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Human DNAJ in cancer and stem cells
Jason N Sterrenberg1, Gregory L Blatch, Adrienne L Edkins
1Biomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry, Microbiology and Biotechnology, Rhodes University, Grahamstown South Africa.
Heat shock protein 40kDa (HSP40/DNAJ) co-chaperones are crucial regulators in cancer and stem cells. Their diverse roles suggest potential as selective drug targets for anti-cancer treatments.
Area of Science:
- Molecular Biology
- Oncology
- Cell Biology
Background:
- Heat shock protein 40kDa (HSP40/DNAJ) co-chaperones are the largest HSP subgroup.
- DNAJ proteins regulate HSP70 and HSP90 chaperone functions.
- DNAJ also possess chaperone-independent biological roles.
Purpose of the Study:
- To review the literature on DNAJ function and expression in cancer, stem cells, and cancer stem cells.
- To propose DNAJ as key regulators in these cellular contexts.
- To explore DNAJ as potential drug targets for cancer therapy.
Main Methods:
- Literature review of current research.
- Analysis of gene expression and proteomics data.
- Integration of findings from various biological systems.
Main Results:
- DNAJ proteins are differentially expressed in human tissues.
- DNAJ can promote or suppress cancer by chaperoning tumor suppressors or oncoproteins.
- DNAJ are implicated as key regulators of cancer, stem cell, and cancer stem cell functions.
Conclusions:
- The diversity of DNAJ suggests specific members may be targeted for anti-cancer drug development.
- Selected DNAJ with established links to malignancy and limited redundancy are attractive therapeutic targets.
- Targeting DNAJ offers potential for specific and selective anti-cancer treatments.
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