Dataset Information

Effects of dietary DINCH exposure on the proteome, phosphoproteome and acetylome of adipose tissue of a murine diet induced model of obesity

ABSTRACT: Here, we evaluated the molecular effects of dietary DINCH exposure, on the proteome, phosphoproteome and acetylome profiles of visceral and subcutaneous adipose tissue in a model of diet-induced obesity in male and female C57BL/6N mice. This study includes data on visceral and subcutaneous adipose tissue of male and female mice that were either fed a standard high-fat diet (HFD) or two HFD diets including doses of DINCH (4,500 ppm and 15,000 ppm).

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Abdominal Adipose Tissue, Subcutaneous Adipose Tissue

SUBMITTER: Alix Sarah Aldehoff

LAB HEAD: Kristin Schubert

PROVIDER: PXD059421 | Pride | 2025-08-05

REPOSITORIES: Pride

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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 31

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

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Project description:Albeit much less abundant than Ser/Thr phosphorylation (pSer/pThr), Tyr phosphorylation (pTyr) is considered a hallmark in cellular signal transduction. However, its analysis remains a challenge. The conventional immunopurification (IP) approach using antibodies pan-specific to pTyr sites is known to have low sensitivity, poor reproducibility and high cost. SH2 domain-derived pTyr-superbinder is a good replacement of pTyr antibody for the specific enrichment of pTyr peptides for phosphoproteomics analysis. In this study, we aim to optimize the approach using SH2 superbinder for tyrosine phosphoproteome analysis. The present work covalently immobilized SH2 superbinders to agrose beads, designed and evaluated four different SH2 superbinder based experimental workflows for phosphotyrosine analysis. After made a head to head comparison of them, we observed that the combined strategy employing Ti4+-IMAC and covalently immobilized SH2 superbinder enrichment in sequence generated the largest pTyr peptide dataset (3519) with the best selectivity (90%). Next the optimal method was applied for pTyr profiling from normal mouse tissues, and resulted in the identification of 197 pTyr sites (of which 73 were novel) from 5 mg protein digests, which validated its high sensitivity. An comparison with antibody 4G10 by isolating pTyr peptides from 5 mg unstimulated Jurkat cell digests were made, our optimal strategy identified 343 while the antibody 4G10 based method identified 242 pTyr sites, respectively, further confirmed the robustness of the method. Finally, the optimal strategy was applied for quantitative pTyr phosphorylation analysis of EGF stimulated/unstimulated HeLa cells, 261 pTyr sites were successfully quantified from 5 mg stable-isotope dimethyl labling protein digests. In general, the combination of Ti4+-IMAC and SH2 superbinder enrichment in sequence generated a facial and robust strategy for qualitative and quantitative analysis of pTyr proteome.

			Action	DRS
	153_SC_AcK_fHFD_1.raw	Raw
	153_SC_AcK_fHFD_2.raw	Raw
	153_SC_AcK_fHFD_3.raw	Raw
	153_SC_AcK_fchow_1.raw	Raw
	153_SC_AcK_fchow_2.raw	Raw