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      Histone Modifications in Acute Kidney Injury

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          Abstract

          Background

          Acute kidney injury (AKI) is a serious clinical problem associated with high morbidity and mortality worldwide. The pathophysiology and pathogenesis of AKI is complex and multifactorial. In recent years, epigenetics has emerged as an important regulatory mechanism in AKI.

          Summary

          There are several types of histone modification, including methylation, acetylation, phosphorylation, crotonylation, citrullination, and sumoylation. Histone modifications are associated with the transcription of many genes and activation of multiple signaling pathways that contribute to the pathogenesis of AKI. Thus, targeting histone modification may offer novel strategies to protect kidneys from AKI and enhance kidney repair and recovery. In this review, we summarize recent advances on the modification, regulation, and implication of histone modifications in AKI.

          Key Messages

          Histone modifications contribute to the pathogenesis of AKI. Understanding of epigenetic regulation in AKI will aid in establishing the utility of pharmacologic targeting of histone modification as a potential novel therapy for AKI.

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          Most cited references162

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          Histone H4-K16 acetylation controls chromatin structure and protein interactions.

          Michael A. Shogren-Knaak, Haruhiko Ishii, Jian-Min Sun … (2006)
          Acetylation of histone H4 on lysine 16 (H4-K16Ac) is a prevalent and reversible posttranslational chromatin modification in eukaryotes. To characterize the structural and functional role of this mark, we used a native chemical ligation strategy to generate histone H4 that was homogeneously acetylated at K16. The incorporation of this modified histone into nucleosomal arrays inhibits the formation of compact 30-nanometer-like fibers and impedes the ability of chromatin to form cross-fiber interactions. H4-K16Ac also inhibits the ability of the adenosine triphosphate-utilizing chromatin assembly and remodeling enzyme ACF to mobilize a mononucleosome, indicating that this single histone modification modulates both higher order chromatin structure and functional interactions between a nonhistone protein and the chromatin fiber.
          Article 0 comments Cited 485 times – based on 0 reviews     Review now
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            Histone core modifications regulating nucleosome structure and dynamics.

            Peter Tessarz, Tony Kouzarides (2014)
            Post-translational modifications of histones regulate all DNA-templated processes, including replication, transcription and repair. These modifications function as platforms for the recruitment of specific effector proteins, such as transcriptional regulators or chromatin remodellers. Recent data suggest that histone modifications also have a direct effect on nucleosomal architecture. Acetylation, methylation, phosphorylation and citrullination of the histone core may influence chromatin structure by affecting histone-histone and histone-DNA interactions, as well as the binding of histones to chaperones.
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              Histone methylation: a dynamic mark in health, disease and inheritance.

              Eric Greer, Yang Shi (2012)
              Organisms require an appropriate balance of stability and reversibility in gene expression programmes to maintain cell identity or to enable responses to stimuli; epigenetic regulation is integral to this dynamic control. Post-translational modification of histones by methylation is an important and widespread type of chromatin modification that is known to influence biological processes in the context of development and cellular responses. To evaluate how histone methylation contributes to stable or reversible control, we provide a broad overview of how histone methylation is regulated and leads to biological outcomes. The importance of appropriately maintaining or reprogramming histone methylation is illustrated by its links to disease and ageing and possibly to transmission of traits across generations.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Kidney Dis (Basel)
                Journal ID (iso-abbrev): Kidney Dis (Basel)
                Journal ID (publisher-id): KDD
                Title: Kidney Diseases
                Publisher: S. Karger AG (Allschwilerstrasse 10, P.O. Box · Postfach · Case postale, CH–4009, Basel, Switzerland · Schweiz · Suisse, Phone: +41 61 306 11 11, Fax: +41 61 306 12 34, karger@karger.com )
                ISSN (Print): 2296-9381
                ISSN (Electronic): 2296-9357
                Publication date Collection: December 2022
                Publication date (Electronic): 10 November 2022
                Publication date PMC-release: 10 November 2022
                Volume: 8
                Issue: 6
                Pages: 466-477
                Affiliations
                [1] aDepartment of Nephrology, Shanghai East Hospital, Tongji University School of Medicine, Shanghai, China
                [2] bDepartment of Medicine, Rhode Island Hospital and Alpert Medical School, Brown University, Providence, Rhode Island, USA
                Author notes
                Article
                Publisher ID: kdd-0008-0466
                DOI: 10.1159/000527799
                PMC ID: 9798838
                PubMed ID: 36590679
                SO-VID: eaacd450-5c48-4667-a97a-e5947f9518fd
                Copyright © Copyright © 2022 by The Author(s). Published by S. Karger AG, Basel
                License:

                This article is licensed under the Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC). Usage and distribution for commercial purposes requires written permission.

                History
                Date received : 10 August 2022
                Date accepted : 24 October 2022
                Date: 2022
                Page count
                Figures: 1, Tables: 1, References: 86, Pages: 12
                Funding
                This work was supported by the National Natural Science Foundation of China (81830021 and 82070700 to S.Z.).
                Categories
                Subject: Review Article

                Keywords: acute kidney injury,histone modifications,acetylation,methylation,phosphorylation,crotonylation,citrullination,sumoylation
                Data availability:
                Keywords: acute kidney injury, histone modifications, acetylation, methylation, phosphorylation, crotonylation, citrullination, sumoylation

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