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      Histone H4 is cleaved by granzyme A during staurosporine-induced cell death in B-lymphoid Raji cells

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          Abstract

          Granzyme A (GzmA) was first identified as a cytotoxic T lymphocyte protease protein with limited tissue expression. A number of cellular proteins are known to be cleaved by GzmA, and its function is to induce apoptosis. Histones H1, H2B, and H3 were identified as GzmA substrates during apoptotic cell death. Here, we demonstrated that histone H4 was cleaved by GzmA during staurosporine-induced cell death; however, in the presence of caspase inhibitors, staurosporine-treated Raji cells underwent necroptosis instead of apoptosis. Furthermore, histone H4 cleavage was blocked by the GzmA inhibitor nafamostat mesylate and by GzmA knockdown using siRNA. These results suggest that histone H4 is a novel substrate for GzmA in staurosporine-induced cells. [BMB Reports 2016; 49(10): 560-565]

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          A chromatin landmark and transcription initiation at most promoters in human cells.

          Matthew Guenther, Stuart S. Levine, Laurie A. Boyer … (2007)
          We describe the results of a genome-wide analysis of human cells that suggests that most protein-coding genes, including most genes thought to be transcriptionally inactive, experience transcription initiation. We found that nucleosomes with H3K4me3 and H3K9,14Ac modifications, together with RNA polymerase II, occupy the promoters of most protein-coding genes in human embryonic stem cells. Only a subset of these genes produce detectable full-length transcripts and are occupied by nucleosomes with H3K36me3 modifications, a hallmark of elongation. The other genes experience transcription initiation but show no evidence of elongation, suggesting that they are predominantly regulated at postinitiation steps. Genes encoding most developmental regulators fall into this group. Our results also identify a class of genes that are excluded from experiencing transcription initiation, at which mechanisms that prevent initiation must predominate. These observations extend to differentiated cells, suggesting that transcription initiation at most genes is a general phenomenon in human cells.
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            Endonuclease G is an apoptotic DNase when released from mitochondria.

            L Li, X. Luo, X. Wang (2001)
            Nucleosomal fragmentation of DNA is a hallmark of apoptosis (programmed cell death), and results from the activation of nucleases in cells undergoing apoptosis. One such nuclease, DNA fragmentation factor (DFF, a caspase-activated deoxyribonuclease (CAD) and its inhibitor (ICAD)), is capable of inducing DNA fragmentation and chromatin condensation after cleavage by caspase-3 (refs 2,3,4). However, although transgenic mice lacking DFF45 or its caspase cleavage site have significantly reduced DNA fragmentation, these mice still show residual DNA fragmentation and are phenotypically normal. Here we report the identification and characterization of another nuclease that is specifically activated by apoptotic stimuli and is able to induce nucleosomal fragmentation of DNA in fibroblast cells from embryonic mice lacking DFF. This nuclease is endonuclease G (endoG), a mitochondrion-specific nuclease that translocates to the nucleus during apoptosis. Once released from mitochondria, endoG cleaves chromatin DNA into nucleosomal fragments independently of caspases. Therefore, endoG represents a caspase-independent apoptotic pathway initiated from the mitochondria.
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              Death by a thousand cuts: granzyme pathways of programmed cell death.

              Dipanjan Chowdhury, Judy Lieberman (2008)
              The granzymes are cell death-inducing enzymes, stored in the cytotoxic granules of cytotoxic T lymphocytes and natural killer cells, that are released during granule exocytosis when a specific virus-infected or transformed target cell is marked for elimination. Recent work suggests that this homologous family of serine esterases can activate at least three distinct pathways of cell death. This redundancy likely evolved to provide protection against pathogens and tumors with diverse strategies for evading cell death. This review discusses what is known about granzyme-mediated pathways of cell death as well as recent studies that implicate granzymes in immune regulation and extracellular proteolytic functions in inflammation.
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                Author and article information

                Journal
                Journal ID (nlm-ta): BMB Rep
                Journal ID (iso-abbrev): BMB Rep
                Journal ID (publisher-id): ksbmb
                Title: BMB Reports
                Publisher: Korean Society for Biochemistry and Molecular Biology
                ISSN (Print): 1976-6696
                ISSN (Electronic): 1976-670X
                Publication date (Print): 31 October 2016
                Volume: 49
                Issue: 10
                Pages: 560-565
                Affiliations
                [1 ]Disease Target Structure Research Center
                [2 ]Metabolic Regulation Research Center
                [5 ]Personalized Genomic Medicine Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon 34141
                [3 ]College of Pharmacy, Chung-Ang University, Seoul 06974
                [4 ]Division of Life Sciences, Korea University, Seoul 02841, Korea
                Author notes
                [* ]Sung Goo Park, Tel: +82-42-860-4262; Fax: +82-42-860-4269; E-mail: sgpark@ 123456kribb.re.kr , Jeong-Hoon Kim, Tel: +82-42-860-4264; Fax: +82-42-860-4269; E-mail: jhoonkim@ 123456kribb.re.kr
                Article
                Publisher ID: BMB-49-560
                DOI: 10.5483/BMBRep.2016.49.10.105
                PMC ID: 5227298
                PubMed ID: 27439606
                SO-VID: 758b45b0-a682-41b9-a86a-82894e43d2b1
                Copyright © Copyright © 2016, Korean Society for Biochemistry and Molecular Biology
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( http://creativecommons.org/licenses/by-nc/4.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 27 June 2016
                Date revision received : 14 July 2016
                Date accepted : 20 July 2016
                Categories
                Subject: Research Article

                Keywords: caspase-independent cell death,granzyme a,histone h4,raji cell
                Data availability:
                Keywords: caspase-independent cell death, granzyme a, histone h4, raji cell

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