ArticleJournal of gastrointestinal oncology2021
AKT inhibits the phosphorylation level of H2A at Tyr57 via CK2α to promote the progression of gastric cancer.
Article in Journal of gastrointestinal oncology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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5 authors at 1 institution in 1 country.
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Abstract
backgroundHistone H2A and its variants have an important effect on DNA damage repair and cancer development. Protein kinase B (AKT) can regulate various cellular functions and play critical roles in the progression of different cancers. However, the interaction mechanism of H2A with AKT in gastric cancer (GC) has not been reported. A series of experiments were carried out in the present study to investigate this issue.
methodsFirstly, we used western blot and immunoprecipitation assays to determine the correlation between AKT and H2A, then detected the relationship between AKT and protein kinase CK2α that can phosphorylate H2A at Tyr57 site (H2A
resultsOur study preliminarily found that AKT was negatively correlated with H2A phosphorylation at the Tyr 57 site (H2A
conclusionsThese findings contribute to understanding the interactions among AKT, CK2α, and H2A in GC, and provide the potential biomarkers for the diagnosis and treatment of GC.
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