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Biomolecules
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Recent Advances in Histone Deacetylase Research in Health and Disease
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Recent Advances in Histone Deacetylase Research in Health and Disease

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Enzymology".

Deadline for manuscript submissions: closed (30 April 2024) | Viewed by 3031

Special Issue Editors

Prof. Dr. Neal Weintraub

E-Mail Website
Guest Editor
Medical College of Georgia, Augusta University, Augusta, GA, USA
Interests: cardiovascular disease; metabolic disease; cardio-oncology; epigenetics; inflammation; oxidative stress; vascular biology; lipid metabolism
Special Issues, Collections and Topics in MDPI journals
Dr. Ha Won Kim

E-Mail Website
Guest Editor
Medical College of Georgia, Augusta University, Augusta, GA, USA
Interests: vascular biology; adipose biology; abdominal aortic aneurysm; atherosclerosis; perivascular adipose tissue; metabolic disease; inflammation; redox signaling

Special Issue Information

Dear Colleagues,

Histone deacetylases (HDACs) play a fundamental role in regulating gene expression, but their abnormal expression and activity contributes to the pathogenesis of various diseases, such as cancer, cardiopulmonary disease, obesity and neurodegenerative disease. HDACs are classified into four groups with a diverse range of structures, enzymatic activities, subcellular localization processes and non-canonical functions. Thus, elucidating the distinct mechanisms whereby HDACs function in different tissues/cell types, under normal conditions and in disease states, is required to develop successful therapeutic strategies. This Special Issue aims to explore the current understanding of the role and mechanisms of HDACs in disease through research from basic, preclinical and clinical studies. We welcome both original research articles and up-to-date reviews that address topics of interest to researchers studying the pathophysiology of HDACs.

Prof. Dr. Neal Weintraub
Dr. Ha Won Kim
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • histone deacetylase
  • HDAC inhibitor
  • deacetylation
  • enzymatic and non-enzymatic activity
  • epigenetics
  • human disease

Published Papers (3 papers)

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Research

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11 pages, 4030 KiB  
Article
Transgenic Overexpression of HDAC9 Promotes Adipocyte Hypertrophy, Insulin Resistance and Hepatic Steatosis in Aging Mice
by Praneet Veerapaneni, Brandee Goo, Samah Ahmadieh, Hong Shi, David S. Kim, Mourad Ogbi, Stephen Cave, Ronnie Chouhaita, Nicole Cyriac, David J. Fulton, Alexander D. Verin, Weiqin Chen, Yun Lei, Xin-Yun Lu, Ha Won Kim and Neal L. Weintraub
Biomolecules 2024, 14(4), 494; https://doi.org/10.3390/biom14040494 - 18 Apr 2024
Viewed by 483
Abstract
Histone deacetylase (HDAC) 9 is a negative regulator of adipogenic differentiation, which is required for maintenance of healthy adipose tissues. We reported that HDAC9 expression is upregulated in adipose tissues during obesity, in conjunction with impaired adipogenic differentiation, adipocyte hypertrophy, insulin resistance, and [...] Read more.
Histone deacetylase (HDAC) 9 is a negative regulator of adipogenic differentiation, which is required for maintenance of healthy adipose tissues. We reported that HDAC9 expression is upregulated in adipose tissues during obesity, in conjunction with impaired adipogenic differentiation, adipocyte hypertrophy, insulin resistance, and hepatic steatosis, all of which were alleviated by global genetic deletion of Hdac9. Here, we developed a novel transgenic (TG) mouse model to test whether overexpression of Hdac9 is sufficient to induce adipocyte hypertrophy, insulin resistance, and hepatic steatosis in the absence of obesity. HDAC9 TG mice gained less body weight than wild-type (WT) mice when fed a standard laboratory diet for up to 40 weeks, which was attributed to reduced fat mass (primarily inguinal adipose tissue). There was no difference in insulin sensitivity or glucose tolerance in 18-week-old WT and HDAC9 TG mice; however, at 40 weeks of age, HDAC9 TG mice exhibited impaired insulin sensitivity and glucose intolerance. Tissue histology demonstrated adipocyte hypertrophy, along with reduced numbers of mature adipocytes and stromovascular cells, in the HDAC9 TG mouse adipose tissue. Moreover, increased lipids were detected in the livers of aging HDAC9 TG mice, as evaluated by oil red O staining. In conclusion, the experimental aging HDAC9 TG mice developed adipocyte hypertrophy, insulin resistance, and hepatic steatosis, independent of obesity. This novel mouse model may be useful in the investigation of the impact of Hdac9 overexpression associated with metabolic and aging-related diseases. Full article
(This article belongs to the Special Issue Recent Advances in Histone Deacetylase Research in Health and Disease)
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16 pages, 1680 KiB  
Article
Biological Effects of HDAC Inhibitors Vary with Zinc Binding Group: Differential Effects on Zinc Bioavailability, ROS Production, and R175H p53 Mutant Protein Reactivation
by Brianna M. Flores, Chandana K. Uppalapati, Agnes S. Pascual, Alan Vong, Margaux A. Baatz, Alisha M. Harrison, Kathryn J. Leyva and Elizabeth E. Hull
Biomolecules 2023, 13(11), 1588; https://doi.org/10.3390/biom13111588 - 28 Oct 2023
Viewed by 1027
Abstract
The coordination of zinc by histone deacetylase inhibitors (HDACi), altering the bioavailability of zinc to histone deacetylases (HDACs), is key to HDAC enzyme inhibition. However, the ability of zinc binding groups (ZBGs) to alter intracellular free Zn+2 levels, which may have far-reaching [...] Read more.
The coordination of zinc by histone deacetylase inhibitors (HDACi), altering the bioavailability of zinc to histone deacetylases (HDACs), is key to HDAC enzyme inhibition. However, the ability of zinc binding groups (ZBGs) to alter intracellular free Zn+2 levels, which may have far-reaching effects, has not been explored. Using two HDACis with different ZBGs, we documented shifts in intracellular free Zn+2 concentrations that correlate with subsequent ROS production. Next, we assayed refolding and reactivation of the R175H mutant p53 protein in vitro to provide greater biological context as the activity of this mutant depends on cellular zinc concentration. The data presented demonstrates the differential activity of HDACi in promoting R175H response element (RE) binding. After cells are treated with HDACi, there are differences in R175H mutant p53 refolding and reactivation, which may be related to treatments. Collectively, we show that HDACis with distinct ZBGs differentially impact the intracellular free Zn+2 concentration, ROS levels, and activity of R175H; therefore, HDACis may have significant activity independent of their ability to alter acetylation levels. Our results suggest a framework for reevaluating the role of zinc in the variable or off-target effects of HDACi, suggesting that the ZBGs of HDAC inhibitors may provide bioavailable zinc without the toxicity associated with zinc metallochaperones such as ZMC1. Full article
(This article belongs to the Special Issue Recent Advances in Histone Deacetylase Research in Health and Disease)
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Review

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26 pages, 2378 KiB  
Review
Zinc-Dependent Histone Deacetylases in Lung Endothelial Pathobiology
by Rahul S. Patil, McKenzie E. Maloney, Rudolf Lucas, David J. R. Fulton, Vijay Patel, Zsolt Bagi, Anita Kovacs-Kasa, Laszlo Kovacs, Yunchao Su and Alexander D. Verin
Biomolecules 2024, 14(2), 140; https://doi.org/10.3390/biom14020140 - 23 Jan 2024
Cited by 2 | Viewed by 1102
Abstract
A monolayer of endothelial cells (ECs) lines the lumen of blood vessels and, as such, provides a semi-selective barrier between the blood and the interstitial space. Compromise of the lung EC barrier due to inflammatory or toxic events may result in pulmonary edema, [...] Read more.
A monolayer of endothelial cells (ECs) lines the lumen of blood vessels and, as such, provides a semi-selective barrier between the blood and the interstitial space. Compromise of the lung EC barrier due to inflammatory or toxic events may result in pulmonary edema, which is a cardinal feature of acute lung injury (ALI) and its more severe form, acute respiratory distress syndrome (ARDS). The EC functions are controlled, at least in part, via epigenetic mechanisms mediated by histone deacetylases (HDACs). Zinc-dependent HDACs represent the largest group of HDACs and are activated by Zn2+. Members of this HDAC group are involved in epigenetic regulation primarily by modifying the structure of chromatin upon removal of acetyl groups from histones. In addition, they can deacetylate many non-histone histone proteins, including those located in extranuclear compartments. Recently, the therapeutic potential of inhibiting zinc-dependent HDACs for EC barrier preservation has gained momentum. However, the role of specific HDAC subtypes in EC barrier regulation remains largely unknown. This review aims to provide an update on the role of zinc-dependent HDACs in endothelial dysfunction and its related diseases. We will broadly focus on biological contributions, signaling pathways and transcriptional roles of HDACs in endothelial pathobiology associated mainly with lung diseases, and we will discuss the potential of their inhibitors for lung injury prevention. Full article
(This article belongs to the Special Issue Recent Advances in Histone Deacetylase Research in Health and Disease)
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