proteome dynamics in the mouse brain. Proc Natl Acad Sci U S A. 2010;107:14508-13.
28. Yanamandra K, Kfoury N, Jiang H, Mahan TE, Ma S, Maloney SE, et al. Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo. Neuron. 2013;80:402-14.
29. Yoshiyama Y, Higuchi M, Zhang B, Huang SM, Iwata N, Saido TC, et al. Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model. Neuron. 2007;53:337-51.
30. Dawson HN, Ferreira A, Eyster MV, Ghoshal N, Binder LI, Vitek MP. Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice. J Cell Sci. 2001;114(Pt 6):1179-87.
31. Basak JM, Kim J, Pyatkivskyy Y, Wildsmith KR, Jiang H, Parsadanian M, et al. Measurement of apolipoprotein E and amyloid β clearance rates in the mouse brain using bolus stable isotope labeling. Mol Neurodegener. 2012;7:14.