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Heat Shock Protein Chaperome Is a Multi-Faceted Vector for Tumor Cell Migratory Activity, Invasion, and Metastasis. / Fedorov, V.; Kurkin, A.; Fofanov, G.; Kaneva, Vitaliya ; Kondratenko, A.; Combs, S.E.; Shevtsov, M.

In: Cells, Vol. 14, No. 23, 2025.

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

Harvard

Fedorov, V, Kurkin, A, Fofanov, G, Kaneva, V, Kondratenko, A, Combs, SE & Shevtsov, M 2025, 'Heat Shock Protein Chaperome Is a Multi-Faceted Vector for Tumor Cell Migratory Activity, Invasion, and Metastasis', Cells, vol. 14, no. 23. https://doi.org/10.3390/cells14231837

APA

Fedorov, V., Kurkin, A., Fofanov, G., Kaneva, V., Kondratenko, A., Combs, S. E., & Shevtsov, M. (2025). Heat Shock Protein Chaperome Is a Multi-Faceted Vector for Tumor Cell Migratory Activity, Invasion, and Metastasis. Cells, 14(23). https://doi.org/10.3390/cells14231837

Vancouver

Fedorov V, Kurkin A, Fofanov G, Kaneva V, Kondratenko A, Combs SE et al. Heat Shock Protein Chaperome Is a Multi-Faceted Vector for Tumor Cell Migratory Activity, Invasion, and Metastasis. Cells. 2025;14(23). https://doi.org/10.3390/cells14231837

Author

Fedorov, V. ; Kurkin, A. ; Fofanov, G. ; Kaneva, Vitaliya ; Kondratenko, A. ; Combs, S.E. ; Shevtsov, M. / Heat Shock Protein Chaperome Is a Multi-Faceted Vector for Tumor Cell Migratory Activity, Invasion, and Metastasis. In: Cells. 2025 ; Vol. 14, No. 23.

BibTeX

@article{0d88f1b5fd7640e4b9199d043aaf8b55,
title = "Heat Shock Protein Chaperome Is a Multi-Faceted Vector for Tumor Cell Migratory Activity, Invasion, and Metastasis",
abstract = "Heat shock proteins (HSPs), in particular, representatives of the HSP70 and HSP90 families, are the folding centers of cell proteins and have been proven to be overexpressed in various types of solid and hematological malignancies. With their involvement in a number of cellular functions (e.g., protection from various stresses including radiochemotherapy, transport regulation, apoptotic signal inhibition, etc.), these chaperones are a valuable target for cancer progression research. However, recent focus has shifted to the HSP interaction network, which includes many molecules involved in cell migration and invasion pathways. Investigating the interplay between different co-chaperones and their effect on cell motility may help with establishing a palette of available diagnostic and therapeutic targets for highly invasive cancer types. In this review, we describe current models of the HSP functional cycle and recent studies proving links between these cycle regulators and contributions to cell migration. Based on detailed studies of various co-chaperones{\textquoteright} involvement in cancer progression, the network approach gives much necessary molecular context to previously established HSP functions. {\textcopyright} 2025 by the authors.",
keywords = "cancer cell migration, cancer progression, chaperome, heat shock proteins, HSP70, HSP90, invasion, molecular network, chaperone, heat shock protein, heat shock protein 90, apoptosis, cancer cell, cancer growth, cell function, cell migration, cell motility, human, metastasis, review, tumor cell, tumor invasion, animal, cell motion, metabolism, neoplasm, pathology, Animals, Cell Movement, Heat-Shock Proteins, Humans, Neoplasm Invasiveness, Neoplasm Metastasis, Neoplasms",
author = "V. Fedorov and A. Kurkin and G. Fofanov and Vitaliya Kaneva and A. Kondratenko and S.E. Combs and M. Shevtsov",
note = "Export Date: 19 February 2026; Cited By: 0; Correspondence Address: M. Shevtsov; Laboratory of Biomedical Nanotechnologies, Institute of Cytology of the Russian Academy of Sciences, RAS, 194064, Russian Federation; email: maxim.shevtsov@tum.de",
year = "2025",
doi = "10.3390/cells14231837",
language = "Английский",
volume = "14",
journal = "Cells",
issn = "2073-4409",
publisher = "MDPI AG",
number = "23",

}

RIS

TY - JOUR

T1 - Heat Shock Protein Chaperome Is a Multi-Faceted Vector for Tumor Cell Migratory Activity, Invasion, and Metastasis

AU - Fedorov, V.

AU - Kurkin, A.

AU - Fofanov, G.

AU - Kaneva, Vitaliya

AU - Kondratenko, A.

AU - Combs, S.E.

AU - Shevtsov, M.

N1 - Export Date: 19 February 2026; Cited By: 0; Correspondence Address: M. Shevtsov; Laboratory of Biomedical Nanotechnologies, Institute of Cytology of the Russian Academy of Sciences, RAS, 194064, Russian Federation; email: maxim.shevtsov@tum.de

PY - 2025

Y1 - 2025

N2 - Heat shock proteins (HSPs), in particular, representatives of the HSP70 and HSP90 families, are the folding centers of cell proteins and have been proven to be overexpressed in various types of solid and hematological malignancies. With their involvement in a number of cellular functions (e.g., protection from various stresses including radiochemotherapy, transport regulation, apoptotic signal inhibition, etc.), these chaperones are a valuable target for cancer progression research. However, recent focus has shifted to the HSP interaction network, which includes many molecules involved in cell migration and invasion pathways. Investigating the interplay between different co-chaperones and their effect on cell motility may help with establishing a palette of available diagnostic and therapeutic targets for highly invasive cancer types. In this review, we describe current models of the HSP functional cycle and recent studies proving links between these cycle regulators and contributions to cell migration. Based on detailed studies of various co-chaperones’ involvement in cancer progression, the network approach gives much necessary molecular context to previously established HSP functions. © 2025 by the authors.

AB - Heat shock proteins (HSPs), in particular, representatives of the HSP70 and HSP90 families, are the folding centers of cell proteins and have been proven to be overexpressed in various types of solid and hematological malignancies. With their involvement in a number of cellular functions (e.g., protection from various stresses including radiochemotherapy, transport regulation, apoptotic signal inhibition, etc.), these chaperones are a valuable target for cancer progression research. However, recent focus has shifted to the HSP interaction network, which includes many molecules involved in cell migration and invasion pathways. Investigating the interplay between different co-chaperones and their effect on cell motility may help with establishing a palette of available diagnostic and therapeutic targets for highly invasive cancer types. In this review, we describe current models of the HSP functional cycle and recent studies proving links between these cycle regulators and contributions to cell migration. Based on detailed studies of various co-chaperones’ involvement in cancer progression, the network approach gives much necessary molecular context to previously established HSP functions. © 2025 by the authors.

KW - cancer cell migration

KW - cancer progression

KW - chaperome

KW - heat shock proteins

KW - HSP70

KW - HSP90

KW - invasion

KW - molecular network

KW - chaperone

KW - heat shock protein

KW - heat shock protein 90

KW - apoptosis

KW - cancer cell

KW - cancer growth

KW - cell function

KW - cell migration

KW - cell motility

KW - human

KW - metastasis

KW - review

KW - tumor cell

KW - tumor invasion

KW - animal

KW - cell motion

KW - metabolism

KW - neoplasm

KW - pathology

KW - Animals

KW - Cell Movement

KW - Heat-Shock Proteins

KW - Humans

KW - Neoplasm Invasiveness

KW - Neoplasm Metastasis

KW - Neoplasms

U2 - 10.3390/cells14231837

DO - 10.3390/cells14231837

M3 - статья

VL - 14

JO - Cells

JF - Cells

SN - 2073-4409

IS - 23

ER -

ID: 149269095