Dataset Information

Effects of MINCH exposure on the acetylome of differentiating human SGBS adipocytes

ABSTRACT: Here, we evaluated the molecular effects of MINCH exposure, as primary metabolite of the DEHP substitute DINCH, on the acetylome profiles of differentiating SGBS adipocytes. This study includes data on rosiglitazone differentiated controls, 10 µM MINCH exposure, and exposure to the selective PPAR inhibitor GW9662, as well as combinations thereof.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Stromal Cell

DISEASE(S): Simpson-golabi-behmel Syndrome Type 1

SUBMITTER: Alix Sarah Aldehoff

LAB HEAD: Kristin Schubert

PROVIDER: PXD059390 | Pride | 2025-08-05

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

Items per page:

1 - 5 of 39

Publications

Advanced Proteomics Approaches Hold Potential for the Risk Assessment of Metabolism-Disrupting Chemicals as Omics-Based NAM: A Case Study Using the Phthalate Substitute DINCH.

Aldehoff Alix Sarah AS Karkossa Isabel I Broghammer Helen H Krupka Sontje S Weiner Juliane J Goerdeler Cornelius C Nuwayhid Rima R Langer Stefan S Wabitsch Martin M Rolle-Kampczyk Ulrike U Klöting Nora N Blüher Matthias M Heiker John T JT von Bergen Martin M Schubert Kristin K

Environmental science & technology 20250730

The concept of metabolic disruption through exposure to chemicals has expanded our understanding of how environmental pollution can contribute to metabolic dysregulation and, ultimately, diseases like obesity. New strategies for assessing the risks posed by chemicals are needed, and omics technologies, including proteomics, have proven to be powerful tools for investigating the molecular mechanisms of these metabolism-disrupting chemicals (MDCs). A potential MDC is the plasticizer DINCH─an alter ...[more]

PMID: 40736767

Similar Datasets

Project description:Alcohol consumption induces hepatocyte damage through complex processes involving oxidative stress and disrupted metabolism. Combined, these factors alter proteomic and epigenetic marks providing a critical opportunity to identify therapeutic targets. Indeed, alcohol-induced protein acetylation is a key post-translational modification (PTM) that regulates hepatic metabolism and is associated with the pathogenesis of alcohol-associated liver disease (ALD). Interestingly, recent evidence suggests lysine acetylation occurs when a proximal cysteine residue is within ~15 Å of a lysine residue, referred to as a cysteine-lysine (Cys-Lys) pair. Here, acetylation can occur through the transfer of an acetyl moiety via an S à N acetyl transfer reaction. Alcohol-mediated hepatic redox stress is known to occur coincident with lysine acetylation, but the biochemical mechanisms related to cysteine and lysine crosstalk within ALD remain unexplored. A chronic murine model of ALD was employed to quantify hepatic cysteine redox and lysine acetylation, revealing that alcohol metabolism significantly reduced the cysteine proteome and increased protein acetylation. Interrogating both cysteine redox and lysine acetylation datasets, 1,281 proteins were mapped by AlphaFold2 to quantify distances between 557,815 cysteine and lysine residues. This process identified 388,698 Cys-Lys pairs that were further used to evaluate thiol redox signaling. Our analysis reveals that alcohol metabolism induces redox changes and acetylation selectively on proximal Cys-Lys pairs with an odds ratio of 1.89 (p< 0.0001). We also identified key redox signaling hubs embedded in metabolic pathways associated with ALD, including lipid metabolism, the TCA cycle, and the electron transport chain. Specific protein targets embedded across these pathways include Echs1, Glrx5, Decr2, and Adh1, among many others. Interestingly, these proximal Cys-Lys exist as four major protein motifs represented by the number of Cys and Lys residues that are pairing (Cysx-Lysx). These motifs include Cys1:Lys1, Cysx:Lys1, Cys1:Lysx and Cysx:Lysx each with a unique microenvironment likely indicative of the mode of enzymatic regulation occurring. The motifs are composed of functionally relevant amino acids altered within ALD, identifying sites of therapeutic potential. Furthermore, these unique Cys-Lys redox signatures are translationally relevant as revealed by orthologous comparison with severe alcohol-associated hepatitis (SAH) explants, revealing numerous pathogenic thiol redox signals in these patients.

			Action	DRS
	145_SGBS_GWMINCH_6_1.raw	Raw
	145_SGBS_GWMINCH_6_2.raw	Raw
	145_SGBS_GWMINCH_6_3.raw	Raw
	145_SGBS_GWMINCH_6_4.raw	Raw
	145_SGBS_GW_4_1.raw	Raw