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Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties.

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TLDR
The depletion or inhibition of HSP27 and HS70 frequently reduces the size of the tumors and even can cause their complete involution (for HSP70).
Abstract
Heat shock proteins (HSP) HSP27 and HSP70 are expressed in response to a wide variety of physiological and environmental insults including anticancer chemotherapy, thus allowing the cell to survive to lethal conditions. Several mechanisms account for the cytoprotective effect of HSP27 and HSP70. (1) Both proteins are powerful chaperones. (2) They both inhibit key effectors of the apoptotic machinery at the pre and post-mitochondrial level. (3) They participate in the proteasome-mediated degradation of proteins under stress conditions, thereby contributing to the so called "protein triage". In cancer cells, the expression of HSP27 and/or HSP70 is abnormally high, and both HSP27 and HSP70 may participate in oncogenesis and in resistance to chemotherapy. In rodent models, HSP27 or HSP70 over-expression increases tumor growth and metastatic potential. The depletion or inhibition of HSP27 and HS70 frequently reduces the size of the tumors and even can cause their complete involution (for HSP70). Therefore, the inhibition of HSP70 and HSP27 has become a novel strategy of cancer therapy.

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Thermal ablation of tumours: biological mechanisms and advances in therapy.

TL;DR: The mechanisms of tumour cell death that are induced by the most common thermoablative techniques are examined and the rapidly developing areas of research in the field are discussed, including combinatorial ablation and immunotherapy, synergy with conventional chemotherapy and radiation, and the development of a new ablation modality in irreversible electroporation.
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Lysosomal membrane permeabilization in cell death

TL;DR: The regulation of LMP is perturbed in cancer cells, suggesting that specific strategies for LMP induction might lead to novel therapeutic avenues.
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Cellular Stress Responses: Cell Survival and Cell Death

TL;DR: The implications of cellular stress responses to human physiology and diseases are manifold and will be discussed in this review in the context of some major world health issues such as diabetes, Parkinson's disease, myocardial infarction, and cancer.
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Regulation of Ligands for the NKG2D Activating Receptor

TL;DR: The numerous pathways that have been implicated in the regulation of NKG2D ligands are reviewed, the pathologic states in which those pathways are likely to act are discussed, and the findings are synthesized into general schemes of NKD ligand regulation in NK cell responses to cancer and infection.
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Hepatocyte Necrosis Induced by Oxidative Stress and IL-1α Release Mediate Carcinogen-Induced Compensatory Proliferation and Liver Tumorigenesis

TL;DR: Hepatocyte-specific p38 alpha ablation enhanced ROS accumulation and liver damage, which were prevented upon administration of an antioxidant, and IL-1 alpha release by necrotic hepatocytes is therefore an important mediator of liver tumorigenesis.
References
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Journal ArticleDOI

Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade

TL;DR: Mutation of the active site of caspase-9 attenuated the activation of cazase-3 and cellular apoptotic response in vivo, indicating that casp enzyme-9 is the most upstream member of the apoptotic protease cascade that is triggered by cytochrome c and dATP.
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Molecular characterization of mitochondrial apoptosis-inducing factor

TL;DR: The identification and cloning of an apoptosis-inducing factor, AIF, which is sufficient to induce apoptosis of isolated nuclei is reported, indicating that AIF is a mitochondrial effector of apoptotic cell death.
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Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition.

TL;DR: The identification of a novel protein, Smac, which promotes caspase activation in the cytochrome c/Apaf-1/caspase-9 pathway and increases cells' sensitivity to apoptotic stimuli is reported.
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Hsp70 chaperones: cellular functions and molecular mechanism.

TL;DR: This work has shown that for specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100, and this ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target H Sp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the HSp70-substrate complex.
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NF-κB activation by tumour necrosis factor requires the Akt serine–threonine kinase

TL;DR: It is shown that the Akt serine–threonine kinase is involved in the activation of NF-κB by tumour necrosis factor (TNF), and that Akt is part of a signalling pathway that is necessary for inducing key immune and inflammatory responses.
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