Different tau species lead to heterogeneous tau pathology propagation and misfolding

被引:73
作者
Dujardin, Simon [1 ,2 ,3 ]
Begard, Severine [1 ]
Caillierez, Raphaelle [1 ]
Lachaud, Cedrick [1 ]
Carrier, Sebastien [1 ]
Lieger, Sarah [1 ]
Gonzalez, Jose A. [2 ,3 ]
Deramecourt, Vincent [1 ]
Deglon, Nicole [4 ]
Maurage, Claude-Alain [1 ]
Frosch, Matthew P. [2 ,3 ]
Hyman, Bradley T. [2 ,3 ]
Colin, Morvane [1 ]
Buee, Luc [1 ]
机构
[1] Univ Lille, INSERM, CHU Lille, UMR S 1172,Alzheimer & Tauopathies,Sch Med, 1 Rue Polonovski, F-59045 Lille, France
[2] Massachusetts Gen Hosp, MassGen Inst Neurodegenerat Dis MIND, Dept Neurol, Charlestown, MA USA
[3] Harvard Med Sch, Dept Neurol, Boston, MA USA
[4] Lausanne Univ Hosp CHUV, Neurosci Res Ctr CRN, Lab Neurotherapies & Neuromodulat LNTM, CH-1011 Lausanne, Switzerland
关键词
Tau; Propagation; Isoforms; Misfolding; Alzheimer's disease; Heterogeneity; PAIRED HELICAL FILAMENTS; PROGRESSIVE SUPRANUCLEAR PALSY; PROTEIN-TAU; ALZHEIMERS-DISEASE; ENDOGENOUS-TAU; MAPT MUTATIONS; REPEAT DOMAIN; AGGREGATION; PHOSPHORYLATION; SECRETION;
D O I
10.1186/s40478-018-0637-7
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Tauopathies are a heterogeneous group of pathologies characterized by tau aggregation inside neurons. Most of them are sporadic but certain tauopathies rely on tau gene (MAPT) mutations. They particularly differ from one to another by their different neuropathological signatures e.g. lesion shapes, regions affected and molecular composition of aggregates. Six isoforms of tau exist, but they do not all co-aggregate in each tauopathy but rather have a unique signature for each one. In some tauopathies such as Alzheimer's disease (AD), tau protein aggregation follows stereotypical anatomical stages. Recent data suggest that this progression is due to an active process of tau protein propagation from neuron-to-neuron. We wondered how tau isoforms or mutations could influence the process of tau aggregation and tau propagation. In human neuropathological material, we found that MAPT mutations induce a faster misfolding compared to tau found in sporadic AD patients. In the rat brain, we observed cell-to-cell transfer of non-pathological tau species irrespective of the tested isoform or presence of a mutation. By contrast, we found that the species of tau impact the propagation of tau pathology markers such as hyperphosphorylation and misfolding. Indeed, misfolding and hyperphosphorylated tau proteins do not spread at the same rate when tau is mutated, or the isoform composition is modified. These results clearly argue for the existence of specific folding properties of tau depending on isoforms or mutations impacting the behavior of pathological tau species.
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页数:12
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