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Eichelbaum, K.* ; Winter, M.* ; Berriel Diaz, M.* ; Herzig, S.* ; Krijgsveld, J.*

Selective enrichment of newly synthesized proteins for quantitative secretome analysis.

Nat. Biotechnol. 30, 984-990 (2012)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Sprache englisch
Veröffentlichungsjahr 2012
HGF-Berichtsjahr 0
ISSN (print) / ISBN 1087-0156
e-ISSN 1546-1696
Zeitschrift Nature Biotechnology
Quellenangaben Band: 30, Heft: 10, Seiten: 984-990 Artikelnummer: , Supplement: ,
Verlag Nature Publishing Group
Verlagsort New York, NY
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Diabetes and Cancer (IDC)
PubMed ID 23000932
DOI 10.1038/nbt.2356
Erfassungsdatum 2012-12-31
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