Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases

The review highlights various aspects of the influence of chaperones on amyloid proteins associated with the development of neurodegenerative diseases and includes studies conducted in our laboratory. Different sections of the article are devoted to the role of chaperones in the pathological transfo...

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Main Authors: Vladimir I. Muronetz, Sofia S. Kudryavtseva, Evgeniia V. Leisi, Lidia P. Kurochkina, Kseniya V. Barinova, Elena V. Schmalhausen
Format: Article
Language:English
Published: MDPI AG 2022-03-01
Series:International Journal of Molecular Sciences
Subjects:
Online Access:https://www.mdpi.com/1422-0067/23/5/2747
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author Vladimir I. Muronetz
Sofia S. Kudryavtseva
Evgeniia V. Leisi
Lidia P. Kurochkina
Kseniya V. Barinova
Elena V. Schmalhausen
author_facet Vladimir I. Muronetz
Sofia S. Kudryavtseva
Evgeniia V. Leisi
Lidia P. Kurochkina
Kseniya V. Barinova
Elena V. Schmalhausen
author_sort Vladimir I. Muronetz
collection DOAJ
description The review highlights various aspects of the influence of chaperones on amyloid proteins associated with the development of neurodegenerative diseases and includes studies conducted in our laboratory. Different sections of the article are devoted to the role of chaperones in the pathological transformation of alpha-synuclein and the prion protein. Information about the interaction of the chaperonins GroE and TRiC as well as polymer-based artificial chaperones with amyloidogenic proteins is summarized. Particular attention is paid to the effect of blocking chaperones by misfolded and amyloidogenic proteins. It was noted that the accumulation of functionally inactive chaperones blocked by misfolded proteins might cause the formation of amyloid aggregates and prevent the disassembly of fibrillar structures. Moreover, the blocking of chaperones by various forms of amyloid proteins might lead to pathological changes in the vital activity of cells due to the impaired folding of newly synthesized proteins and their subsequent processing. The final section of the article discusses both the little data on the role of gut microbiota in the propagation of synucleinopathies and prion diseases and the possible involvement of the bacterial chaperone GroE in these processes.
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spelling doaj.art-b4ef619a3d1343f0945ae4b03c11256e2023-11-23T23:09:02ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-03-01235274710.3390/ijms23052747Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative DiseasesVladimir I. Muronetz0Sofia S. Kudryavtseva1Evgeniia V. Leisi2Lidia P. Kurochkina3Kseniya V. Barinova4Elena V. Schmalhausen5Belozersky Institute of Physico Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, RussiaFaculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, 119991 Moscow, RussiaFaculty of Biology, Lomonosov Moscow State University, 119991 Moscow, RussiaBelozersky Institute of Physico Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, RussiaBelozersky Institute of Physico Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, RussiaBelozersky Institute of Physico Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, RussiaThe review highlights various aspects of the influence of chaperones on amyloid proteins associated with the development of neurodegenerative diseases and includes studies conducted in our laboratory. Different sections of the article are devoted to the role of chaperones in the pathological transformation of alpha-synuclein and the prion protein. Information about the interaction of the chaperonins GroE and TRiC as well as polymer-based artificial chaperones with amyloidogenic proteins is summarized. Particular attention is paid to the effect of blocking chaperones by misfolded and amyloidogenic proteins. It was noted that the accumulation of functionally inactive chaperones blocked by misfolded proteins might cause the formation of amyloid aggregates and prevent the disassembly of fibrillar structures. Moreover, the blocking of chaperones by various forms of amyloid proteins might lead to pathological changes in the vital activity of cells due to the impaired folding of newly synthesized proteins and their subsequent processing. The final section of the article discusses both the little data on the role of gut microbiota in the propagation of synucleinopathies and prion diseases and the possible involvement of the bacterial chaperone GroE in these processes.https://www.mdpi.com/1422-0067/23/5/2747alpha-synucleinamyloid proteinschaperoneschaperoninsmicrobiotamisfolded proteins
spellingShingle Vladimir I. Muronetz
Sofia S. Kudryavtseva
Evgeniia V. Leisi
Lidia P. Kurochkina
Kseniya V. Barinova
Elena V. Schmalhausen
Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases
International Journal of Molecular Sciences
alpha-synuclein
amyloid proteins
chaperones
chaperonins
microbiota
misfolded proteins
title Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases
title_full Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases
title_fullStr Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases
title_full_unstemmed Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases
title_short Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases
title_sort regulation by different types of chaperones of amyloid transformation of proteins involved in the development of neurodegenerative diseases
topic alpha-synuclein
amyloid proteins
chaperones
chaperonins
microbiota
misfolded proteins
url https://www.mdpi.com/1422-0067/23/5/2747
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