Apoptotic tumor cell death under the influence of the cytotoxic complex Tag7–Hsp70 is induced by interaction with the TNFR1 receptor

Ivanova, Olga K.; Sharapova, Tatiana N.; Romanova, E. A.; Sashchenko, Lidia P.; Гнучев, Н. В.; Yashin, Denis V.

doi:10.1134/s0012496616010038

Cited by 1 publication

(1 citation statement)

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“…Another mechanism, how extracellular HSP70 might affect tumour cells is the complex formation of the innate immunity protein Tag7 with HSP70 [62,63]. It has been shown that interaction of the Tag7-HSP70 complex with TNFR1 triggers the activation of RIP1-kinase, an increase in intracellular concentration of Ca 2þ ions and an activation of calpains which result in the permeabilization of lysosomal membranes [63][64][65][66].…”

Section: Role Of Intracellular Membrane and Extracellular Heat Shock Protein 70 In Tumour Cellsmentioning

confidence: 99%

Membrane heat shock protein 70: a theranostic target for cancer therapy

Shevtsov

Gao

Multhoff

2017

Phil. Trans. R. Soc. B

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Members of the 70 kDa stress protein family are found in nearly all subcellular compartments of nucleated cells where they fulfil a number of chaperoning functions. Heat shock protein 70 (HSP70), also termed HSPA1A, the major stress-inducible member of this family is overexpressed in a large variety of different tumour types. Apart from its intracellular localization, a tumour-selective HSP70 membrane expression has been determined. A membrane HSP70–positive tumour phenotype is associated with aggressiveness and therapy resistance, but also serves as a recognition structure for targeted therapies. Furthermore, membrane-bound and extracellularly residing HSP70 derived from tumour cells play pivotal roles in eliciting anti-tumour immune responses. Herein, we want to shed light on the multiplicity of different activities of HSP70, depending on its intracellular, membrane and extracellular localization with the goal to use membrane HSP70 as a target for novel therapies including nanoparticle-based approaches for the treatment of cancer.This article is part of the theme issue ‘Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective’.

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