[Hsp70 chaperone and the prospects of its application in anticancer therapy]

Full Abstract

Major stress protein Hsp70 is known to possess two important properties:
ATP-dependent activity and protective activity; these two are thought to play a significant role in anticancer therapy. Many malignant tumors contain high amounts of intracellular Hsp70. Moreover, many anticancer drugs themselves are able to elevate Hsp70 expression in tumor cells. Since Hsp70 was found to disturb many signal pathways of apoptosis in many points, the high chaperone expression may lead to an increased resistance of tumor cells to anticancer drugs. On the other hand, when overexpressed by a certain mechanism, Hsp70 is able to emerge at the cell surface by itself or together with tumor antigens and present these to immune cells T-lymphocytes and natural killers, in such a manner that makes cancer cell recognized and abolished. These properties make Hsp70 very promising instrument in designing some novel anticancer vaccines.

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Author information

Author/s: Guzhova, I V (IV); Novoselov, S S (SS); Margulis, B A (BA);

Journal and publication information

Publication Type: English Abstract; Journal Article; Review

Journal: Tsitologiia (Tsitologiia), published in Russia (Federation). (Language: rus)

Reference: 2005-; vol 47 (issue 3) : pp 187-99

Dates: Created 2006/05/18; Completed 2006/06/13; Revised 2008/11/21;

PMID: 16706162, status: MEDLINE (last retrieval date: 12/26/2008)

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Animals
Antigens, Neoplasm - metabolism
Apoptosis - physiology
Cancer Vaccines - therapeutic use
DNA-Binding Proteins - metabolism
Eukaryotic Cells - immunology; metabolism; pathology
HSP40 Heat-Shock Proteins - metabolism
HSP70 Heat-Shock Proteins - chemistry; physiology; therapeutic use
Humans

Immunity, Cellular
Immunologic Factors - therapeutic use
Killer Cells, Natural - immunology
Models, Molecular
Neoplasms - therapy
Protein Structure, Tertiary
Signal Transduction - drug effects
T-Lymphocytes - immunology
Transcription Factors - metabolism

Associated Chemicals: Antigens, Neoplasm (0) ; BCL2-associated athanogene 1 protein (0) ; Cancer Vaccines (0) ; DNA-Binding Proteins (0) ; DNAJB1 protein, human (0) ; HSP40 Heat-Shock Proteins (0) ; HSP70 Heat-Shock Proteins (0) ; Immunologic Factors (0) ; Transcription Factors (0)

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