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Transcriptomics and proteomics reveals the potential mechanisms of hydroquinone-inhibited erythroid differentiation in K562 cells.

Created on 14 Sep 2026

Authors

Chunhong Yu, Jiaxi Chen, Zetao Zhao, Xinyue Tan, Xinyu Liu, Zongchun Yi

Published in

Toxicology research. Volume 14. Issue 4. Pages tfaf093. Epub Jul 21, 2025.

Abstract

Hydroquinone (HQ), a key phenolic metabolite of benzene, plays a crucial role in the mechanisms underlying benzene-induced hematotoxicity and carcinogenicity. The mechanism of benzene-induced hematotoxicity hasn't been fully understood yet. The study aimed to elucidate the molecular mechanisms underlying benzene metabolites, HQ-inhibited erythroid differentiation. In this study, K562 cells were exposed to 40 μM HQ for 72 h, followed by induction with 40 μM Hemin for 48 h. Cell proliferation, hemoglobin synthesis, and gene and protein expression were assessed using trypan blue, benzidine staining, RT-PCR, RNA-seq, label-free proteomic analysis, and parallel reaction monitoring (PRM). The results demonstrated that HQ significantly inhibited erythroid differentiation in Hemin-induced K562 cells, downregulating key erythroid differentiation genes. HQ-induced differentially expressed genes (DEGs) and differentially expressed proteins (DEPs) were involved in oxidative stress, apoptosis, and erythroid differentiation-related GO terms, as well as metabolic, ferroptosis, biosynthesis of amino acids-related pathways. Network analysis identified five key hub proteins (MYB, ALAS1, ALAS2, FECH, and STAT5B) with the highest interaction scores, among which ALAS2 emerged as a potential major regulator in HQ-exposed K562 cells based on its role in erythroid differentiation. These findings provide novel insights into the molecular mechanisms underlying HQ-induced hematotoxicity and highlight potential therapeutic targets for mitigating the adverse effects of benzene exposure.

PMID:
40697400
Bibliographic data and abstract were imported from PubMed on 14 Sep 2026.

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