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Crosstalk between S-nitrosylation and glycation defines a novel metabolic vulnerability in liver and renal cancers

ABSTRACT: Methylglyoxal (MGO)-derived advanced glycation end products (AGEs) are hallmarks of carbonyl stress and contribute to cancer progression. Here, we established and validated an LC–MS/MS workflow to detect MGO-induced protein modifications in wild-type (WT) and AKR1A1 knockout (KO) Huh7 cells. Following MGO treatment, proteins were digested and analyzed by liquid chromatography–tandem mass spectrometry to identify characteristic glycation products, including methylglyoxal-derived hydroimidazolone (MG-H1) and Nε-(1-carboxyethyl)-L-lysine (CEL). Comparative analysis demonstrated increased accumulation of MGO-derived modifications in AKR1A1 KO cells compared with WT cells, consistent with impaired detoxification of reactive dicarbonyl species. These findings validate a robust LC–MS/MS workflow for profiling MGO-mediated protein glycation and support its application for investigating carbonyl stress in cancer models.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hepatocyte, Cell Culture

SUBMITTER: Marcus Nielsen

LAB HEAD: Marcus Nielsen

PROVIDER: PXD080543 | Pride | 2026-07-08

REPOSITORIES: Pride

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			Action	DRS
	20260408_HB_12_MVR_Batch1_sample12_1.raw	Raw
	20260408_HB_12_MVR_Batch1_sample12_2.raw	Raw
	20260408_HB_12_MVR_Batch1_sample12_3.raw	Raw
	20260408_HB_16_MVR_Batch1_sample16_1.raw	Raw
	20260408_HB_16_MVR_Batch1_sample16_2.raw	Raw

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