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Proteomic Analysis of intersection protein that binds to KDM1A in Rat primary cardiomyocytes

ABSTRACT: The intersection proteins under hypoxia condition (0, 24, 48 h) in primary neonatal rat ventricular myocytes (NRVMs) were detected by Mass spectrometry.

INSTRUMENT(S):

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Myocardial Endocrine Cell Of Atrium, Cell Culture

DISEASE(S): Cardiovascular System Disease

SUBMITTER: Wan-Zhong Huang

LAB HEAD: Wan-Zhong Huang

PROVIDER: PXD070144 | Pride | 2026-01-19

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	CELL-24h-IP.raw	Raw
	CELL-24h-IP.txt	Txt
	CELL-48h-IP.raw	Raw
	CELL-48h-IP.txt	Txt
	CELL-Con-IP.raw	Raw

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Publications

USP16 S-nitrosylation aggravates coronary microembolization-induced myocardial injury via repressing KDM1A-mediated glutathione homeostasis.

Su Qiang Q Qin Jiao-Qin JQ Huang Yuan Y Dai Ri-Xin RX Wu Qing-Yun QY Mo Li-Rong LR Wu Qiang Q Huang Wan-Zhong WZ Yang Hua-Feng HF Liu Yang-Chun YC Pan Di-Guang DG

Nature communications 20251203 1

Coronary microembolization (CME) is a serious cardiovascular complication that causes severe cardiac dysfunction and arrhythmias. Glutathione (GSH) exhaustion-induced oxidative stress is a key contributor to CME. Here, we explore the molecular mechanisms underlying GSH imbalance during CME. We show that CME induces myocardial injury by disturbing GSH homeostasis, which is ameliorated by glutamate-cysteine ligase modifier subunit (GCLM) or glutaminase (GLS) overexpression. Lysine-specific histone ...[more]

PMID: 41339351

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Proteomic Analysis of the ubiquitination sites of KDM1A in rat myocardial tissue.

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