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ATP antagonizes the crowding-induced destabilization of the human eye-lens protein γS-crystallin.

Abstract：

:In lens, αβγ-crystallins accounting for ∼90% of ocular proteins with concentrations >400 mg/ml need to remain soluble for the whole life-span and their aggregation can lead to cataract. Mysteriously, despite being a metabolically-quiescent organ, lens maintains ATP concentrations of 3-7 mM. Very recently, ATP was proposed to hydrotropically prevent aggregation of crystallins but the mechanism remains unexplored. Here by NMR, DLS and DSF, we characterized the association, thermal stability and conformation of the 178-residue human γS-crystallin at concentrations from 2 to 100 mg/ml in the absence and in the presence of ATP. Results together reveal for the first time that ATP does antagonize the crowding-induced destabilization, although it has no significant binding to γS-crystallin as well as no alteration of its conformation. Therefore, ATP prevents aggregation in lens by a novel mechanism, thus rationalizing the fact that declining concentrations of ATP upon being aged is related to age-related cataractogenesis. To restore the normal concentrations of ATP in lens may represent a promising therapeutic strategy to treat aggregation-causing eye diseases.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

He Y,Kang J,Song J

doi

10.1016/j.bbrc.2020.04.014

subject

Has Abstract

pub_date

2020-06-11 00:00:00

pages

1112-1117

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(20)30736-1

journal_volume

526

pub_type

杂志文章

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