Direct proteomic quantification of the secretome of activated immune cells

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Direct proteomic quantification of the secretome of activated immune cells. / Meissner, Felix; Scheltema, Richard A; Mollenkopf, Hans-Joachim; Mann, Matthias.

In: Science (New York, N.Y.), Vol. 340, No. 6131, 26.04.2013, p. 475-8.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Meissner, F, Scheltema, RA, Mollenkopf, H-J & Mann, M 2013, 'Direct proteomic quantification of the secretome of activated immune cells', Science (New York, N.Y.), vol. 340, no. 6131, pp. 475-8. https://doi.org/10.1126/science.1232578

APA

Meissner, F., Scheltema, R. A., Mollenkopf, H-J., & Mann, M. (2013). Direct proteomic quantification of the secretome of activated immune cells. Science (New York, N.Y.), 340(6131), 475-8. https://doi.org/10.1126/science.1232578

Vancouver

Meissner F, Scheltema RA, Mollenkopf H-J, Mann M. Direct proteomic quantification of the secretome of activated immune cells. Science (New York, N.Y.). 2013 Apr 26;340(6131):475-8. https://doi.org/10.1126/science.1232578

Author

Meissner, Felix ; Scheltema, Richard A ; Mollenkopf, Hans-Joachim ; Mann, Matthias. / Direct proteomic quantification of the secretome of activated immune cells. In: Science (New York, N.Y.). 2013 ; Vol. 340, No. 6131. pp. 475-8.

Bibtex

@article{d0e9d1b2063c40e991823707017e2b67,
title = "Direct proteomic quantification of the secretome of activated immune cells",
abstract = "Protein secretion allows communication of distant cells in an organism and controls a broad range of physiological functions. We describe a quantitative, high-resolution mass spectrometric workflow to detect and quantify proteins that are released from immune cells upon receptor ligation. We quantified the time-resolved release of 775 proteins, including 52 annotated cytokines from only 150,000 primary Toll-like receptor 4-activated macrophages per condition. Achieving low picogram sensitivity, we detected secreted proteins whose abundance increased by a factor of more than 10,000 upon stimulation. Secretome to transcriptome comparisons revealed the transcriptionally decoupled release of lysosomal proteins. From genetic models, we defined secretory profiles that depended on distinct intracellular signaling adaptors and showed that secretion of many proinflammatory proteins is safeguarded by redundant mechanisms, whereas signaling adaptor synergy promoted the release of anti-inflammatory proteins.",
keywords = "Animals, Lipopolysaccharides, Macrophage Activation, Macrophages, Mass Spectrometry, Mice, Mice, Knockout, Proteins, Proteome, Proteomics, Toll-Like Receptor 4, Transcription, Genetic, Transcriptome",
author = "Felix Meissner and Scheltema, {Richard A} and Hans-Joachim Mollenkopf and Matthias Mann",
year = "2013",
month = apr,
day = "26",
doi = "10.1126/science.1232578",
language = "English",
volume = "340",
pages = "475--8",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "6131",

}

RIS

TY - JOUR

T1 - Direct proteomic quantification of the secretome of activated immune cells

AU - Meissner, Felix

AU - Scheltema, Richard A

AU - Mollenkopf, Hans-Joachim

AU - Mann, Matthias

PY - 2013/4/26

Y1 - 2013/4/26

N2 - Protein secretion allows communication of distant cells in an organism and controls a broad range of physiological functions. We describe a quantitative, high-resolution mass spectrometric workflow to detect and quantify proteins that are released from immune cells upon receptor ligation. We quantified the time-resolved release of 775 proteins, including 52 annotated cytokines from only 150,000 primary Toll-like receptor 4-activated macrophages per condition. Achieving low picogram sensitivity, we detected secreted proteins whose abundance increased by a factor of more than 10,000 upon stimulation. Secretome to transcriptome comparisons revealed the transcriptionally decoupled release of lysosomal proteins. From genetic models, we defined secretory profiles that depended on distinct intracellular signaling adaptors and showed that secretion of many proinflammatory proteins is safeguarded by redundant mechanisms, whereas signaling adaptor synergy promoted the release of anti-inflammatory proteins.

AB - Protein secretion allows communication of distant cells in an organism and controls a broad range of physiological functions. We describe a quantitative, high-resolution mass spectrometric workflow to detect and quantify proteins that are released from immune cells upon receptor ligation. We quantified the time-resolved release of 775 proteins, including 52 annotated cytokines from only 150,000 primary Toll-like receptor 4-activated macrophages per condition. Achieving low picogram sensitivity, we detected secreted proteins whose abundance increased by a factor of more than 10,000 upon stimulation. Secretome to transcriptome comparisons revealed the transcriptionally decoupled release of lysosomal proteins. From genetic models, we defined secretory profiles that depended on distinct intracellular signaling adaptors and showed that secretion of many proinflammatory proteins is safeguarded by redundant mechanisms, whereas signaling adaptor synergy promoted the release of anti-inflammatory proteins.

KW - Animals

KW - Lipopolysaccharides

KW - Macrophage Activation

KW - Macrophages

KW - Mass Spectrometry

KW - Mice

KW - Mice, Knockout

KW - Proteins

KW - Proteome

KW - Proteomics

KW - Toll-Like Receptor 4

KW - Transcription, Genetic

KW - Transcriptome

U2 - 10.1126/science.1232578

DO - 10.1126/science.1232578

M3 - Journal article

C2 - 23620052

VL - 340

SP - 475

EP - 478

JO - Science

JF - Science

SN - 0036-8075

IS - 6131

ER -

ID: 88584908