Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2023 Feb 3;15(3):984.
doi: 10.3390/cancers15030984.

Heat-Shock Proteins in Leukemia and Lymphoma: Multitargets for Innovative Therapeutic Approaches

Vincent Cabaud-Gibouin  1 , Manon Durand  1 , Ronan Quéré  1 , François Girodon  1   2 , Carmen Garrido  1   3 , Gaëtan Jego  1
Affiliations
Review

Heat-Shock Proteins in Leukemia and Lymphoma: Multitargets for Innovative Therapeutic Approaches

Vincent Cabaud-Gibouin et al. Cancers (Basel). .

Abstract

Heat-shock proteins (HSPs) are powerful chaperones that provide support for cellular functions under stress conditions but also for the homeostasis of basic cellular machinery. All cancer cells strongly rely on HSPs, as they must continuously adapt to internal but also microenvironmental stresses to survive. In solid tumors, HSPs have been described as helping to correct the folding of misfolded proteins, sustain oncogenic pathways, and prevent apoptosis. Leukemias and lymphomas also overexpress HSPs, which are frequently associated with resistance to therapy. HSPs have therefore been proposed as new therapeutic targets. Given the specific biology of hematological malignancies, it is essential to revise their role in this field, providing a more adaptable and comprehensive picture that would help design future clinical trials. To that end, this review will describe the different pathways and functions regulated by HSP27, HSP70, HSP90, and, not least, HSP110 in leukemias and lymphomas.

Keywords: heat-shock protein; leukemia; lymphoma; targeted therapy.

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
HSP are chaperones of cell signaling components in the BCR/TCR, JAK/STAT and PI3K/AKT pathways. Schematic of a leukemia/lymphoma cell showing the main actors involved in the major signaling pathways BCR/TCR, JAK/STAT and PI3K/AKT, as well as the involvement of the major heat shock protein families. CLL: chronic lymphocytic leukemia, MCL: mantle cell lymphoma, ABC-DLBCL: active B-cell diffuse large lymphoma, ALL: acute lymphoblastic leukemia, AML: acute myeloid leukemia, BL: Burkitt lymphoma, APL: acute promyelocytic leukemia, cHL: classical Hodgkin lymphoma, CML: chronic myeloid leukemia, MM: multiple myeloma MPN: myeloproliferative neoplasms.
Figure 2
Figure 2
HSP are chaperones of oncogenes, epigenetic regulators, metabolism regulators, chaperones of DNA repair, and sequesters of apoptotic actors in leukemia and lymphoma. Schematic of a leukemia/lymphoma cell showing the four major roles of HSPs in the global cellular homeostasis, which are: chaperones of oncogenes, chaperones of epigenetic regulators, chaperones of DNA repair actors, and their involvement in metabolism. SSB: single-strand break, DSB: double-strand break, DNPB: de novo purine biosynthetic pathway, HR: homologous recombination.
See this image and copyright information in PMC

References

    1. De Moraes Hungria V.T., Chiattone C., Pavlovsky M., Abenoza L.M., Agreda G.P., Armenta J., Arrais C., Flores O.A., Barroso F., Basquiera A.L., et al. Epidemiology of hematologic malignancies in real-world settings: Findings from the hemato-oncology Latin america observational registry study. J. Glob. Oncol. 2019;2019:1–19. doi: 10.1200/JGO.19.00025. - DOI - PMC - PubMed
    1. Bhullar K.S., Lagarón N.O., McGowan E.M., Parmar I., Jha A., Hubbard B.P., Rupasinghe H.P.V. Kinase-targeted cancer therapies: Progress, challenges and future directions. Mol. Cancer. 2018;17:48. doi: 10.1186/s12943-018-0804-2. - DOI - PMC - PubMed
    1. Carneiro B.A., El-Deiry W.S. Targeting apoptosis in cancer therapy. Nat. Rev. Clin. Oncol. 2020;17:395–417. doi: 10.1038/s41571-020-0341-y. - DOI - PMC - PubMed
    1. Jiang P., Sinha S., Aldape K., Hannenhalli S., Sahinalp C., Ruppin E. Big data in basic and translational cancer research. Nat. Rev. Cancer. 2022;22:625–639. doi: 10.1038/s41568-022-00502-0. - DOI - PMC - PubMed
    1. Thomas X., Campos L., Mounier C., Cornillon J., Flandrin P., Le Q.H., Piselli S., Guyotat D. Expression of heat-shock proteins is associated with major adverse prognostic factors in acute myeloid leukemia. Leuk. Res. 2005;29:1049–1058. doi: 10.1016/j.leukres.2005.02.010. - DOI - PubMed