EZH2 inhibitor GSK126 suppresses antitumor immunity by driving production of myeloid-derived suppressor cells
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Abstract
Abstract Enhancer of zeste homolog (EZH2) is a key epigenetic regulator of gene expression and is frequently overexpressed in various cancer types, suggesting a role in oncogenesis. The therapeutic potential of EZH2 inhibitors is currently being explored, but their effect on antitumor immunity is largely unknown. Here we report that suppressing EZH2 activity using EZH2 inhibitor GSK126 resulted in increased numbers of myeloid-derived suppressor cells (MDSC) and fewer CD4+ and IFNγ+CD8+ T cells, which are involved in antitumor immunity. Addition of a neutralizing antibody against the myeloid differentiation antigen GR-1 or gemcitabine/5-fluorouracil–depleted MDSCs alleviated MDSC-mediated immunosuppression and increased CD4+ and CD8+ T-cell tumor infiltration and GSK126 therapeutic efficacy. Mechanistically, we identified a novel pathway of MDSC production in cancer in which EZH2 inhibition directs myeloid differentiation from primitive hematopoietic progenitor cells. These findings suggest that modulating the tumor immune microenvironment may improve the efficacy of EZH2 inhibitors. Significance: This study uncovers a potential mechanism behind disappointing results of a phase I clinical trial of EZH2 inhibitor GSK126 and identifies a translatable combinational strategy to overcome it.
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The EZH2 inhibitor GSK126 promotes MDSC expansion and immunosuppressive functions.
“EZH2 inhibition with GSK126 reportedly favors MDSC expansion and immunosuppressive functions”
From Immunomodulation by targeted anticancer agents (2021) · cites this paper as Huang et al., 2019
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Greer, C. B., Wright, J., Weiss, J. D., Lazarenko, R. M., Moran, S. P., Zhu, J., Chronister, K. S., Jin, A., Kennedy, A. J., Sweatt, J. D., et al. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.1821-20.2020 · Cited by 41 · see citing works
“To test whether H3K27me3-mediated silencing accounted for differences in Tet1 expression between glia and neurons, we blocked formation of the repressive mark using the two histone-lysine N-methyltransferase Enhancer of Zeste Homolog 2 (EZH2) inhibitors, GSK126 and GSK343 (Verma et al., 2012; Huang et al., 2019).”
MethodAdvances in Epigenetic Cancer Therapeutics
Hillyar, C., Rallis, K. S., & Varghese, J. S. (2020) · Cureus · doi:10.7759/cureus.11725 · Cited by 40 · see citing works
“GSK126 reduces anti-tumour immunity by increasing the number of myeloid-derived suppressor cells, leading to fewer CD4+ and CD8+ T cells in the tumour microenvironment [28].”
BackgroundEzh2 competes with p53 to license lncRNA Neat1 transcription for inflammasome activation
Yuan, J., Zhu, Q., Zhang, X., Wen, Z., Zhang, G., Li, N., Pei, Y., Wang, Y., Pei, S., Xu, J., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00992-3 · Cited by 37 · see citing works
“Targeting SETmediated methyltransferase activity through the selective inhibitor GSK126 has been applied in clinical trials for the treatment of patients with multiple types of tumours [14, 42, 43].”
EZH2: An Accomplice of Gastric Cancer
Yu, W., Liu, N., Song, X., Chen, L., Wang, M., Xiao, G., Li, T., Wang, Z., & Zhang, Y. (2023) · Cancers · doi:10.3390/cancers15020425 · Cited by 37 · see citing works
“In another study, however, GSK126 exerted anti-tumor activity in immunologically active hosts combined with drugs (gemcitabine and 5-fluorouracil) that deplete myeloid-derived suppressor cells [104].”
BackgroundLi, L., Zhang, H., Zhou, Z., Duan, L., Fan, D., Wang, R., Xu, S., Qiao, D., & Zhu, W. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116470 · Cited by 37 · see citing works
EZH2: The roles in targeted therapy and mechanisms of resistance in breast cancer
Chen, Y., Zhu, H., Luo, Y., Tong, S., & Liu, Y. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116624 · Cited by 35 · see citing works
Histone Methylation Related Therapeutic Challenge in Cardiovascular Diseases
Yang, Y., Luan, Y., Luan, Y., & Luan, Y. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.710053 · Cited by 34 · see citing works
“Among these inhibitors, GSK126 is a potent and highly selective methyltransferase inhibitor for the histone methyltransferase EZH2 [Figure 4; (143)].”
BackgroundEZH2 Inhibitor Enhances the STING Agonist‒Induced Antitumor Immunity in Melanoma
Xu, T., Dai, J., Tang, L., Yang, L., Si, L., Sheng, X., Cui, C., Chi, Z., Kong, Y., & Guo, J. (2021) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2021.08.437 · Cited by 34 · see citing works
Huang, J., Zhang, J., Guo, Z., Li, C., Tan, Z. W., Wang, J., Yang, J., & Xue, L. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.741302 · Cited by 32 · see citing works
Uceda, S., Echeverry‐Alzate, V., Reiriz, M., Miguel, E. M., Pérez-Curiel, A., Gómez-Senent, S., & Beltrán-Velasco, A. I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713294 · Cited by 35 · see citing works
Liu, W., Kuang, T., Liu, L., & Deng, W. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1407449 · Cited by 32 · see citing works
The Role of Histone Modification in DNA Replication-Coupled Nucleosome Assembly and Cancer
Zhang, Y., Zhang, Q., Zhang, Y., & Han, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054939 · Cited by 32 · see citing works
Hou, Y., Žák, J., Shi, Y., Pratumchai, I., Dinner, B., Wang, W., Qin, K., Weber, E. W., Teijaro, J. R., & Wu, P. (2024) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-24-0089 · Cited by 31 · see citing works
Mechanism and Therapeutic Opportunities of Histone Modifications in Chronic Liver Disease
Cai, Q., Gan, C., Tang, C., Wu, H. M., & Gao, J. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.784591 · Cited by 30 · see citing works
“…Methylates histone H3K36 and H3K4 — Perugorria et al. (2012) EZH2 4MI5 Methylates histone H3K27 Tazemetostat; Valemetostat, GSK126, CPI0209, CPI-1205 Huang et al. (2019), Bates (2020) SETDB1 3DLM Methylates histone H3K9 Mithramycin, DZNep Rivière et al. (2015), Karanth et al. (2017) MLL4/KMT2D,…”
Polycomb Directed Cell Fate Decisions in Development and Cancer
German, B., & Ellis, L. (2022) · Epigenomes · doi:10.3390/epigenomes6030028 · Cited by 36 · see citing works
“Interestingly, the depletion of MDSCs in TME promotes antitumor immune responses through the increased infiltration of functional T-cells [245].”
BackgroundLiu, Q., Yu, M., Lin, Z., Wu, L., Xia, P., Zhu, M., Huang, B., Wu, W., Zhang, R., Li, K., et al. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.217731 · Cited by 30 · see citing works
Qiu, J., Sharma, S., Rollins, R. A., & Paul, T. A. (2020) · Future Medicinal Chemistry · doi:10.4155/fmc-2020-0072 · Cited by 29 · see citing works
Reversing Epigenetic Gene Silencing to Overcome Immune Evasion in CNS Malignancies
Ratnam, N. M., Sonnemann, H. M., Frederico, S. C., Chen, H. A., Hutchinson, M.-K. N. D., Dowdy, T., Reid, C. M., Jung, J., Zhang, W., Song, H., et al. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.719091 · Cited by 28 · see citing works
Hegde, M., Kumar, A., Girisa, S., Alqahtani, M. S., Abbas, M. A. E., Goel, A., Hui, K. M., Sethi, G., & Kunnumakkara, A. B. (2023) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2023.06.001 · Cited by 28 · see citing works
Chemical biology and pharmacology of histone lysine methylation inhibitors
Barghout, S. H., Machado, R. A. C., & Baršytė-Lovejoy, D. (2022) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2022.194840 · Cited by 27 · see citing works
Lanzi, C., Arrighetti, N., Pasquali, S., & Cassinelli, G. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115727 · Cited by 27 · see citing works
Al‐Ghabkari, A., & Narendran, A. (2021) · Cancer Biology & Therapy · doi:10.1080/15384047.2021.1902913 · Cited by 26 · see citing works
“cytotoxic activity of a panel of EZH2-selcetive inhibitors; GSK343 [37], DZNep [38], GSK126 [39], EI1 [40], EPZ-5687 [41], UNC1999 [42], EPZ-6438 [43], and GSK503 [44].”
Maher, N., Maiellaro, F., Ghanej, J., Rasi, S., Moia, R., & Gaïdano, G. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26178132 · Cited by 25 · see citing works
“For instance, GSK126, despite its strong preclinical activity against mutant EZH2 , failed to show meaningful clinical responses in a phase I trial in R/R DLBCL, transformed FL, and other NHL, leading to early trial termination [139,140].”
Epigenetic Modifiers: Anti-Neoplastic Drugs With Immunomodulating Potential
Maes, K., Mondino, A., Lasarte, J. J., Agirre, X., Vanderkerken, K., Prósper, F., & Breckpot, K. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.652160 · Cited by 25 · see citing works
“The inhibition of the H3K27me3 HMT EZH2 using GSK126 increased the presence of MDSC within the TME of LLC (Lewis FIGURE 2 | Epigenetic factors that regulate TADC activity.”
BackgroundSunitinib attenuates reactive MDSCs enhancing anti-tumor immunity in HNSCC
Liu, J., Lin, W., Su, W., Wu, Z., Yang, Q., Wang, S., Sun, T.-G., Huang, C., Wang, X., & Sun, Z. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110243 · Cited by 25 · see citing works
Xiao, C., Fan, T. T., Zheng, Y., Tian, H., Deng, Z., Liu, J., Li, C., & He, J. (2023) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2022-005693 · Cited by 25 · see citing works
The functions of EZH2 in immune cells: Principles for novel immunotherapies
Shao, F.-F., Chen, B.-J., & Wu, G. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.1ru0520-311r · Cited by 23 · see citing works
Mola, S., Pinton, G., Erreni, M., Corazzari, M., Andrea, M. D., Grolla, A. A., Martini, V., Moro, L., & Porta, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094391 · Cited by 25 · see citing works
“Inhibition of EZH2 has been reported to be linked with enhanced NK and T cell effector activities in certain cancers [25], as well as with an increased expansion of myeloid-derived suppressor cells (MDSCs) and consequent suppression of antitumor immunity [44].”
BackgroundEZH2 presents a therapeutic target for neuroendocrine tumors of the small intestine
Barazeghi, E., Hellman, P., Norlén, O., Westin, G., & Stalberg, P. L. H. (2021) · Scientific Reports · doi:10.1038/s41598-021-02181-7 · Cited by 23 · see citing works
PD-L1 small-molecule modulators: A new hope in epigenetic-based multidrug cancer therapy?
Zwergel, C., Fioravanti, R., & Mai, A. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.103435 · Cited by 23 · see citing works
Liu, K., Li, Y., Shen, M., Xu, W., Wu, S., Yang, X., Zhang, B., & Lin, N. (2025) · Biomolecules · doi:10.3390/biom15010071 · Cited by 23 · see citing works
“The EZH2 inhibitor GSK126 was reported to direct myeloid differentiation and resulted in MDSC accumulation and TIL exclusion in syngeneic mouse models of lung cancers and colon cancer [161].”
Xiao, L., Zhou, Z., Li, W., et al. (2019) · Aging · doi:10.18632/aging.102241 · Cited by 22 · see citing works
Treating human cancer by targeting EZH2
Xu, M., Xu, C., Wang, R., Tang, Q., Zhou, Q., Wu, W., Wan, X., Mo, H., Pan, J., & Wang, S. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2024.101313 · Cited by 22 · see citing works
“…anti-tumor effect than EZH2 selective inhibitor 114 ; gemcitabine/5-fluorouracil plus GSK126 combination therapy improves the efficacy of GSK126 and blocks tumor growth 117 ; combined anti-C-C motif chemokine ligand 2 therapy may improve the efficacy of EZH2 inhibitors in breast cancer treatment.”
Regulation of histone H3K27 methylation in inflammation and cancer
Ma, J., Zhang, Y., Li, J., Dang, Y., & Hu, D. (2025) · Molecular Biomedicine · doi:10.1186/s43556-025-00254-x · Cited by 25 · see citing works
“GSK126, an EZH2 inhibitor, induced MDSC production and suppressed T-cell-mediated tumor immunity, masking its tumor-suppressing effects [149].”
Prognostic Value of EZH2 in Non‐Small‐Cell Lung Cancers: A Meta‐Analysis and Bioinformatics Analysis
Fan, K., Zhang, C., Qi, Y., Dai, X., Birling, Y., Tan, Z., & Cao, F. (2020) · BioMed Research International · doi:10.1155/2020/2380124 · Cited by 21 · see citing works
Targeting EZH2 to overcome the resistance to immunotherapy in lung cancer
Shin, D. S., Park, K., Garon, E. B., & Dubinett, S. M. (2022) · Seminars in Oncology · doi:10.1053/j.seminoncol.2022.06.005 · Cited by 20 · see citing works
Fischetti, I., Botti, L., Sulsenti, R., Cancila, V., Enriquez, C., Ferri, R., Bregni, M., Crivelli, F., Tripodo, C., Colombo, M. P., et al. (2024) · Epigenomics · doi:10.2217/epi-2023-0374 · Cited by 20 · see citing works
“Thus, our data do not contradict the findings from the paper of Huang et al. [25] , which tested GSK-126 as a single agent (showing that only doses higher than 50 mg / Kg have antitumor activity).”
BackgroundResultThe Adhesome Network: Key Components Shaping the Tumour Stroma
Nikolopoulou, P., Koufaki, M. A., & Kostourou, V. (2021) · Cancers · doi:10.3390/cancers13030525 · Cited by 21 · see citing works
“Interestingly, a recent study showed that Ezh2 inhibition in mice increased the number of immunosuppressive CD11b+Gr1+ cells within subcutaneous tumours [252].”
BackgroundEZH2 regulatory roles in cancer immunity and immunotherapy
Mortezaee, K. (2025) · Pathology - Research and Practice · doi:10.1016/j.prp.2025.155992 · Cited by 20 · see citing works
AI‐Assisted Drug Re‐Purposing for Human Liver Fibrosis
Guan, Y., Cui, L., Inchai, J., Fang, Z., Law, J., Brito, A. A. G., Pawlosky, A., Gottweis, J., Daryin, A., Myaskovsky, A., et al. (2025) · Advanced Science · doi:10.1002/advs.202508751 · Cited by 19 · see citing works
Yang, J. C., Weisberg, E., Qi, S., Wei Min, N. I., Mei, H., Wang, Z., Meng, C., Zhang, S., Hou, M., Qi, Z., et al. (2022) · Leukemia · doi:10.1038/s41375-021-01494-w · Cited by 19 · see citing works
Obesity-associated epigenetic alterations and the obesity-breast cancer axis
Lagarde, C. B., Kavalakatt, J., Benz, M. C., Hawes, M. L., Arbogast, C. A., Cullen, N. M., McConnell, E. C., Rinderle, C. H., Hebert, K. L., Khosla, M., et al. (2024) · Oncogene · doi:10.1038/s41388-024-02954-0 · Cited by 19 · see citing works
“Interestingly, treatment with selective EZH2 inhibitors promoted M2 TAM in fi ltration and suppressed anti-tumor immune responses [96, 97].”
He, L., Liao, L., & Du, L. (2020) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2020.4638 · Cited by 19 · see citing works
“In addition, inhibition experiments were performed using the EZH2 inhibitor, GSK126 (a compound competes with S-adenosyl-methionine for binding to EZH2, thereby inhibiting histone methyltransferase activity without affecting EZH2 protein expression), as previously described (16).”
MethodWu, L., Xu, Y., Zhao, H., Zhou, Y. J., Chen, Y., Yang, S., Lei, J., Zhang, J., Wang, J., Wu, Y., et al. (2021) · Theranostics · doi:10.7150/thno.66575 · Cited by 18 · see citing works
“Multiple evidence indicates that depletion of MDSCs by treatment with anti-Gr-1 neutralizing antibody or gemcitabine can restore immune surveillance and improve the efficacy of cancer immunotherapies in vivo [10, 34].”
BackgroundCui, H., Lan, Z., Zou, K., Zhao, Y., & Yu, G. (2022) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-022-03336-9 · Cited by 18 · see citing works
Tan, L., Qin, Y., Xie, R., Xia, T., Duan, X., Peng, L., You, R., Liu, Y., Zou, X., Zhang, M., et al. (2022) · Theranostics · doi:10.7150/thno.76689 · Cited by 18 · see citing works
“The previous study has shown that suppressing EZH2 activity resulted in increased numbers of myeloid-derived suppressor cells (MDSC) and fewer CD4+ and IFNγ+CD8+ T cells, which are involved in antitumor immunity [40].”
BackgroundPickles, O. J., Wanigasooriya, K., Ptasinska, A., Patel, A. J., Robbins, H. L., Bryer, C., Whalley, C., Tee, L. J., Lal, N., Pinna, C. M. A., et al. (2023) · Cancer Research Communications · doi:10.1158/2767-9764.crc-23-0091 · Cited by 18 · see citing works
Nanomedicine and epigenetics: New alliances to increase the odds in pancreatic cancer survival
Urbanova, M., Cihova, M., Buociková, V., Slopovský, J., Dubovan, P., Pinďák, D., Tomáš, M., García‐Bermejo, L., Rodríguez-Garrote, M., Earl, J., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115179 · Cited by 18 · see citing works
The Growing Relevance of Immunoregulation in Pediatric Brain Tumors
Melcher, V., & Kerl, K. (2021) · Cancers · doi:10.3390/cancers13225601 · Cited by 17 · see citing works
“This epigenetic intervention restrained tumor growth in immunocompromised mice but not in immunocompetent mice [94].”
BackgroundMxi1 participates in the progression of lung cancer via the microRNA-300/KLF9/GADD34 Axis
Lei, Y., Huang, Y., Lin, J., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04778-w · Cited by 17 · see citing works
“It has been previously noted that depletion of MDSCs is able to alleviate MDSC-mediated immunosuppression [36].”
BackgroundCombining EZH2 inhibitors with other therapies for solid tumors: more choices for better effects
Huang, R., Wu, Y., & Zou, Z. (2022) · Epigenomics · doi:10.2217/epi-2022-0320 · Cited by 17 · see citing works
Sylvestre, M., Tarte, K., & Roulois, D. (2019) · Epigenomics · doi:10.2217/epi-2019-0165 · Cited by 17 · see citing works
Evolution and Targeting of Myeloid Suppressor Cells in Cancer: A Translational Perspective
Bleve, A., Consonni, F. M., Porta, C., Garlatti, V., & Sica, A. (2022) · Cancers · doi:10.3390/cancers14030510 · Cited by 17 · see citing works
Fan, K., Zhang, B.-H., Deng, H., & Sun, Y.-C. (2023) · BMC Bioinformatics · doi:10.1186/s12859-023-05271-7 · Cited by 16 · see citing works
“The increased efficacy of anti-CTLA-4 immunotherapy and enhanced overall survival in tumor models of syngeneic mice [58, 59].”
BackgroundHistone Modifications and Their Targeting in Lymphoid Malignancies
Fernández-Serrano, M., Winkler, R., Santos, J. C., Pannérer, M.-M. L., Buschbeck, M., & Roué, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010253 · Cited by 14 · see citing works
“More recently, two orally bioavailable EZH1/2 dual inhibitors, (R)-OR-S1 and (R)-OR-S2, demonstrated improved antitumor activity in in vitro and in vivo models of EZH2MUT DLBCL with no significant toxicity [199].”
BackgroundInfluentialCombinatorial Epigenetic and Immunotherapy in Breast Cancer Management: A Literature Review
Lee, Y.-T., Chuang, Y., & Chan, M. W. Y. (2020) · Epigenomes · doi:10.3390/epigenomes4040027 · Cited by 16 · see citing works
“reported that suppressing EZH2 activity promotes hematopoietic progenitor cell differentiation to myeloid-derived suppressor cells (MDSCs), and increases MDSCs in the tumor microenvironment, thus suppressing antitumor immunity [89].”
BackgroundOne-carbon metabolism in cancer: moonlighting functions of metabolic enzymes and anti-tumor therapy
Cao, X., Guo, Y., Guo, Z., Liu, Y., Dou, Y., & Xue, L. (2025) · Cancer and Metastasis Reviews · doi:10.1007/s10555-025-10308-9 · Cited by 16 · see citing works
Yan, H., Shi, J., Dai, Y., Li, X., Wu, Y., Zhang, J., Gu, Z., Zhang, C., & Leng, J. (2022) · Cancer Cell International · doi:10.1186/s12935-022-02580-4 · Cited by 15 · see citing works
“have found modulating MDSCs in TME may improve the efficacy of EZH2 inhibitors to suppress antitumor immunity [113].”
BackgroundDesign, Synthesis, and Biological Evaluation of Potent EZH2/LSD1 Dual Inhibitors for Prostate Cancer
Le, M.-L., Lu, W., Tan, X., Luo, B., Yu, T., Sun, Y., Guo, Z., Huang, P., Zhu, D., Wu, Q., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01250 · Cited by 15 · see citing works
The correlation of EZH2 expression with the progression and prognosis of hepatocellular carcinoma
Wu, S.-Y., Xie, Z., Yan, L.-Y., Liu, X., Zhang, Y., Wang, D., Dong, J., & Sun, H. (2022) · BMC Immunology · doi:10.1186/s12865-022-00502-7 · Cited by 15 · see citing works
Potential therapies targeting nuclear metabolic regulation in cancer
Chen, Y., Xu, J., Liu, X., Guo, L., Yi, P., & Cheng, C. (2023) · MedComm · doi:10.1002/mco2.421 · Cited by 14 · see citing works
- Authors
- Huang, S., Wang, Z., Zhou, J., Huang, J., Zhou, L., Luo, J., Wan, Y. Y., Long, H., & Zhu, B.
- Affiliations
- Army Medical University (CN)
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Long, Haixia
- Zhu, Bo
- Venue
- Cancer Research
- Published
- 2019-04-15
- Volume
- 79
- Issue
- 8
- Pages
- 2009-2020
- ISSN
- 0008-5472 (ISSN-L)
- 1538-7445
- OpenAlex
- W2911341716
- Cited by
- 185
- References
- 43
- Citations by year
- 2026: 10 · 2025: 28 · 2024: 28 · 2023: 30 · 2022: 29 · 2021: 29 · 2020: 21 · 2019: 9
- FWCI
- 8.92
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cancer Research (publishedVersion)
- PubMed (publishedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- UNC Libraries
- Funders
- National Nature Science Foundation of China (81472648, 81802865, and 81620108023)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune cells in cancer
- Health Sciences › Medicine › Oncology › Cancer Immunotherapy and Biomarkers
- Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
- Keywords
- EZH2, GSK126, EZH2 inhibitors, myeloid-derived suppressor cells, antitumor immunity, tumor immune microenvironment, CD4+ T cells, CD8+ T cells, interferon-gamma, Gr-1, hematopoietic progenitor cells, myeloid differentiation, epigenetic regulation, combination therapy
- MeSH terms
- Enhancer of Zeste Homolog 2 Protein, Myeloid-Derived Suppressor Cells, Animals, Colonic Neoplasms, Female, Humans, Indoles, Mice, Inbred C57BL, Mice, Nude, Pyridones, Tumor Cells, Cultured, Apoptosis, CD8-Positive T-Lymphocytes, Carcinoma, Lewis Lung, Receptors, Chemokine, Xenograft Model Antitumor Assays, Cell Proliferation, Mice, Antibodies, Neutralizing
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