2010
DOI: 10.1159/000296508
|View full text |Cite
|
Sign up to set email alerts
|

Dual Role of Heat Shock Proteins as Regulators of Apoptosis and Innate Immunity

Abstract: tems. In cancer, most immunotherapeutical approaches based on extracellular HSPs exploit their carrier function for immunogenic peptides. This review will focus on the roles of HSP70 and HSP90 in apoptosis and in innate immunity and how these functions are being exploited in cancer therapy.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
2

Citation Types

0
193
0
7

Year Published

2012
2012
2022
2022

Publication Types

Select...
8

Relationship

1
7

Authors

Journals

citations
Cited by 275 publications
(207 citation statements)
references
References 95 publications
0
193
0
7
Order By: Relevance
“…Data obtained in the last decade indicate that Heat shock proteins (Hsps) have anti-apoptotic and, consequently, pro-tumor properties [29,30,31]. Apoptosis contributes to tumor demise following chemotherapy but, in patient management, it is still unclear how to achieve a healthy balance between cell proliferation and death [32].…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Data obtained in the last decade indicate that Heat shock proteins (Hsps) have anti-apoptotic and, consequently, pro-tumor properties [29,30,31]. Apoptosis contributes to tumor demise following chemotherapy but, in patient management, it is still unclear how to achieve a healthy balance between cell proliferation and death [32].…”
Section: Discussionmentioning
confidence: 99%
“…In some instances, elevated levels of Hsps protect tumor cells against therapy-induced apoptosis [33]. Hsps can block both the intrinsic and the extrinsic apoptotic pathways through the interaction with proteins involved in the apoptotic process [30,31,33]. For example, high levels of Hsp27, or Hsp70, or Hsp90 inhibit apoptosis by preventing Caspase activation in a variety of cellular models [34][35][36].…”
Section: Discussionmentioning
confidence: 99%
“…[1,2] A growing body of evidence has expanded the role of HSP, which have been regarded as intracellular chaperones beyond their cytoprotective function. The main goal of the chaperones discussed extensively in the recent reviews [3,4] is to preserve cell survival by controlling the three -dimensional structure of the synthesized proteins, preventing misfolding or degradation. Therefore, HSP regulates the response to any detrimental factors such as temperature, radiation, hypoxia, toxins or infectious agents.…”
Section: Introductionmentioning
confidence: 99%
“…Among these, HSP 60, 70 and 90 have been studied extensively. [3] In each of these groups, two types of HSPs can be found: stress-induced isoforms (HSP 60, 70 and 90 alpha), as well as those constitutively and independent of stress conditions (HSP 70, HSP 90ß).…”
Section: Introductionmentioning
confidence: 99%
“…Heat shock proteins are stress proteins, which are protective against a variety of cytotoxic stresses, as seen in various diseases (Saluja, 2008;Joly, 2010). The esophageal epithelium is routinely exposed to acid reflux and thermal stress and these epithelial cells have presumably, evolved protective mechanisms to withstand environmental insults and repair damaged cells (Hopwood, 1997;Yagui-Beltran, 2001).…”
Section: Discussionmentioning
confidence: 99%