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Langlais"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Mitochondria","Cc16","Asthma"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067703"],"tissue":["Lung Cell Line"],"sample_protocol":["100 ug of protein was subjected to acetone precipitation by adding six times the sample volume of pre-chilled 100 % acetone and incubated one hour at -20° C. The precipitates were centrifuged at 16,000 x g for 10 minutes at 4°C and the acetone was removed. 400 uL of pre-chilled 90% acetone was added to the protein pellet, briefly vortexed and centrifuged at 16,000 x g for 5 minutes at 4°C. The remaining acetone was removed, the protein pellets were air dried for 3 minutes, resuspended in 100 uL of 50 mM NH4HCO3 and sonicated for 5 minutes. The samples were supplemented with dithiothreitol (DTT) at a final concentration of 5 mM and incubated at 70° C for 30 minutes. Samples were cooled to room temperature for 10 minutes and incubated with 15 mM acrylamide for 30 minutes at room temperature while protected from light. The reaction was quenched with DTT with a final concentration of 5 mM and incubated in the dark for 15 minutes.  One ug of Lys-C was added to each sample and incubated at 37° C for 2-3 hours while shaking at 300 rpm followed by the addition of 50 uL of 50mM ammonium bicarbonate and 2 ug of trypsin and incubation overnight at 37° C while shaking at 300 rpm. 14.7 uL of 40% FA/1% HFBA was added to each sample and incubated for 10 minutes (final concentration is 4% FA/0.1% HFBA) to stop trypsin digestion. The samples were desalted with Pierce Peptide Desalting Spin Columns per the manufacturer’s protocol (ThermoFisher Scientific, cat no. 89852) and the peptides were dried by vacuum centrifugation. The dried peptides were resuspended in 20 uL of 0.1% FA (v/v) and the peptide concentration was determined with the Pierce Quantitative Colorimetric Peptide Assay Kit per the manufacturer’s protocol (ThermoFisher Scientific, cat no. 23275). 350 ng of the final sample was analyzed by mass spectrometry."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Progenesis QI for proteomics software (version 2.4, Nonlinear Dynamics Ltd., Newcastle upon Tyne, UK) was used to perform ion-intensity based label-free quantification. In an automated format, raw files were imported and converted into two-dimensional maps (y-axis = time, x-axis =m/z) followed by selection of a reference run for alignment purposes. An aggregate data set containing all peak information from all samples was created from the aligned runs, which was then further narrowed down by selecting only +2, +3, and +4 charged ions for further analysis. The samples were then grouped according to experimental design. Peak lists of fragment ion spectra were exported in Mascot generic file (.mgf) format and searched against the Swissprot Mus musculus database (17097 entries) using Mascot (Matrix Science, London, UK; version 2.8). The search variables that were used were: 10 ppm mass tolerance for precursor ion masses and 0.5 Da for product ion masses; digestion with trypsin; a maximum of two missed tryptic cleavages; variable modifications of oxidation of methionine and phosphorylation of serine, threonine, and tyrosine; 13C=1. The resulting Mascot .xml file was then imported into Progenesis, allowing for peptide/protein assignment, while peptides with a Mascot Ion Score of <25 were not considered for further analysis. Precursor ion-abundance values for peptide ions were normalized to all proteins. For quantification, proteins must have possessed at least one or more unique, identifying peptide. Principle component analysis and unbiased hierarchical clustering (heat map) was performed in Perseus and volcano plots were generated in GraphPad Prism 8.0 (Graph Pad Inc.; San Diego, CA). Significant apically secreted proteins from WT and CC16-/- MTECs were exported from Progenesis for further analysis. Using multiple cohorts, apically secreted proteins whose expression reproduced in all cohorts based on highest mean condition and significance were used for further analysis. Significantly secreted proteins (p<0.05) were used as input into the Database for Annotation, Visualization and Integrated Discovery (DAVID) 38 to identify enriched biological themes through use of Gene Onotology (GO), as well as visualization of biological pathways using KEGG pathway maps (https://david.ncifcrf.gov/)."],"omics_type":["Proteomics"],"labhead":["Julie Ledford"],"instrument_platform":[""],"labhead_affiliation":["Professor Cellular and Molecular Medicine Department University of Arizona College of Medicine - Tucson"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)","Mus Musculus (mouse)"],"submitter_mail":["langlais@deptofmed.arizona.edu"],"publication":["42154955 Berthiaume Fox KA, Iannuzo N, Li J, Rojas-Quintero J, Kimura H, Santiago Raj PV, Schnellmann RG, Johnson MDL, Polverino F, Langlais PR, Kraft M, Park JA, Ledford JG. Mechanical compression reduces CC16 expression and disrupts metabolic homeostasis in airway epithelial cells. Am J Respir Cell Mol Biol. 2026:aanag077 10.1093/ajrcmb/aanag077"],"submitter_affiliation":["University of Arizona"],"submitter_country":["United States"],"doi":["10.6019/PXD067703"],"pubmed_abstract":["Recent evidence suggests that bronchial epithelial cells from individuals with asthma exhibit altered metabolic signatures. This metabolic shift of energetically demanding cells leads to increased inflammation, excessive reactive oxygen species production (ROS), and oxidative stress-all hallmarks of mitochondrial dysfunction. While mitochondrial dysfunction has been implicated in disruption in epithelial cell function in asthma, the mechanistic link between bronchoconstriction observed in asthma and these metabolic alterations remains poorly defined. Club cell secretory protein (CC16) is the most abundant protein found in the lung and exerts key anti-inflammatory and antioxidant functions contributing to protection against airway remodeling. Decreased levels of CC16 in both serum and bronchial alveolar lavage fluid (BALF) are characteristic of asthma and worsening respiratory disease. Using a well-established transmembrane compression system to model bronchoconstriction coupled with mass spectrometry and quantitative proteomics, we investigated how modeling bronchoconstriction in airway cells impacts CC16 expression and cell metabolic pathway changes over time. Using naive mouse tracheal epithelial cells (MTECs) and normal human bronchial epithelial cells (HBECs), we observed that recombinant (r)CC16 induces the expression of proteins related to various metabolic pathways, such as glycolysis, gluconeogenesis, and the pentose phosphate pathway and that compression of airway cells results in acute decreases in CC16 expression, as well as decreases in metabolic processes. MTECs deficient in CC16 (CC16-/-) had lower mitochondrial oxygen consumption rate (OCR) compared to WT cells. Exogenous addition of rCC16 significantly increased OCR of both WT and CC16 deficient MTECs. Our findings suggest a novel role for CC16 in mediating airway epithelial cell metabolic processes, which could be decreased by bronchoconstrictive events in human asthma. The mass spectrometry proteomics data are available via ProteomeXchange with identifier PXD067703."],"pubmed_title":["Mechanical compression reduces CC16 expression and disrupts metabolic homeostasis in airway epithelial cells."],"pubmed_authors":["Berthiaume Fox Kayleigh A KA, Iannuzo Natalie N, Li Julia J, Rojas-Quintero Joselyn J, Kimura Hiroki H, Santiago Raj Paul Victor PV, Schnellmann Rick G RG, Johnson Michael D L MDL, Polverino Francesca F, Langlais Paul R PR, Kraft Monica M, Park Jin-Ah JA, Ledford Julie G JG"],"additional_accession":[]},"is_claimable":false,"name":"Mechanical compression reduces CC16 expression and disrupts metabolic homeostasis in airway epithelial cells","description":"Recent evidence suggests that bronchial epithelial cells from asthmatic patients exhibit altered metabolic signatures. This metabolic shift of energetically demanding cells leads to increased inflammation, excessive reactive oxygen species production (ROS), and oxidative stress—all hallmarks of mitochondrial dysfunction. While mitochondrial dysfunction has been implicated in asthmatic epithelial cells, the mechanistic link between bronchoconstriction and these metabolic alterations remains poorly defined. Club cell secretory protein (CC16) is the most abundant protein found in the lung and exerts key anti-inflammatory and antioxidant functions, culminating in protection against airway remodeling. Decreased levels of CC16 are characteristic of asthma and worsening respiratory disease. Using a well-established transmembrane compression system to model bronchoconstriction coupled with mass spectrometry and quantitative proteomics, we investigated how modeling bronchoconstriction in airway cells impacts CC16 expression and cell metabolic pathway changes over time. Additionally, using rCC16, we examined the direct impact on airway cell metabolism. Using naïve mouse tracheal epithelial cells (MTECs) and normal human bronchial epithelial cells (HBECs), we observed that rCC16 induces the expression of proteins related to various metabolic pathways, such as glycolysis, gluconeogenesis, and the pentose phosphate pathway and that compression of airway cells results in acute decreases in CC16 expression, as well as decreases in metabolic processes. MTECs deficient in CC16 (CC16-/-) had lower mitochondrial oxygen consumption rate (OCR) compared to WT cells, both of which could be increased by exogenous addition of rCC16. Our findings suggest a novel role for CC16 in mediating airway epithelial cell metabolic processes, which could be decreased by bronchoconstrictive events in asthma 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