FGF2 supports NANOG expression via pyruvate dehydrogenase-dependent histone acetylation under low oxygen conditions.

ABSTRACT:

Introduction

The safe and effective application of human pluripotent stem cells (hPSCs) in research and regenerative medicine requires precise control over pluripotency and cell fate. Pluripotency is characterized by high histone acetylation and aerobic glycolysis, while differentiation involves metabolic remodeling and reduced acetylation. Pyruvate dehydrogenase (PDH) links these processes by converting glycolytic pyruvate into acetyl coenzyme A (Ac-CoA), the key substrate for histone acetylation.

Methods

We investigated how PDH activity regulates histone acetylation and pluripotency maintenance under physiologically relevant oxygen levels (5% and 21% O₂). PDH contribution to histone acetylation was assessed using a specific PDH inhibitor, followed by rescue experiments wit

SUBMITTER: Fojtik P 

PROVIDER: S-EPMC12602506 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature