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Open Access Green as soon as Postprint is submitted to ZB.
Selective enrichment of newly synthesized proteins for quantitative secretome analysis.
Nat. Biotechnol. 30, 984-990 (2012)
Secreted proteins constitute a large and biologically important subset of proteins that are involved in cellular communication, adhesion and migration. Yet secretomes are understudied because of technical limitations in the detection of low-abundance proteins against a background of serum-containing media. Here we introduce a method that combines click chemistry and pulsed stable isotope labeling with amino acids in cell culture to selectively enrich and quantify secreted proteins. The combination of these two labeling approaches allows cells to be studied irrespective of the complexity of the background proteins. We provide an in-depth and differential secretome analysis of various cell lines and primary cells, quantifying secreted factors, including cytokines, chemokines and growth factors. In addition, we reveal that serum starvation has a marked effect on secretome composition. We also analyze the kinetics of protein secretion by macrophages in response to lipopolysaccharides.
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Publication type
Article: Journal article
Document type
Scientific Article
Language
english
Publication Year
2012
HGF-reported in Year
0
ISSN (print) / ISBN
1087-0156
e-ISSN
1546-1696
Journal
Nature Biotechnology
Quellenangaben
Volume: 30,
Issue: 10,
Pages: 984-990
Publisher
Nature Publishing Group
Publishing Place
New York, NY
Reviewing status
Peer reviewed
Institute(s)
Institute of Diabetes and Cancer (IDC)
PubMed ID
23000932
DOI
10.1038/nbt.2356
Erfassungsdatum
2012-12-31