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        <title>Frontiers in Cell Death | Apoptosis section | New and Recent Articles</title>
        <link>https://www.frontiersin.org/journals/cell-death/sections/apoptosis</link>
        <description>RSS Feed for Apoptosis section in the Frontiers in Cell Death journal | New and Recent Articles</description>
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        <pubDate>2026-05-14T08:04:49.374+00:00</pubDate>
        <ttl>60</ttl>
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        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/fceld.2026.1821035</guid>
        <link>https://www.frontiersin.org/articles/10.3389/fceld.2026.1821035</link>
        <title><![CDATA[Challenges in drug efficacy and toxicity screening with 3D bioprinted melanoma models]]></title>
        <pubdate>2026-05-08T00:00:00Z</pubdate>
        <category>Perspective</category>
        <author>Lissinda H. du Plessis</author><author>Nonzuzo Myeza</author><author>Chrisna Gouws</author><author>Awie F. Kotzé</author><author>Daniel Nieto</author>
        <description><![CDATA[Melanoma, an aggressive form of skin cancer, poses a significant public health challenge due to its metastatic potential, drug resistance and increasing prevalence. The development of three-dimensional (3D) bioprinted melanoma models has shown promise in providing a more cellular and biochemical relevant representation of the tumor microenvironment. Through 3D bioprinting, a bioink comprised of a mixture of living cells within biocompatible hydrogel biomaterials, can be bioprinted in defined patterns, layer-by-layer, using a pre-determined digital computer-aided design. These models facilitate more physiologically relevant investigation of tumor behavior, drug efficacy, and toxicity. However, there is a need to develop scalable and reproducible 3D bioprinted models for drug efficacy and toxicity screening. There is also a growing need to optimize analysis techniques for more complex 3D models, as most existing methods were primarily designed for two-dimensional (2D) cell culture models. Microscopy-, colorimetric- and fluorescence-based assays present some challenges in analyzing 3D models, including accurately capturing the heterogeneity of cell distribution and the presence of varying spheroid sizes. In addition, with 3D bioprinted constructs the physical properties of the 3D bioprinted biomaterial, such as its opaque nature and optical density, can interfere with imaging, leading to issues like optical light scattering, light absorption and reduced light penetration. This leads to inconsistent or inaccurate readings that fail to accurately reflect the biological processes within the 3D bioprinted model. This perspective will comment on challenges relating to drug efficacy and toxicity screening of 3D bioprinted melanoma models, focusing on the analysis of drug-induced apoptosis.]]></description>
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        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/fceld.2025.1658598</guid>
        <link>https://www.frontiersin.org/articles/10.3389/fceld.2025.1658598</link>
        <title><![CDATA[C/EBPβ deficiency enhances keratinocyte apoptosis after UVB-induced DNA damage via regulation of the type I IFN and TNF responses]]></title>
        <pubdate>2025-09-03T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Emma E. Tobin</author><author>Ayushma Sharma</author><author>Samantha T. Kros</author><author>Dereje D. Jima</author><author>Sophia C. Gray</author><author>Jonathan R. Hall</author>
        <description><![CDATA[The epidermis is routinely subjected to DNA damage induced by ultraviolet B (UVB) solar radiation. In addition to activating canonical DNA damage responses such as cycle cell checkpoints and DNA repair, UVB-induced DNA damage can also activate additional signaling pathways including inflammatory responses. The pathways activated downstream of UVB-induced DNA damage have a critical role in determining cellular survival to UVB radiation. Here we report that loss of CCAAT/enhancer binding protein β (C/EBPβ) in mouse keratinocytes results in enhanced UVB-induced apoptosis through activation of extrinsic apoptosis genes cleaved caspase-8 and truncated BH3 interacting-domain death agonist (tBid). RNAseq and Ingenuity Pathway Analysis of UVB-treated C/EBPβ−/− primary keratinocytes revealed an enrichment of inflammatory signaling pathways, including the type I interferon (IFN-I) pathway as the most enriched pathway. Numerous IFN-I stimulated genes were up-regulated in UVB-treated C/EBPβ−/− keratinocytes, including genes that regulate extrinsic apoptosis. Inhibition of the interferon-α/β receptor or the associated kinase Tyk2 greatly reduced cell death in UVB-exposed C/EBPβ deficient keratinocytes, demonstrating the dependence of IFN signaling in C/EBPβ regulated apoptosis. The apoptosis inducing cytokine tumor necrosis factor alpha (TNF-α) was identified as one of the most significant upstream regulators activated in UVB-exposed C/EBPβ−/− keratinocytes compared to UVB exposed wild type control. UVB-exposed C/EBPβ−/− keratinocytes displayed increased expression of TNF-α and the enhanced apoptosis in C/EBPβ−/− keratinocytes was suppressed by a TNF-α neutralizing antibody. Our results indicate that loss of C/EBPβ enhances activation of a non-canonical UVB DNA damage response pathway involving interferon and TNF signaling to induce keratinocyte cell death.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/fceld.2025.1592636</guid>
        <link>https://www.frontiersin.org/articles/10.3389/fceld.2025.1592636</link>
        <title><![CDATA[Corrigendum: Identification of miR-342-5p/MDM4/p53 network in acute myeloid leukemia]]></title>
        <pubdate>2025-04-25T00:00:00Z</pubdate>
        <category>Correction</category>
        <author>Sema Misir</author><author>Serap Ozer Yaman</author><author>Ceylan Hepokur</author><author>Osman Akidan</author><author>Yuksel Aliyazicioglu</author><author>Francisco J. Enguita</author><author>Mazhar Salim Al Zoubi</author>
        <description></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/fceld.2024.1471050</guid>
        <link>https://www.frontiersin.org/articles/10.3389/fceld.2024.1471050</link>
        <title><![CDATA[The histone demethylase Kdm5 controls Hid-induced cell death in Drosophila]]></title>
        <pubdate>2024-11-20T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Hans-Martin Herz</author><author>Andreas Bergmann</author>
        <description><![CDATA[We conducted an EMS mutagenesis screen on chromosome arm 2L to identify recessive suppressors of GMR-hid-induced apoptosis in the Drosophila eye. Through this screen, we recovered three alleles of the lysine demethylase gene Kdm5. Kdm5, a member of the JmjC-domain-containing protein family, possesses histone demethylase activity towards H3K4me3. Our data suggest that Kdm5 specifically regulates Hid-induced cell death during development, as we did not observe control of Reaper- or Grim-induced cell death by Kdm5. Interestingly, GMR-hid-induced apoptosis is suppressed independently of Kdm5’s demethylase activity. Our findings indicate that Rbf and dMyc are necessary for Kdm5 mosaics to suppress GMR-hid-induced cell death. Moreover, Kdm5 mosaics failed to suppress apoptosis induced by a mutant form of Hid that is resistant to inhibition by Erk-type MAPK activity. Additionally, Kdm5 dominantly enhances the wing phenotype of an activated MAPK mutant. These results collectively suggest that Kdm5 controls Hid-induced apoptosis by regulating the Rbf, dMyc, and MAPK pathways.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/fceld.2024.1503241</guid>
        <link>https://www.frontiersin.org/articles/10.3389/fceld.2024.1503241</link>
        <title><![CDATA[Identification of miR-342-5p/MDM4/p53 network in acute myeloid leukemia]]></title>
        <pubdate>2024-11-14T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Sema Misir</author><author>Serap Ozer Yaman</author><author>Ceylan Hepokur</author><author>Osman Akidan</author><author>Yuksel Aliyazicioglu</author><author>Francisco J. Enguita</author><author>Mazhar Salim Al Zoubi</author>
        <description><![CDATA[Acute myeloid leukemia (AML) is one of the most prevalent hematological malignancies. miRNAs play roles in cancer initiation and progression in various cancer types by post-transcriptional regulation of gene expression. The aim of this study is to investigate the mechanisms in the development and progression of acute myeloid leukemia and to identify potential target genes and miRNAs by bioinformatic analysis. miRNA expression profiles were obtained from the GSE51908 dataset on the Gene Expression Omnibus (GEO). GEO2R was used to identify differentially expressed miRNAs. The diagnostic and overall survival effects of the identified miRNA were determined using ROC analysis and Kaplan-Meier curve, respectively. Putative miRNA targets were determined based on miRWalk and miRDB tools. The expression change and overall survival analysis of the identified target gene were analyzed by Gene Expression Profiling Interactive Analysis (GEPIA). Protein-protein interaction (PPI) networks of the target gene were determined using STRING and GeneMANIA. Functional enrichment analysis was performed using the DAVID program. 24 DE-miRNAs were identified, including 16 upregulated and 8 downregulated genes. miR-342-5p expression had significantly shorter survival than those in higher expression control group (p = 0.0001), and its AUC value to discriminate AML from control groups was 0.795. High expression of MDM4 predicts an unfavorable prognosis in AML patients. The MDM4 gene was determined to be associated with decreased survival rates. According to KEGG results, microRNAs, p53 signaling pathway, and cell cycle are associated with AML development. The current study based on the GEO database, miR-342-5p/MDM4/p53 axis AML may provide new therapeutic targets.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/fceld.2023.1281137</guid>
        <link>https://www.frontiersin.org/articles/10.3389/fceld.2023.1281137</link>
        <title><![CDATA[Molecular and temporal control of restimulation-induced cell death (RICD) in T lymphocytes]]></title>
        <pubdate>2023-10-30T00:00:00Z</pubdate>
        <category>Review</category>
        <author>Katherine P. Lee</author><author>Benjamin Epstein</author><author>Camille M. Lake</author><author>Andrew L. Snow</author>
        <description><![CDATA[For effective adaptive immunity, T lymphocytes must rapidly expand and contract in an antigen-specific manner to effectively control invading pathogens and preserve immunological memory, without sustaining excessive collateral damage to host tissues. Starting from initial antigen encounter, carefully calibrated programmed cell death pathways are critical for maintaining homeostasis over distinct phases of the T cell response. Restimulation-induced cell death (RICD), a self-regulatory apoptosis pathway triggered by re-engagement of the T cell receptor (TCR), is particularly important for constraining effector T cell expansion to preclude overt immunopathology; indeed, genetic disorders affecting key molecules involved in RICD execution can manifest in excessive lymphoproliferation, malignancy, and autoimmunity. Herein we review our current knowledge of how RICD sensitivity is ultimately regulated over the course of an immune response, including recent revelations on molecules that tune RICD by enforcing resistance or promoting susceptibility in expanding versus mature effector T cells, respectively. Detailed dissection of the molecular and temporal control of RICD also illuminates novel therapeutic strategies for correcting abnormal T cell responses noted in various immune disorders by ultimately tuning RICD sensitivity.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/fceld.2023.1223926</guid>
        <link>https://www.frontiersin.org/articles/10.3389/fceld.2023.1223926</link>
        <title><![CDATA[Regulators mount up: the metabolic roles of apoptotic proteins]]></title>
        <pubdate>2023-07-03T00:00:00Z</pubdate>
        <category>Mini Review</category>
        <author>James H. Schofield</author><author>Zachary T. Schafer</author>
        <description><![CDATA[The induction of apoptosis, a programmed cell death pathway governed by activation of caspases, can result in fundamental changes in metabolism that either facilitate or restrict the execution of cell death. In addition, metabolic adaptations can significantly impact whether cells in fact initiate the apoptotic cascade. In this mini-review, we will highlight and discuss the interconnectedness of apoptotic regulation and metabolic alterations, two biological outcomes whose regulators are intertwined.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/fceld.2023.1169966</guid>
        <link>https://www.frontiersin.org/articles/10.3389/fceld.2023.1169966</link>
        <title><![CDATA[Multifaceted promotion of apoptosis by acetylcholinesterase]]></title>
        <pubdate>2023-04-17T00:00:00Z</pubdate>
        <category>Review</category>
        <author>Debbra Y. Knorr</author><author>Defne Demirbas</author><author>Ralf Heinrich</author>
        <description><![CDATA[Elevated expression of acetylcholinesterase (AChE) is a common characteristic of apoptotic cells in both invertebrate and vertebrate species. While increased levels of acetylcholinesterase sensitize cells to apoptogenic stimuli, its absence or pharmacological inactivation interferes with apoptotic cell death. acetylcholinesterase may exert its pro-apoptotic function directly as an integral component of the apoptotic molecular machinery or indirectly by limiting the availability of receptor ligands and structural binding partners that promote cell survival under non-apoptogenic conditions. acetylcholinesterase promotes formation of the apoptosome and degrades DNA after nuclear accumulation. Its esterase activity limits the availability of acetylcholine as ligand for cell membrane-located nicotinic and muscarinic ACh-receptors and mitochondrial nicotinic ACh-receptors that normally support vital physiological states. Studies on insects suggest, that cytokine-activated cell-protective pathways may suppress acetylcholinesterase overexpression under apoptogenic conditions to prevent apoptotic cell death. We provide an overview of studies on various organisms and cell types that summarizes the contribution of acetylcholinesterase to the progress of apoptosis via multiple mechanisms.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/fceld.2023.1147605</guid>
        <link>https://www.frontiersin.org/articles/10.3389/fceld.2023.1147605</link>
        <title><![CDATA[Biophysics at the edge of life and death: Radical control of apoptotic mechanisms]]></title>
        <pubdate>2023-02-27T00:00:00Z</pubdate>
        <category>Mini Review</category>
        <author>Samantha J. Hack</author><author>Wendy S. Beane</author><author>Kelly Ai-Sun Tseng</author>
        <description><![CDATA[Recent studies have furthered our understanding of how dying and living cells interact in different physiological contexts, however the signaling that initiates and mediates apoptosis and apoptosis-induced proliferation are more complex than previously thought. One increasingly important area of study is the biophysical control of apoptosis. In addition to biochemical regulation, biophysical signals (including redox chemistry, bioelectric gradients, acoustic and magnetic stimuli) are also known yet understudied regulators of both cell death and apoptosis-induced proliferation. Mounting evidence suggests biophysical signals may be key targets for therapeutic interventions. This review highlights what is known about the role of biophysical signals in controlling cell death mechanisms during development, regeneration, and carcinogenesis. Since biophysical signals can be controlled spatiotemporally, bypassing the need for genetic manipulation, further investigation may lead to fine-tuned modulation of apoptotic pathways to direct desired therapeutic outcomes.]]></description>
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