Heat shock proteins in cancer: chaperones of tumorigenesis.

@article{Calderwood2006HeatSP,
  title={Heat shock proteins in cancer: chaperones of tumorigenesis.},
  author={Stuart K. Calderwood and Md. Abdul Khaleque and Douglas B. Sawyer and Daniel Ram{\'o}n Ciocca},
  journal={Trends in biochemical sciences},
  year={2006},
  volume={31 3},
  pages={
          164-72
        }
}
The heat shock proteins (HSPs) induced by cell stress are expressed at high levels in a wide range of tumors and are closely associated with a poor prognosis and resistance to therapy. The increased transcription of HSPs in tumor cells is due to loss of p53 function and to higher expression of the proto-oncogenes HER2 and c-Myc, and is crucial to tumorigenesis. The HSP family members play overlapping, essential roles in tumor growth both by promoting autonomous cell proliferation and by… Expand
Heat Shock Proteins Promote Cancer: It's a Protection Racket.
TLDR
Current data strongly support efforts to target HSPs in cancer treatment, and mainly focuses on Hsp27, Hsp70, and Hsp90. Expand
Heat Shock Proteins in Cancer Immunotherapy
TLDR
A review discusses recent advances and perspectives on the research of HSP-based cancer immunotherapy and suggests these highly expressed HSPs may be exploited as viable immunotherapeutic targets for different types of cancers. Expand
Heat shock proteins as novel therapeutic targets in cancer.
TLDR
Members of the HSP family have been implicated in cancer growth as promoting tumour cell proliferation as well as inhibiting cellular death pathways and inhibitors of HSP90 have emerged as potentially beneficial anticancer agents. Expand
Heat shock proteins in hepatocellular carcinoma: Molecular mechanism and therapeutic potential
TLDR
The expression profiles, functions and molecular mechanisms of HSPs (HSP27, HSP70 and HSP90) as well as a HSP‐like protein (clusterin) in HCC are summarized and progression and challenges in targeting these H SPs as novel therapeutic strategies in H CC are addressed. Expand
Targeting heat shock proteins in cancer.
TLDR
This review describes the different molecules and approaches being used or proposed in cancer therapy based on the in inhibition of HSP90, HSP70 and HSP27. Expand
Heat shock proteins in cancer: targeting the 'chaperones'.
TLDR
The function of Hsps is described focusing on current efforts in exploiting the attributes of HSps as potential targets for anticancer therapy, including Hsp90, which has several client proteins and is emerging as a particularly exciting cancer target. Expand
Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets
TLDR
The role of membrane-associated molecular chaperones in normal and tumor cells is comprehensively reviewed with implications of these proteins as plausible targets for cancer therapy and diagnostics. Expand
Implications of Heat Shock Proteins in Carcinogenesis and Cancer Progression
TLDR
This chapter examines the participation of the Hsp response in tumor cell transformation, either by up-regulation or down-regulation of specific Hsp, which can explain the variations in Hsp expression found in pre-neoplastic and neoplastic human tumors in different tissues and organs. Expand
The heat shock proteins as targets for radiosensitization and chemosensitization in cancer
TLDR
Attempts to target these proteins, particularly the small HSPs, in developing potent radiation and chemotherapy sensitizers, are focused on, as well as proposed mechanisms for this sensitization effect. Expand
Heat Shock Proteins at the Crossroads between Cancer and Alzheimer's Disease
TLDR
Cancer and Alzheimer's disease have plenty of overlapping regions in molecular genetics and cell biology associated with Hsp70/90, which make existing anticancer drugs target Hsp 70/90 which might be used in AD therapy. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 89 REFERENCES
Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms.
TLDR
The first thorough analysis of the expression and function of the cytosolic Hsp70 proteins in human cancer cells is presented and HSp70-2 is identified, a protein essential for spermatogenesis, as an important regulator of cancer cell growth. Expand
Heat shock protein 90
TLDR
Hsp90 inhibitors may circumvent the characteristic genetic plasticity that has allowed cancer cells to eventually evade the toxic effects of most molecularly targeted agents, and should augment the treatment of multiple forms of cancer. Expand
Hsp90 inhibitors as novel cancer chemotherapeutic agents.
  • L. Neckers
  • Biology, Medicine
  • Trends in molecular medicine
  • 2002
TLDR
Because of the chemoprotective activity of several proteins that are Hsp90 clients, the combination of an HSp90 inhibitor with a standard chemotherapeutic agent could dramatically increase the in vivo efficacy of the therapeutic agent. Expand
Heat Shock Protein 70 Is Required for the Survival of Cancer Cells
TLDR
The results indicate that the high expression of Hsp70 is a prerequisite for the survival of human cancer cells of various origins and reveal HSp70 as the only protein described so far whose expression is specifically needed for thesurvival of tumorigenic cells. Expand
Induction of heat shock proteins by heregulin β1 leads to protection from apoptosis and anchorage-independent growth
TLDR
It is shown that HSP elevation in tumor cells can be induced by the highly malignant factor heregulin β1 (HRGβ1), which induces HSP expression through heat shock transcription factor 1 (HSF1), indicating a role for HSF1 in this tumorigenic pathway. Expand
Hsp90 and Cdc37 -- a chaperone cancer conspiracy.
  • L. Pearl
  • Medicine, Biology
  • Current opinion in genetics & development
  • 2005
TLDR
The Hsp90 molecular chaperone system is involved in the activation of an important set of cell regulatory proteins, including many whose disregulation drives cancer, and is an important target for future anti-cancer drug development. Expand
Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications
TLDR
Although Hsp levels are not informative at the diagnostic level, they are useful biomarkers for carcinogenesis in some tissues and signal the degree of differentiation and the aggressiveness of some cancers. Expand
Message in a bottle: Role of the 70‐kDa heat shock protein family in anti‐tumor immunity
TLDR
The ability of HSP70‐peptide complexes (HSP 70‐PC) to break tolerance and cause tumor regression employs these dual properties as signaling ligand and antigen transporter. Expand
[Heat shock proteins as molecular chaperones].
  • A. Arrigo
  • Chemistry, Medicine
  • Medecine sciences : M/S
  • 2005
TLDR
Cells have developed a conserved defense mechanism aimed at reducing the deleterious effects induced by protein folding alteration, characterized by the expression of a small number of genes encoding specific proteins, named Hsps, which act as molecular chaperones through their ability to refold polypeptides with an altered conformation. Expand
The Hsp90 complex--a super-chaperone machine as a novel drug target.
TLDR
Interestingly, under physiological conditions, Hsp90 seems to perform its chaperone function in a complex with a set of partner proteins, suggesting that the Hsp 90 complex is a multi-chaperone machine specialized in guiding the maturation of conformationally labile proteins. Expand
...
1
2
3
4
5
...