Heat shock protein Hsp70: prerequisites for use as a medicinal product


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Heat shock protein Hsp70 is one of the main cytoprotection components under the action of various external stimuli. The analysis of the literature data shows that nowadays, the researches’ overwhelming evidence has proven the role of Hsp70 as a biological target for the drug development; however, the ideas about its use as a drug are often multidirectional.

The aim of the article is to analyze and generalize the literature data on the features of the physiological functions of heat shock protein Hsp 70, and indicate the possibilities of its use for the pharmacological correction of various pathological conditions.

Materials and methods. In the process of selecting material for writing this review article, such databases as Google Patents, Science Research Portal, Google Scholar, ScienceDirect, CiteSeer, Publications, ResearchIndex, Ingenta, PubMed, KEGG, etc. were used The following words and word combinations were selected as markers for identifying the literature: Hsp70, Hsp70 stroke, Hsp70 neuroprotection, Hsp70 cytoprotection, recombinant drugs.

Results. In this review, the pharmacology of one of the key members of this family, Hsp70, was focused on. The literary analysis confirms that this molecule is an endogenous regulator of many physiological processes and demonstrates tissue protective effects in modeling ischemic, neurodegenerative and inflammatory processes. The use of recombinant exogenous Hsp70 mimics the endogenous function of the protein, indicating the absence of a number of typical limitations characteristic of pharmacotherapy with high molecular weight compounds, such as immunogenicity, a rapid degradation by proteases, or a low penetration of histohematogenous barriers.

Conclusion. Thus, Hsp70 may become a promising agent for clinical trials as a drug for the treatment of patients with neurological, immunological, and cardiovascular profiles.

作者简介

Vladimir Pokrovsky

Belgorod State National Research University (NRU “BelSU”)

编辑信件的主要联系方式.
Email: vmpokrovsky@yandex.ru
ORCID iD: 0000-0003-3138-2075

6th year student

俄罗斯联邦, 85, Pobeda St., Belgorod, 308015

Evgeniy Patrakhanov

Belgorod State National Research University (NRU “BelSU”)

Email: pateval7@gmail.com
ORCID iD: 0000-0002-8415-4562

6th year student of the Medical Institute

俄罗斯联邦, 85, Pobeda St., Belgorod, 308015

Oleg Antsiferov

Belgorod State National Research University (NRU “BelSU”)

Email: antsiferov@bsu.edu.ru
ORCID iD: 0000-0001-6439-2419

Senior Lecturer, Department of Faculty Therapy

俄罗斯联邦, 85, Pobeda St., Belgorod, 308015

Inga Kolesnik

Belgorod State National Research University (NRU “BelSU”)

Email: kolesnik_inga@mail.ru

sociate Professor of the Department of Pharmacology and Clinical Pharmacology

俄罗斯联邦, 85, Pobeda St., Belgorod, 308015

Anastasia Belashova

Belgorod State National Research University (NRU “BelSU”)

Email: belashova_av@mail.ru
ORCID iD: 0000-0001-9737-6378

student of Medical Institute

俄罗斯联邦, 85, Pobeda St., Belgorod, 308015

Valeria Soldatova

Belgorod State National Research University (NRU “BelSU”)

Email: lorsoldatova@gmail.com
ORCID iD: 0000-0002-9970-4109

postgraduate student of the Department of Pharmacology and Clinical Pharmacology

俄罗斯联邦, 85, Pobeda St., Belgorod, 308015

Olga Pokopeiko

First Moscow State Medical University n. a. I.M. Sechenov (Sechenov University)

Email: OPokopejko@mail.ru

4th year student

俄罗斯联邦, Bldg. 2, 8, Trubetskaya St., Moscow, 119991

Anastasia Karagodina

Belgorod State National Research University (NRU “BelSU”)

Email: anastasiavolmedic@gmail.com
ORCID iD: 0000-0001-9440-5866

6th year student, the Medical Institute

俄罗斯联邦, 85, Pobeda St., Belgorod, 308015

Ivan Arkhipov

Belgorod State National Research University (NRU “BelSU”)

Email: iaarkhipovbsu@gmail.com

6th year student of the Medical Institute

俄罗斯联邦, 85, Pobeda St., Belgorod, 308015

Diana Voronina

Belgorod State National Research University (NRU “BelSU”)

Email: diana0085@inbox.ru

Research Institute of Pharmacology of Living Systems

俄罗斯联邦, 85, Pobeda St., Belgorod, 308015

Daria Sushkova

Belgorod State National Research University (NRU “BelSU”)

Email: maslova_d@bsu.edu.ru

Junior Researcher, Research Institute of Pharmacology of Living Systems

俄罗斯联邦, 85, Pobeda St., Belgorod, 308015

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2. Figure 1 – Model of the Hsp70 oligomerization assembly line. Note: Cellular stress changes chaperone conformation, which facilitates Hsp 70 oligomerization. Co-chaperones and associated substrates bind to Hsp 70 oligomer, forming active chaperone complex

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3. Figure 2 – Interaction of Hsp70 with apoptosis and inflammation regulating proteins

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版权所有 © Pokrovsky V.M., Patrakhanov E.A., Antsiferov O.V., Kolesnik I.M., Belashova A.V., Soldatova V.A., Pokopeiko O.N., Karagodina A.Y., Arkhipov I.A., Voronina D.G., Sushkova D.N., 2021

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