Heat-shock protein HSP70 decreases activity of proteasomes in human neuroblastoma cells treated by amyloid-beta 1-42 with isomerized Asp7

A. V. Morozov; M. M. Yurinskaya; V. A. Mitkevich; D. G. Garbuz; O. V. Preobrazhenskaia; M. G. Vinokurov; M. B. Evgen'ev; V. L. Karpov; A. A. Makarov

doi:10.7868/S0026898416060136

Heat-shock protein HSP70 decreases activity of proteasomes in human neuroblastoma cells treated by amyloid-beta 1-42 with isomerized Asp7

A. V. Morozov, M. M. Yurinskaya, V. A. Mitkevich, D. G. Garbuz, O. V. Preobrazhenskaia, M. G. Vinokurov, M. B. Evgen'ev, V. L. Karpov, A. A. Makarov

Research output: Contribution to journal › Article › peer-review

Abstract

Experimental evidences indicate that heat-shock protein 70 (HSP70) can serve as a prospective therapeutic agent to treat Alzheimer's disease (AD). It has demonstrated a neuroprotective effect in vivo on mice models of AD. Moreover, HSP70 decreases oxidative stress in neurons induced by amyloid-β (Aβ42) and its more toxic form with isomerized Asp7 (isoAβ42). The dysfunction of Ubiquitin-proteasome system (UPS) is observed in AD. UPS is responsible for the degradation of the majority of cellular proteins and plays an important role in protecting cells from oxidative stress. Here, we have shown that the incubation of human neuroblastoma cells SK-N-SH with isoAβ42 increases the activity of intracellular proteasomes, which are the principal elements of the UPS. On the contrary, the proteasomal activity was decreased in isoAβ42-treated cells in the presence of exogenous HSP70. These results highlight the existence of an interplay between Aβ peptides, proteasomes, and HSP70.

Original language	English
Pages (from-to)	166-171
Number of pages	6
Journal	Molekulyarnaya Biologiya
Volume	51
Issue number	1
DOIs	https://doi.org/10.7868/S0026898416060136
State	Published - 1 Jan 2017
Externally published	Yes

Keywords

HSP70
amyloid-β peptide (Aβ42) isoAβ42
neuroblastoma SK-N-SH
proteasome

ASJC Scopus subject areas

General Medicine

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.7868/S0026898416060136

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Morozov, A. V., Yurinskaya, M. M., Mitkevich, V. A., Garbuz, D. G., Preobrazhenskaia, O. V., Vinokurov, M. G., Evgen'ev, M. B., Karpov, V. L., & Makarov, A. A. (2017). Heat-shock protein HSP70 decreases activity of proteasomes in human neuroblastoma cells treated by amyloid-beta 1-42 with isomerized Asp7. Molekulyarnaya Biologiya, 51(1), 166-171. https://doi.org/10.7868/S0026898416060136

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title = "Heat-shock protein HSP70 decreases activity of proteasomes in human neuroblastoma cells treated by amyloid-beta 1-42 with isomerized Asp7",

abstract = "Experimental evidences indicate that heat-shock protein 70 (HSP70) can serve as a prospective therapeutic agent to treat Alzheimer's disease (AD). It has demonstrated a neuroprotective effect in vivo on mice models of AD. Moreover, HSP70 decreases oxidative stress in neurons induced by amyloid-β (Aβ42) and its more toxic form with isomerized Asp7 (isoAβ42). The dysfunction of Ubiquitin-proteasome system (UPS) is observed in AD. UPS is responsible for the degradation of the majority of cellular proteins and plays an important role in protecting cells from oxidative stress. Here, we have shown that the incubation of human neuroblastoma cells SK-N-SH with isoAβ42 increases the activity of intracellular proteasomes, which are the principal elements of the UPS. On the contrary, the proteasomal activity was decreased in isoAβ42-treated cells in the presence of exogenous HSP70. These results highlight the existence of an interplay between Aβ peptides, proteasomes, and HSP70.",

keywords = "HSP70, amyloid-β peptide (Aβ42) isoAβ42, neuroblastoma SK-N-SH, proteasome",

author = "Morozov, {A. V.} and Yurinskaya, {M. M.} and Mitkevich, {V. A.} and Garbuz, {D. G.} and Preobrazhenskaia, {O. V.} and Vinokurov, {M. G.} and Evgen'ev, {M. B.} and Karpov, {V. L.} and Makarov, {A. A.}",

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doi = "10.7868/S0026898416060136",

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Morozov, AV, Yurinskaya, MM, Mitkevich, VA, Garbuz, DG, Preobrazhenskaia, OV, Vinokurov, MG, Evgen'ev, MB, Karpov, VL & Makarov, AA 2017, 'Heat-shock protein HSP70 decreases activity of proteasomes in human neuroblastoma cells treated by amyloid-beta 1-42 with isomerized Asp7', Molekulyarnaya Biologiya, vol. 51, no. 1, pp. 166-171. https://doi.org/10.7868/S0026898416060136

TY - JOUR

T1 - Heat-shock protein HSP70 decreases activity of proteasomes in human neuroblastoma cells treated by amyloid-beta 1-42 with isomerized Asp7

AU - Morozov, A. V.

AU - Yurinskaya, M. M.

AU - Mitkevich, V. A.

AU - Garbuz, D. G.

AU - Preobrazhenskaia, O. V.

AU - Vinokurov, M. G.

AU - Evgen'ev, M. B.

AU - Karpov, V. L.

AU - Makarov, A. A.

PY - 2017/1/1

Y1 - 2017/1/1

N2 - Experimental evidences indicate that heat-shock protein 70 (HSP70) can serve as a prospective therapeutic agent to treat Alzheimer's disease (AD). It has demonstrated a neuroprotective effect in vivo on mice models of AD. Moreover, HSP70 decreases oxidative stress in neurons induced by amyloid-β (Aβ42) and its more toxic form with isomerized Asp7 (isoAβ42). The dysfunction of Ubiquitin-proteasome system (UPS) is observed in AD. UPS is responsible for the degradation of the majority of cellular proteins and plays an important role in protecting cells from oxidative stress. Here, we have shown that the incubation of human neuroblastoma cells SK-N-SH with isoAβ42 increases the activity of intracellular proteasomes, which are the principal elements of the UPS. On the contrary, the proteasomal activity was decreased in isoAβ42-treated cells in the presence of exogenous HSP70. These results highlight the existence of an interplay between Aβ peptides, proteasomes, and HSP70.

AB - Experimental evidences indicate that heat-shock protein 70 (HSP70) can serve as a prospective therapeutic agent to treat Alzheimer's disease (AD). It has demonstrated a neuroprotective effect in vivo on mice models of AD. Moreover, HSP70 decreases oxidative stress in neurons induced by amyloid-β (Aβ42) and its more toxic form with isomerized Asp7 (isoAβ42). The dysfunction of Ubiquitin-proteasome system (UPS) is observed in AD. UPS is responsible for the degradation of the majority of cellular proteins and plays an important role in protecting cells from oxidative stress. Here, we have shown that the incubation of human neuroblastoma cells SK-N-SH with isoAβ42 increases the activity of intracellular proteasomes, which are the principal elements of the UPS. On the contrary, the proteasomal activity was decreased in isoAβ42-treated cells in the presence of exogenous HSP70. These results highlight the existence of an interplay between Aβ peptides, proteasomes, and HSP70.

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Heat-shock protein HSP70 decreases activity of proteasomes in human neuroblastoma cells treated by amyloid-beta 1-42 with isomerized Asp7

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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