Heat shock proteins on the surface of tumor cells as a target for anti-tumor therapy

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According to WHO, oncological diseases are the cause of ~5 million people deaths annually. To date, there is no universal solution to fight cancer, despite outstanding achievements in the field of radiotherapy, chemotherapy, and immunotherapy. In this regard, there is a need to develop new approaches to antitumor therapy, in particular based on the search and use of targeted molecules that allow killing tumor cells of various types with high efficiency, without significant toxic effects on healthy organs and tissues. This review presents the characteristics of the main heat shock protein (HSP) families, the features of their expression in tumor cells and the possibility of using monoclonal antibodies to these proteins as a guiding vector for antitumor immunotherapy.

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Sobre autores

A. Makarova

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry RAS; Lomonosov Moscow State University

Email: amsap@mail.ru
Rússia, ul. Miklukho-Maklaya 16/10, Moscow, 117997; Leninskie Gory 1, Moscow, 119991

V. Kostenko

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry RAS; Lomonosov Moscow State University

Email: amsap@mail.ru
Rússia, ul. Miklukho-Maklaya 16/10, Moscow, 117997; Leninskie Gory 1, Moscow, 119991

O. Ovsyanikova

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry RAS; Lomonosov Moscow State University

Email: amsap@mail.ru
Rússia, ul. Miklukho-Maklaya 16/10, Moscow, 117997; Leninskie Gory 1, Moscow, 119991

E. Svirshchevskaya

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry RAS

Email: amsap@mail.ru
Rússia, ul. Miklukho-Maklaya 16/10, Moscow, 117997

G. Lutsenko

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry RAS

Email: amsap@mail.ru
Rússia, ul. Miklukho-Maklaya 16/10, Moscow, 117997

A. Sapozhnikov

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry RAS

Autor responsável pela correspondência
Email: amsap@mail.ru
Rússia, ul. Miklukho-Maklaya 16/10, Moscow, 117997

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2. Fig. 1. Mechanism of protein structure refolding by HSP70. HSP40 (DnaJ), containing the J-domain, transports misfolded protein (substrate) to HSP70 (1); HSP40 triggers ATP hydrolysis and conformational changes in the HSP70 structure, stabilizing the bonds between the substrate and HSP70 (2); the nucleotide exchange factor GrpE (HSP10) is involved in nucleotide exchange in the HSP70 molecule (3); the released substrate either comes to its native conformation (resolved conformation) (4), or its structure is unresolved (unresolved), and, again binding to HSP70, the protein is sent for refolding [15].

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