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Updated: May 23, 2026

Intracellular Refolding Assay
Published on: January 24, 2012
Role of Hsp70 in cancer growth and survival
Marcus P D Hatfield1, Sándor Lovas
1Department of Biomedical Sciences, Creighton University School of Medicine, 2500 California Plaza, Omaha, NE 68178, USA.
Abstract:
Hsp70 is a highly conserved protein that refolds misfolded proteins and has numerous housekeeping functions which regulate apoptosis and other cell activities. Hsp70 consists of a nucleotide binding domain which binds ATP and a substrate binding domain that binds misfolded proteins. The substrate binding domain contains a peptide binding pocket which is covered by a helical lid. In humans, there are three major cytosolic Hsp70 isotypes, Hsp70-8, Hsp70-1 and Hsp70-2. Leukemic and numerous other cancer cells have a greater amount of Hsp70-1 and -2, which help the cancer cells inhibit apoptosis in response to stress. This review summarizes the structure and role of Hsp70 proteins in cancer survival.
Insights
Heat shock protein 70 (Hsp70) helps cancer cells survive by inhibiting apoptosis. This review covers Hsp70 structure and its role in cancer, focusing on Hsp70-1 and Hsp70-2 isotypes.
Area of Science:
- Molecular Biology
- Cell Biology
- Oncology
Background:
- Heat shock protein 70 (Hsp70) is a conserved protein crucial for cellular homeostasis.
- Hsp70 functions include refolding misfolded proteins and regulating apoptosis.
- Hsp70 comprises a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD).
Purpose of the Study:
- To review the structure and function of Hsp70 proteins.
- To elucidate the role of Hsp70 in cancer cell survival.
- To highlight the increased expression of Hsp70-1 and Hsp70-2 in cancer cells.
Main Methods:
- Literature review of Hsp70 structure and function.
- Analysis of Hsp70 expression in cancer.
- Summary of Hsp70's role in apoptosis regulation in cancer.
Main Results:
- Hsp70 proteins are vital for cellular processes, including protein folding and apoptosis.
- Cancer cells, particularly leukemic cells, exhibit elevated levels of Hsp70-1 and Hsp70-2.
- Increased Hsp70 expression contributes to cancer cell resistance to apoptosis under stress.
Conclusions:
- Hsp70 proteins play a significant role in maintaining cancer cell survival.
- Targeting Hsp70 may represent a therapeutic strategy for cancer treatment.
- Further research into Hsp70 isotypes in cancer is warranted.
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