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@article{Burg:2018:10.1021/acs.jproteome.8b00018,
author = {Burg, D and Schofield, JPR and Brandsma, J and Staykova, D and Folisi, C and Bansal, A and Nicholas, B and Xian, Y and Rowe, A and Corfield, J and Wilson, S and Ward, J and Lutter, R and Fleming, L and Shaw, DE and Bakke, PS and Caruso, M and Dahlen, S-E and Fowler, SJ and Hashimoto, S and Horváth, I and Howarth, P and Krug, N and Montuschi, P and Sanak, M and Sandström, T and Singer, F and Sun, K and Pandis, I and Auffray, C and Sousa, AR and Adcock, IM and Chung, KF and Sterk, PJ and Djukanovi, R and Skipp, PJ and The, U-Biopred Study Group},
doi = {10.1021/acs.jproteome.8b00018},
journal = {Journal of Proteome Research},
pages = {2072--2091},
title = {Large-scale label-free quantitative mapping of the sputum proteome},
url = {http://dx.doi.org/10.1021/acs.jproteome.8b00018},
volume = {17},
year = {2018}
}

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TY  - JOUR
AB  - Analysis of induced sputum supernatant is a minimally invasive approach to study the epithelial lining fluid and, thereby, provide insight into normal lung biology and the pathobiology of lung diseases. We present here a novel proteomics approach to sputum analysis developed within the U-BIOPRED (unbiased biomarkers predictive of respiratory disease outcomes) international project. We present practical and analytical techniques to optimize the detection of robust biomarkers in proteomic studies. The normal sputum proteome was derived using data-independent HDMSE applied to 40 healthy nonsmoking participants, which provides an essential baseline from which to compare modulation of protein expression in respiratory diseases. The "core" sputum proteome (proteins detected in ≥40% of participants) was composed of 284 proteins, and the extended proteome (proteins detected in ≥3 participants) contained 1666 proteins. Quality control procedures were developed to optimize the accuracy and consistency of measurement of sputum proteins and analyze the distribution of sputum proteins in the healthy population. The analysis showed that quantitation of proteins by HDMSE is influenced by several factors, with some proteins being measured in all participants' samples and with low measurement variance between samples from the same patient. The measurement of some proteins is highly variable between repeat analyses, susceptible to sample processing effects, or difficult to accurately quantify by mass spectrometry. Other proteins show high interindividual variance. We also highlight that the sputum proteome of healthy individuals is related to sputum neutrophil levels, but not gender or allergic sensitization. We illustrate the importance of design and interpretation of disease biomarker studies considering such protein population and technical measurement variance.
AU  - Burg,D
AU  - Schofield,JPR
AU  - Brandsma,J
AU  - Staykova,D
AU  - Folisi,C
AU  - Bansal,A
AU  - Nicholas,B
AU  - Xian,Y
AU  - Rowe,A
AU  - Corfield,J
AU  - Wilson,S
AU  - Ward,J
AU  - Lutter,R
AU  - Fleming,L
AU  - Shaw,DE
AU  - Bakke,PS
AU  - Caruso,M
AU  - Dahlen,S-E
AU  - Fowler,SJ
AU  - Hashimoto,S
AU  - Horváth,I
AU  - Howarth,P
AU  - Krug,N
AU  - Montuschi,P
AU  - Sanak,M
AU  - Sandström,T
AU  - Singer,F
AU  - Sun,K
AU  - Pandis,I
AU  - Auffray,C
AU  - Sousa,AR
AU  - Adcock,IM
AU  - Chung,KF
AU  - Sterk,PJ
AU  - Djukanovi,R
AU  - Skipp,PJ
AU  - The,U-Biopred Study Group
DO  - 10.1021/acs.jproteome.8b00018
EP  - 2091
PY  - 2018///
SN  - 1535-3893
SP  - 2072
TI  - Large-scale label-free quantitative mapping of the sputum proteome
T2  - Journal of Proteome Research
UR  - http://dx.doi.org/10.1021/acs.jproteome.8b00018
UR  - https://www.ncbi.nlm.nih.gov/pubmed/29737851
UR  - http://hdl.handle.net/10044/1/60217
VL  - 17
ER  -

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