Journal article
Proteomic analysis of pure human airway gland mucus reveals a large component of protective proteins
PloS one, Vol.10(2), pp.e0116756-e0116756
2015
DOI: 10.1371/journal.pone.0116756
PMCID: PMC4338240
PMID: 25706550
Abstract
Airway submucosal glands contribute to innate immunity and protect the lungs by secreting mucus, which is required for mucociliary clearance and which also contains antimicrobial, anti-inflammatory, anti-proteolytic and anti-oxidant proteins. We stimulated glands in tracheal trimmings from three lung donors and collected droplets of uncontaminated mucus as they formed at the gland orifices under an oil layer. We analyzed the mucus using liquid chromatography-tandem mass spectrometry (LC-MS/MS). Analysis identified 5486 peptides and 441 proteins from across the 3 samples (269-319 proteins per subject). We focused on 269 proteins common to at least 2 0f 3 subjects, of which 102 (38%) had protective or innate immunity functions. While many of these have long been known to play such roles, for many others their cellular protective functions have only recently been appreciated in addition to their well-studied biologic functions (e.g. annexins, apolipoproteins, gelsolin, hemoglobin, histones, keratins, and lumican). A minority of the identified proteins are known to be secreted via conventional exocytosis, suggesting that glandular secretion occurs via multiple mechanisms. Two of the observed protective proteins, major vault protein and prohibitin, have not been observed in fluid from human epithelial cultures or in fluid from nasal or bronchoalveolar lavage. Further proteomic analysis of pure gland mucus may help clarify how healthy airways maintain a sterile environment.
Details
- Title: Subtitle
- Proteomic analysis of pure human airway gland mucus reveals a large component of protective proteins
- Creators
- Nam Soo Joo - The Cystic Fibrosis Research Laboratory, Stanford University, Stanford, CA, 94305, United States of AmericaIdil Apak T Evans - Department of Anatomy and Cell Biology, Carver College of Medicine, University of Iowa, Iowa City, IA, 52242, United States of AmericaHyung-Ju Cho - The Cystic Fibrosis Research Laboratory, Stanford University, Stanford, CA, 94305, United States of AmericaIl-Ho Park - The Cystic Fibrosis Research Laboratory, Stanford University, Stanford, CA, 94305, United States of AmericaJohn F Engelhardt - Department of Anatomy and Cell Biology, Carver College of Medicine, University of Iowa, Iowa City, IA, 52242, United States of AmericaJeffrey J Wine - The Cystic Fibrosis Research Laboratory, Stanford University, Stanford, CA, 94305, United States of America
- Resource Type
- Journal article
- Publication Details
- PloS one, Vol.10(2), pp.e0116756-e0116756
- DOI
- 10.1371/journal.pone.0116756
- PMID
- 25706550
- PMCID
- PMC4338240
- NLM abbreviation
- PLoS One
- ISSN
- 1932-6203
- eISSN
- 1932-6203
- Publisher
- Public Library of Science; United States
- Grant note
- R01 HL108902 / NHLBI NIH HHS P30 ES005605 / NIEHS NIH HHS DK047967 / NIDDK NIH HHS HL108902 / NHLBI NIH HHS R37 DK047967 / NIDDK NIH HHS DK054759 / NIDDK NIH HHS R01 DK047967 / NIDDK NIH HHS P30 DK054759 / NIDDK NIH HHS
- Language
- English
- Date published
- 2015
- Academic Unit
- Roy J. Carver Department of Biomedical Engineering; Anatomy and Cell Biology; Radiation Oncology; Internal Medicine
- Record Identifier
- 9984025368702771
Metrics
35 Record Views