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- W2913261672 abstract "Histone3‐lysine9 (H3K9) residues not only control gene expression, but also contribute to RNA splicing. Here, the H3K9 histone demethylase PHF 8 was investigated in endothelial cells for its involvement in alternative splicing. An angiogenic sprouting assay shows the importance of PHF 8 for endothelial cells. Immunoprecipitation reveals that PHF 8 interacts with U1 spliceosomal proteins, such as SRPK 1 and sn RNP 70. We identify the histocompatibility antigen HLA ‐G as a target of PHF 8. The inclusion of HLA ‐G intron 4, with concomitant RNA Polymerase II accumulation at this intron is controlled by PHF 8 and H3K9. Soluble HLA ‐G is generated after PHF 8 knockdown, which leads to reduced T‐cell proliferation. Collectively, PHF 8 knockdown generates the immunosuppressive alternative splice product soluble HLA ‐G, which is secreted by endothelial cells to elicit a potential inhibitory effect on inflammation." @default.
- W2913261672 created "2019-02-21" @default.
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- W2913261672 date "2019-02-27" @default.
- W2913261672 modified "2023-10-14" @default.
- W2913261672 title "The histone demethylase <scp>PHF</scp> 8 facilitates alternative splicing of the histocompatibility antigen <scp>HLA</scp> ‐G" @default.
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- W2913261672 doi "https://doi.org/10.1002/1873-3468.13337" @default.
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