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Keywords {🔍}

cmyc, cells, cell, article, myeloma, compound, fig, rpmi, google, scholar, assay, expression, protein, cas, analysis, treated, inhibitor, btz, apoptosis, cmycmax, dna, additional, group, molecular, treatment, file, stability, western, ncih, multiple, blot, damage, cdk, binding, dose, gene, drug, max, studies, showed, transcriptional, tumor, phosphorylation, target, china, control, figure, screening, results, degradation,

Topics {✒️}

2 μg p3flag-cmv-9-c-myc plasmids annexin v-apc/7-aad assay p3flag-cmv-9-myc plasmid pan-caspase inhibitor z-vad-fmk block c-myc/max heterodimerization targeting c-myc/max interaction blocking c-myc/max heterodimerization flag-tagged c-myc plasmids c-myc/max heterodimers bound c-myc response elements c-myc/max heterodimer significantly c-myc/max interaction domain c-myc unstable domain destroy c-myc/max interaction c-myc/max complex binding c-myc/max mutants obtained f-box protein fbw7 c-myc inhibitory activity proteasome-mediated protein degradation c-myc protein half-life c-myc/max complex interface dna double-strand breaks potential c-myc inhibitor c-myc transcriptional target disturb c-myc stability c-myc-mediated oncogenesis purchased commercial gst-c-myc c-myc thr58 promoted exogenous flag-c-myc c-myc inhibitor d347-2761 c-myc protein stability c-myc/max heterodimerization c-myc gene rearrangement c-myc protein instability c-myc/max complex c-myc binding sites e-box motif proto-oncogenic transcription factors c-myc–mediated physiological time-dependently inhibited rpmi-8226 targeting c-myc myc-max oncoprotein complex transcription factor c-myc c-myc promoter activity structure-based virtual screening c-myc downstream targets c-myc/max heterodimer phosphorylate c-myc thr58 pim kinase-dependent inhibition p-c-myc ser62

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Novel dual-targeting c-Myc inhibitor D347-2761 represses myeloma growth via blocking c-Myc/Max heterodimerization and disturbing its stability
         description:Transcription factor c-Myc plays a critical role in various physiological and pathological events. c-Myc gene rearrangement is closely associated with multiple myeloma (MM) progression and drug resistance. Thereby, targeting c-Myc is expected to be a useful therapeutic strategy for hematological disease, especially in MM. Molecular docking-based virtual screening and dual-luciferase reporter gene assay were used to identify novel c-Myc inhibitors. Cell viability and flow cytometry were performed for evaluating myeloma cytotoxicity. Western blot, immunofluorescence, immunoprecipitation, GST pull down and Electrophoretic Mobility Shift Assay were performed for protein expression and interaction between c-Myc and Max. c-Myc downstream targets were measured by Q-PCR and Chromatin immunoprecipitation methods. Animal experiments were used to detect myeloma xenograft and infiltration in vivo. We successfully identified a novel c-Myc inhibitor D347-2761, which hindered the formation of c-Myc/Max heterodimer and disturbed c-Myc protein stability simultaneously. Compound D347-2761 dose-and time-dependently inhibited myeloma cell proliferation and induced apoptosis. Dual knockout Bak/Bax partially restored D347-2761-mediated cell death. Additionally, compound D347-2761 could, in combination with bortezomib (BTZ), enhance MM cell DNA damage and overcome BTZ drug resistance. Our in vivo studies also showed that compound D347-2761 repressed myeloma growth and distal infiltration by downregulating c-Myc expression. Mechanistically, novel dual-targeting c-Myc inhibitor D347-2761 promoted c-Myc protein degradation via stimulating c-Myc Thr58 phosphorylation levels, which ultimately led to transcriptional repression of CDK4 promoter activity. We identified a novel dual-targeting c-Myc small molecular inhibitor D347-2761. And this study may provide a solid foundation for developing a novel therapeutic agent targeting c-Myc.
         datePublished:2022-05-26T00:00:00Z
         dateModified:2022-05-26T00:00:00Z
         pageStart:1
         pageEnd:16
         license:http://creativecommons.org/publicdomain/zero/1.0/
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         keywords:
            c-Myc inhibitor
            Multiple myeloma
            DNA damage
            Drug resistance
            Apoptosis
            Cell Biology
            Protein-Ligand Interactions
            Receptors
            Cytokines and Growth Factors
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                        name:Blood Diseases Institute, Xuzhou Medical University, Xuzhou, China
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               name:Yan Zhang
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               name:Kailin Xu
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      headline:Novel dual-targeting c-Myc inhibitor D347-2761 represses myeloma growth via blocking c-Myc/Max heterodimerization and disturbing its stability
      description:Transcription factor c-Myc plays a critical role in various physiological and pathological events. c-Myc gene rearrangement is closely associated with multiple myeloma (MM) progression and drug resistance. Thereby, targeting c-Myc is expected to be a useful therapeutic strategy for hematological disease, especially in MM. Molecular docking-based virtual screening and dual-luciferase reporter gene assay were used to identify novel c-Myc inhibitors. Cell viability and flow cytometry were performed for evaluating myeloma cytotoxicity. Western blot, immunofluorescence, immunoprecipitation, GST pull down and Electrophoretic Mobility Shift Assay were performed for protein expression and interaction between c-Myc and Max. c-Myc downstream targets were measured by Q-PCR and Chromatin immunoprecipitation methods. Animal experiments were used to detect myeloma xenograft and infiltration in vivo. We successfully identified a novel c-Myc inhibitor D347-2761, which hindered the formation of c-Myc/Max heterodimer and disturbed c-Myc protein stability simultaneously. Compound D347-2761 dose-and time-dependently inhibited myeloma cell proliferation and induced apoptosis. Dual knockout Bak/Bax partially restored D347-2761-mediated cell death. Additionally, compound D347-2761 could, in combination with bortezomib (BTZ), enhance MM cell DNA damage and overcome BTZ drug resistance. Our in vivo studies also showed that compound D347-2761 repressed myeloma growth and distal infiltration by downregulating c-Myc expression. Mechanistically, novel dual-targeting c-Myc inhibitor D347-2761 promoted c-Myc protein degradation via stimulating c-Myc Thr58 phosphorylation levels, which ultimately led to transcriptional repression of CDK4 promoter activity. We identified a novel dual-targeting c-Myc small molecular inhibitor D347-2761. And this study may provide a solid foundation for developing a novel therapeutic agent targeting c-Myc.
      datePublished:2022-05-26T00:00:00Z
      dateModified:2022-05-26T00:00:00Z
      pageStart:1
      pageEnd:16
      license:http://creativecommons.org/publicdomain/zero/1.0/
      sameAs:https://doi.org/10.1186/s12964-022-00868-6
      keywords:
         c-Myc inhibitor
         Multiple myeloma
         DNA damage
         Drug resistance
         Apoptosis
         Cell Biology
         Protein-Ligand Interactions
         Receptors
         Cytokines and Growth Factors
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                     type:PostalAddress
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                  name:The Affiliated Hospital of Xuzhou Medical University
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            name:Linlin Liu
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                  address:
                     name:College of Medical Imaging, Xuzhou Medical University, Xuzhou, China
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               type:PostalAddress
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      name:Linlin Liu
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            name:Xuzhou Medical University
            address:
               name:College of Medical Imaging, Xuzhou Medical University, Xuzhou, China
               type:PostalAddress
            type:Organization
      name:Yan Zhang
      affiliation:
            name:Xuzhou Medical University
            address:
               name:Blood Diseases Institute, Xuzhou Medical University, Xuzhou, China
               type:PostalAddress
            type:Organization
      name:Jian Gao
      affiliation:
            name:Xuzhou Medical University
            address:
               name:Jiangsu Key Laboratory of New Drug Research and Clinical Pharmacy, Xuzhou Medical University, Xuzhou, China
               type:PostalAddress
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      email:[email protected]
      name:Kailin Xu
      url:http://orcid.org/0000-0003-1375-1084
      affiliation:
            name:Xuzhou Medical University
            address:
               name:Blood Diseases Institute, Xuzhou Medical University, Xuzhou, China
               type:PostalAddress
            type:Organization
            name:The Affiliated Hospital of Xuzhou Medical University
            address:
               name:Department of Hematology, The Affiliated Hospital of Xuzhou Medical University, Xuzhou, China
               type:PostalAddress
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      email:[email protected]
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      name:Blood Diseases Institute, Xuzhou Medical University, Xuzhou, China
      name:Department of Hematology, The Affiliated Hospital of Xuzhou Medical University, Xuzhou, China
      name:Xuzhou Ruihu Health Management and Consulting Co., Ltd, Xuzhou, China
      name:Blood Diseases Institute, Xuzhou Medical University, Xuzhou, China
      name:Blood Diseases Institute, Xuzhou Medical University, Xuzhou, China
      name:College of Medical Imaging, Xuzhou Medical University, Xuzhou, China
      name:Blood Diseases Institute, Xuzhou Medical University, Xuzhou, China
      name:Jiangsu Key Laboratory of New Drug Research and Clinical Pharmacy, Xuzhou Medical University, Xuzhou, China
      name:Blood Diseases Institute, Xuzhou Medical University, Xuzhou, China
      name:Department of Hematology, The Affiliated Hospital of Xuzhou Medical University, Xuzhou, China

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