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. 2023 Sep 29;42:253. doi: 10.1186/s13046-023-02815-w

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 7 — The mechanism of reduced intracellular lactate induced by oxamate leading to H3K18 lactylation on CD39, CD73 and CCR8 gene promotors. Oxamate inhibits lactate production and release into TME. Reduced lactate in GSCs and T cells suppresses histone H3K18 lactylation, leading to the decrease of CD73 gene promotor activity. Low level of H3K18 lactylation restrains the activity of CD39 gene promotor in Treg cells and macrophages. The conversion of ATP to AMP then to adenosine is inhibited by reduced levels of CD39 and CD73, respectively. Reduced CCR8 level due to low H3K18 lactylation blocks the binding to its ligands CCL1 and CCL18 secreted by macrophages. Oxamate changes the immunosuppressive microenvironment of GBM and improves the effect of CAR-T therapy