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OGA-mediated protein glycosylation regulates pluripotency states in human embryonic stem cells

ABSTRACT: In our previous study, we uncovered that OGA significantly elevated in naïve hESC. Therefore, we sought to investigate the effects of O-GlcNAc on hESC and the interconvert of both pluripotent states. Depletion of OGA, which results in global O-GlcNAcylation increased, would impair naïve hESC pluripotency but can promote naïve to primed hESC transition. In addition, we obtained the profiles of O-GlcNAcylated proteins in H9 primed hESC and H9-PXGL hESC via MS based-quantitative proteomics.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Zhiya Fan

LAB HEAD: Qin Weijie

PROVIDER: PXD041605 | Pride | 2024-08-10

REPOSITORIES: Pride

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O-GlcNAcase regulates pluripotency states of human embryonic stem cells.

Liu Qianyu Q Chen Cheng C Fan Zhiya Z Song Honghai H Sha Yutong Y Yu Liyang L Wang Yingjie Y Qin Weijie W Yi Wen W

Stem cell reports 20240627 7

Understanding the regulation of human embryonic stem cells (hESCs) pluripotency is critical to advance the field of developmental biology and regenerative medicine. Despite the recent progress, molecular events regulating hESC pluripotency, especially the transition between naive and primed states, still remain unclear. Here we show that naive hESCs display lower levels of O-linked N-acetylglucosamine (O-GlcNAcylation) than primed hESCs. O-GlcNAcase (OGA), the key enzyme catalyzing the removal o ...[more]

PMID: 38942028

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