High-resolution mass spectrometric analysis of the secretome from mouse lung endothelial progenitor
cells
Katherina Hemmen1*, Tobias Reinl2*, Kerstin Buttler3, Friederike Behler1, Hauke Dieken1, Lothar Jaensch2, Jörg
Wilting3, Herbert A. Weich1
1
Dept. Gene Regulation and 2Proteome Research Group, Helmholtz Centre for Infection Research,
Braunschweig; Germany; 3Dept. Anatomy and Cell Biology, Georg-August-University, Goettingen, Germany.
Corresponding Author: H.A.W. (herbert.weich@helmholtz-hzi.de)
Supplement Caption
Supplement 1: Secretome specific proteins from mouse lung endothelial progenitor cells
HPLC-MS/MS analysis was used to identify secretome specific proteins from mouse lung endothelial progenitor
cells. Proteins from equal volumes of either cell culture supernatant (secretome proteins) or fresh cell culture
medium (background proteins) were precipitated, digested and identified separately using an Acquity UPLC
system connected to an LTQ-Orbitrap Velos mass spectrometer. Proteins that were available in fresh cell culture
medium were not considered as secretome specific proteins and subtracted. Finally, we identified 523 proteins
that were exclusively abundant in the secretome samples (background corrected list). Protein Score, number of
unique peptides and sequence coverage were calculated as mean from four HPLC-MS/MS analyses and the
respective standard deviation is indicated.
Supplement 2: Secretome specific secreted proteins and membrane proteins from mouse lung endothelial
precursor cells
Using Gene Ontology (GO) terms we extracted all secretome specific proteins from Supplement 1 that are
described as secreted proteins and/or membrane localized proteins. In total, 133 proteins from our set of 523
secretome specific proteins matched these criteria.