Inhibition of chaperonin GroEL by a monomer of ovine prion protein and its oligomeric forms

被引：0

作者：

S. S. Kudryavtseva

Y. Y. Stroylova

I. A. Zanyatkin

T. Haertle

V. I. Muronetz

机构：

[1] Lomonosov Moscow State University,Belozersky Institute of Physico

[2] Faculty of Bioengineering and Bioinformatics,Chemical Biology

[3] Institut National de la Recherche Agronomique,Lomonosov Moscow State University

来源：

Biochemistry (Moscow) | 2016年 / 81卷

关键词：

amyloid proteins; chaperonin GroEL; prion PrP; oligomeric forms of prion protein; glyceraldehyde-3-phosphate dehydrogenase; reactivation; inhibition of chaperonin;

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摘要：

The possibility of inhibition of chaperonin functional activity by amyloid proteins was studied. It was found that the ovine prion protein PrP as well as its oligomeric and fibrillar forms are capable of binding with the chaperonin GroEL. Besides, GroEL was shown to promote amyloid aggregation of the monomeric and oligomeric PrP as well as PrP fibrils. The monomeric PrP was shown to inhibit the GroEL-assisted reactivation of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The oligomers of PrP decelerate the GroEL-assisted reactivation of GAPDH, and PrP fibrils did not affect this process. The chaperonin GroEL is capable of interacting with GAPDH and different PrP forms simultaneously. A possible role of the inhibition of chaperonins by amyloid proteins in the misfolding of the enzymes involved in cell metabolism and in progression of neurodegenerative diseases of amyloid nature is discussed.

引用

页码：1213 / 1220

页数：7