当前位置： SCI文献检索 > BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS期刊下所有文献 > Number and molecular brightness analysis reveals Htt25Q protein aggregation upon the uptake of Htt97Q aggregates.

Number and molecular brightness analysis reveals Htt25Q protein aggregation upon the uptake of Htt97Q aggregates.

Abstract：

:Number and molecular Brightness (N&B) analysis is a powerful method used to monitor protein aggregation in living cells. Here, we used the N&B method to characterize the unexpanded HTT protein oligomerization after the internalization of the mutant HTT (mHTT) which contains a CAG repeat extensions encoding for long polyglutamine (polyQ) proteins resulting in misfolding and aggregation. HEK cells expressing Htt25Q-mCherry proteins were infected with Htt97Q-EGFP aggregates, by cell to cell uptake, in cultured conditions resulting in an increasing population of dimers and tetramers compared to our controls. This study shows for the first time the impact of protein aggregation in the unexpanded Htt25Q-mCherry expressing cells that occurs from cell to cell transfer of the expanded Htt97Q-EGFP. These results signify the sporadic behavior of the polyQ inclusion that gives insight into the mechanism of protein dynamics as a consequence of secreted mHTT aggregates.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Sameni S,Zhang R,Digman MA

doi

10.1016/j.bbrc.2019.10.041

subject

Has Abstract

pub_date

2020-01-29 00:00:00

pages

133-137

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(19)31930-8

journal_volume

522

pub_type

杂志文章

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