Differential induction of mutant SOD1 misfolding and aggregation by tau and α-synuclein pathology.

ABSTRACT:

Background

Prior studies in C. elegans demonstrated that the expression of aggregation-prone polyglutamine proteins in muscle wall cells compromised the folding of co-expressed temperature-sensitive proteins, prompting interest in whether the accumulation of a misfolded protein in pathologic features of human neurodegenerative disease burdens cellular proteostatic machinery in a manner that impairs the folding of other cellular proteins.

Methods

Mice expressing high levels of mutant forms of tau and α-synuclein (αSyn), which develop inclusion pathologies of the mutant protein in brain and spinal cord, were crossed to mice expressing low levels of mutant superoxide dismutase 1 fused to yellow fluorescent protein (G85R-SOD1:YFP) for aging and neuropathological evaluation.

R

SUBMITTER: Pace MC 

PROVIDER: S-EPMC5960184 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature