<HashMap><database>iProX</database><scores/><additional><omics_type>Proteomics</omics_type><submitter>Rong Zeng</submitter><species>Mus Musculus</species><full_dataset_link>http://www.iprox.org/page/project.html?id=IPX0012673000</full_dataset_link><submitter_email>zengrong@shanghaitech.edu.cn</submitter_email><submitter_affiliation>University of Shanghaitech</submitter_affiliation><sample_protocol></sample_protocol><repository>iProX</repository><data_protocol></data_protocol></additional><is_claimable>false</is_claimable><name>ILC2-intrinsic IL-33 promotes ILC2 activation and exacerbates allergic lung 1  inflammation</name><description>Mass spectrometry-based proteomics serves as an invaluable tool for pinpointing critical biomarkers and elucidating cellular functions and regulatory pathways. However, the proteomic changes in ILC2s during activation remain unexplored. To characterize the dynamic proteomic profiles of lung-resident ILC2s under physiological and inflammatory conditions, we performed high-resolution liquid chromatography-tandem mass spectrometry (LC-MS/MS) to systematically compare the molecular signatures of FACS-purified pulmonary ILC2 populations (Live CD45+CD90.2+Lineage- ST2+) isolated from two experimental groups: 1) steady-state control mice and 2) papain-challenged mice exhibiting acute airway inflammation (Fig. 1a and Supplementary Fig. 1a). Papain-induced lung inflammation was chosen because papain is a classical protease allergen triggering the release of pro-inflammatory factors including IL-33 to develop ILC2-derived lung inflammation.</description><dates><publication>Sat May 16 00:00:00 GMT+01:00 2026</publication></dates><accession>PXD078462</accession><cross_references><TAXONOMY>10090</TAXONOMY></cross_references></HashMap>