Abstract
Various types of histone methylation have been associated with cancer progression. Depending on the methylation site in histone proteins, its effects on transcription are different. DPY30 is a common member of SET1/MLL histone H3K4 methyltransferase complexes. However, its expression and roles in gastric cancer have been poorly characterized. To determine whether DPY30 has pathophysiological roles in gastric cancer, its expression and roles were examined. Immunohistochemistry and real time PCR showed up-regulation of DPY30 expression in some gastric cancer cell lines and patients’ tissues. Its knockdown by siRNA decreased the proliferation, migration, and invasion of gastric cancer cells, whereas its overexpression showed the opposite effects. These results indicate that DPY30 has critical roles in the proliferation, migration, and invasion of gastric cancer cells, and suggest DPY30 might be a therapeutic target in gastric cancer.
Highlights
Covalent modifications of histone tails, such as, acetylation, phosphorylation, ubiquitination, and methylation, modulate chromatin structure and play pivotal roles in the regulation of cellcycle progression, gene transcription, DNA repair, embryonic development, and cellular differentiation [1, 2]
These results indicate that DPY30 is highly expressed in some human gastric cancers
Roles of DPY30 in cancer biology have been poorly characterized its roles in differentiation of embryonic stem cells (ESCs) and hematopoietic progenitor cells had been reported [10, 12]
Summary
Covalent modifications of histone tails, such as, acetylation, phosphorylation, ubiquitination, and methylation, modulate chromatin structure and play pivotal roles in the regulation of cellcycle progression, gene transcription, DNA repair, embryonic development, and cellular differentiation [1, 2]. While increased histone acetylation is generally associated with transcriptional activation, the methylation of histone is correlated with transcriptional activation and repression. Mono-, di-, and tri-methylation of H3K4 (H3K4me, H3K4me, and H3K4me3) are performed by six distinct SET1/MLL family complexes (SET1A, SET1B, MLL1, MLL2, MLL3, and MLL4) [4, 5]. These H3K4 methyltransferases (H3K4MT) contain different catalytic subunits, and the activities of all six family complexes are controlled by common multi-subunit core components, which include WDR5, RBBP5, ASH2L, and DPY30, and are referred to as WRADs. WDR5 and RBBP5 are crucial for all three kinds of methylation of H3K4
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