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Therapeutic potency of heat-shock protein-70 in the pathogenesis of colorectal cancer, current status and perspectives.

08:00 EDT 1st October 2018 | BioPortfolio

Summary of "Therapeutic potency of heat-shock protein-70 in the pathogenesis of colorectal cancer, current status and perspectives."

Heat-shock protein-70 (HSP70) is critical to the folding, stability and activity of several client proteins including many responsible for cancer cell proliferation, apoptosis, drug toxicity, and metastasis. Up-regulation of HSP70 is positively associated with increased tumorigenicity as well as poor survival in colon cancer patients, supporting the diagnostic, prognostic and therapeutic potencies of HSP70 in colorectal cancer. Administration of specific pharmacological inhibitors or gene knock-down for HSP70 suppresses tumor progression and enhances tumor cells chemosensitivity. This review summarizes different tumorigenic properties of HSP70 and potential therapeutic potency of HSP70 inhibitors as a novel strategy in colorectal cancer therapy for a better understanding and hence a better management of this disease.

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This article was published in the following journal.

Name: Biochemistry and cell biology = Biochimie et biologie cellulaire
ISSN: 1208-6002
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Medical and Biotech [MESH] Definitions

A family of heat-shock proteins that contain a 70 amino-acid consensus sequence known as the J domain. The J domain of HSP40 heat shock proteins interacts with HSP70 HEAT-SHOCK PROTEINS. HSP40 heat-shock proteins play a role in regulating the ADENOSINE TRIPHOSPHATASES activity of HSP70 heat-shock proteins.

A subfamily of small heat-shock proteins that are closely related to ALPHA B-CRYSTALLIN. Hsp20 heat-shock proteins can undergo PHOSPHORYLATION by CYCLIC GMP-DEPENDENT PROTEIN KINASES.

Stress-inducible members of the heat-shock proteins 70 family. HSP72 heat shock proteins function with other MOLECULAR CHAPERONES to mediate PROTEIN FOLDING and to stabilize pre-existent proteins against aggregation.

A group of eukaryotic high-molecular mass heat-shock proteins that represent a subfamily of HSP70 HEAT-SHOCK PROTEINS. Hsp110 proteins prevent protein aggregation and can maintain denatured proteins in folding-competent states.

Heat and cold stress-inducible, transcription factors that bind to inverted 5'-NGAAN-3' pentamer DNA sequences and are regulated by poly(ADP) ribosylation. They play essential roles as transcriptional activators of the HEAT-SHOCK RESPONSE by inducing expression of large classes of MOLECULAR CHAPERONES and heat-shock proteins. They also function in DNA REPAIR; transcriptional reactivation of latent HIV-1; and pre-mRNA processing and nuclear export of HSP70 HEAT-SHOCK PROTEINS during heat stress.

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