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An unbiased quantitative phosphoproteomics analysis in16HBE cells

ABSTRACT: An unbiased quantitative phosphoproteomics analysis in 16HBE cells treated with or without IL-13 and 2-D08.

ORGANISM(S): Homo Sapiens

SUBMITTER: Ximei Wu

PROVIDER: PXD042842 | iProX | Thu Jun 08 00:00:00 BST 2023

REPOSITORIES: iProX

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SUMOylation of Rho-associated protein kinase 2 induces goblet cell metaplasia in allergic airways.

Tan Dan D Lu Meiping M Cai Yuqing Y Qi Weibo W Wu Fugen F Bao Hangyang H Qv Meiyu M He Qiangqiang Q Xu Yana Y Wang Xiangzhi X Shen Tingyu T Luo Jiahao J He Yangxun Y Wu Junsong J Tang Lanfang L Barkat Muhammad Qasim MQ Xu Chengyun C Wu Ximei X

Nature communications 20230701 1

Allergic asthma is characterized by goblet cell metaplasia and subsequent mucus hypersecretion that contribute to the morbidity and mortality of this disease. Here, we explore the potential role and underlying mechanism of protein SUMOylation-mediated goblet cell metaplasia. The components of SUMOylaion machinery are specifically expressed in healthy human bronchial epithelia and robustly upregulated in bronchial epithelia of patients or mouse models with allergic asthma. Intratracheal suppressi ...[more]

PMID: 37393345

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Phosphoproteomics

Project description:Phosphoproteomics

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Project description:Allergic asthma is a chronic inflammatory airway disease driven by the cytokine interleukin-13 (IL-13). Although IL-13 signals through the canonical JAK1/TYK2/STAT6 pathway, our understanding of the totality of IL-13-induced signaling intermediates is incomplete. To address this, we performed an unbiased phospho-proteomic analysis of IL-13-stimulated A549 human airway epithelial cells. IL-13 stimulation led to differential phosphorylation at 145 unique serine/threonine residues across 97 proteins involved in diverse cellular processes. These processes included RNA splicing, cytoskeletal remodeling, GTPase activity, and focal adhesion complex formation. Network analysis identified SRC, a non-receptor tyrosine kinase, as a potential upstream regulator of IL-13-induced changes in phosphorylation. Kinetic molecular approaches confirmed that SRC is rapidly activated following IL-13 stimulation, prior to activation of the canonical IL-13 signaling intermediate STAT6 in both human and mouse lung fibroblasts. Pharmacological inhibition of SRC reduced IL-13–induced STAT6 phosphorylation and downstream gene expression in vitro. In vivo, SRC antagonism attenuated IL-13–induced airway hyperresponsiveness (AHR) without significantly affecting inflammatory cell infiltration or gene expression in bronchoalveolar lavage fluid. These findings identify SRC as a novel and selective mediator of IL-13–driven airway responses and suggest that targeting SRC may offer therapeutic benefit in allergic asthma.

2025-12-05 | PXD066489 | Pride

Quantitative SILAC phosphoproteomics and proteomics of HL60 cells treated with covalent CDK7 inhibitor SY351

Project description:Using the covalent inhibitor SY-351 and quantitative SILAC phosphoproteomics, we identified CDK7 kinase substrates in human cells. We performed a double-label SILAC phosphoproteomics experiment, in which we metabolically labeled HL60 cells with light labeled (Lys0, Arg0) or heavy labeled (Lys8, Arg8) amino acids, which were treated with vehicle (DMSO) or 50 nM SY-351, followed by phosphopeptide enrichment and mass spectrometry analysis. The experimental design included two biological replicates of SY-351 treated heavy cells compared with DMSO treated light cells, a label-flip biological replicate of SY-351 light cells compared with DMSO treated heavy cells, and a null condition for which both heavy and light were treated with DMSO. The label-flip and null conditions control for systematic errors in phosphopeptide Heavy:Light SILAC ratios that are independent of the SY-351 treatment effect. We used a linear statistical model to capture these systematic errors, which improved our statistical power to detect phosphorylation sites that changed in abundance with SY-351 treatment.

2020-06-10 | MSV000085575 | MassIVE

Gene Expression Effects of IL-13 on Primary Human Airway Epithelial Cells

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2012-12-04 | E-GEOD-37693 | biostudies-arrayexpress

Phosphoproteomics identifies microglial Siglec-F inflammatory response during neurodegeneration

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Quantitative phosphoproteomics of proteasome inhibition in multiple myeloma cells.

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H89 Phosphoproteomics in PKA-Null Cells

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Next Generation Sequencing Facilitates Quantitative Analysis of Yeast Cells Treated with and without Proanthocyanidins

Project description:Next Generation Sequencing Facilitates Quantitative Analysis of Yeast Cells Treated with and without Proanthocyanidins

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M2 cytokines alter the miRNA expression profile in macrophages

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2014-07-12 | E-GEOD-59348 | biostudies-arrayexpress

In-depth analysis of the phosphoprotein landscape of cytotoxic T lymphocytes and its regulation by cytokines

Project description:Here we present high-resolution mass spectrometry analysis of changes to the phosphoproteome of cytotoxic T lymphocytes (CTL) induced by the cytokine, Interleukin 12 (IL-12). We treated CTL with a short and long IL-12 stimulation and mapped the changes to the phosphoproteome using quantitative SILAC-based phosphoproteomics.

2016-08-24 | PXD004644 | Pride

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