Literature DB >> 36036883

HDAC6: A unique HDAC family member as a cancer target.

Sumeet Kaur1, Prerna Rajoria1, Madhu Chopra2.   

Abstract

BACKGROUND: HDAC6, a structurally and functionally distinct member of the HDAC family, is an integral part of multiple cellular functions such as cell proliferation, apoptosis, senescence, DNA damage and genomic stability, all of which when deregulated contribute to carcinogenesis. Among several HDAC family members known so far, HDAC6 holds a unique position. It differs from the other HDAC family members not only in terms of its subcellular localization, but also in terms of its substrate repertoire and hence cellular functions. Recent findings have considerably expanded the research related to the substrate pool, biological functions and regulation of HDAC6. Studies in HDAC6 knockout mice highlighted the importance of HDAC6 as a cell survival player in stressful situations, making it an important anticancer target. There is ample evidence stressing the importance of HDAC6 as an anti-cancer synergistic partner of many chemotherapeutic drugs. HDAC6 inhibitors have been found to enhance the effectiveness of conventional chemotherapeutic drugs such as DNA damaging agents, proteasome inhibitors and microtubule inhibitors, thereby highlighting the importance of combination therapies involving HDAC6 inhibitors and other anti-cancer agents.
CONCLUSIONS: Here, we present a review on HDAC6 with emphasis on its role as a critical regulator of specific physiological cellular pathways which when deregulated contribute to tumorigenesis, thereby highlighting the importance of HDAC6 inhibitors as important anticancer agents alone and in combination with other chemotherapeutic drugs. We also discuss the synergistic anticancer effect of combination therapies of HDAC6 inhibitors with conventional chemotherapeutic drugs.
© 2022. Springer Nature Switzerland AG.

Entities:  

Keywords:  Cancer; Combination therapy; HDAC6; Signaling pathways; Tumorigenesis

Mesh:

Substances:

Year:  2022        PMID: 36036883     DOI: 10.1007/s13402-022-00704-6

Source DB:  PubMed          Journal:  Cell Oncol (Dordr)        ISSN: 2211-3428            Impact factor:   7.051


  215 in total

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Review 2.  Acetylation of non-histone proteins modulates cellular signalling at multiple levels.

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Review 3.  Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug.

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Journal:  Nat Biotechnol       Date:  2007-01       Impact factor: 54.908

Review 4.  The world of protein acetylation.

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Journal:  Biochim Biophys Acta       Date:  2016-06-11

Review 5.  Histone deacetylases (HDACs): characterization of the classical HDAC family.

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Journal:  Biochem J       Date:  2003-03-15       Impact factor: 3.857

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Authors:  Elise A Olsen; Youn H Kim; Timothy M Kuzel; Theresa R Pacheco; Francine M Foss; Sareeta Parker; Stanley R Frankel; Cong Chen; Justin L Ricker; Jean Marie Arduino; Madeleine Duvic
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8.  Lysine acetylation targets protein complexes and co-regulates major cellular functions.

Authors:  Chunaram Choudhary; Chanchal Kumar; Florian Gnad; Michael L Nielsen; Michael Rehman; Tobias C Walther; Jesper V Olsen; Matthias Mann
Journal:  Science       Date:  2009-07-16       Impact factor: 47.728

9.  Phase II multi-institutional trial of the histone deacetylase inhibitor romidepsin as monotherapy for patients with cutaneous T-cell lymphoma.

Authors:  Richard L Piekarz; Robin Frye; Maria Turner; John J Wright; Steven L Allen; Mark H Kirschbaum; Jasmine Zain; H Miles Prince; John P Leonard; Larisa J Geskin; Craig Reeder; David Joske; William D Figg; Erin R Gardner; Seth M Steinberg; Elaine S Jaffe; Maryalice Stetler-Stevenson; Stephen Lade; A Tito Fojo; Susan E Bates
Journal:  J Clin Oncol       Date:  2009-10-13       Impact factor: 44.544

Review 10.  Protein post-translational modifications and regulation of pluripotency in human stem cells.

Authors:  Yu-Chieh Wang; Suzanne E Peterson; Jeanne F Loring
Journal:  Cell Res       Date:  2013-11-12       Impact factor: 25.617

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