Multidimensional analysis of protease substrates and their cellular origins in mixed secretomes from multiple cell types

Research output: Chapter in Book/Report/Conference proceedingBook chapter – Annual report year: 2017Researchpeer-review

Without internal affiliation

Standard

Multidimensional analysis of protease substrates and their cellular origins in mixed secretomes from multiple cell types. / Schlage, Pascal; auf dem Keller, Ulrich.

Protein Terminal Profiling . Vol. 1574 Humana Press, 2017. p. 91-104 (Methods in Molecular Biology, Vol. 1574).

Research output: Chapter in Book/Report/Conference proceedingBook chapter – Annual report year: 2017Researchpeer-review

Harvard

Schlage, P & auf dem Keller, U 2017, Multidimensional analysis of protease substrates and their cellular origins in mixed secretomes from multiple cell types. in Protein Terminal Profiling . vol. 1574, Humana Press, Methods in Molecular Biology, vol. 1574, pp. 91-104. https://doi.org/10.1007/978-1-4939-6850-3_7

APA

Schlage, P., & auf dem Keller, U. (2017). Multidimensional analysis of protease substrates and their cellular origins in mixed secretomes from multiple cell types. In Protein Terminal Profiling (Vol. 1574, pp. 91-104). Humana Press. Methods in Molecular Biology, Vol.. 1574 https://doi.org/10.1007/978-1-4939-6850-3_7

CBE

MLA

Schlage, Pascal and Ulrich auf dem Keller "Multidimensional analysis of protease substrates and their cellular origins in mixed secretomes from multiple cell types". Protein Terminal Profiling . Chapter 7, Humana Press. (Methods in Molecular Biology, Vol. 1574). 2017, 91-104. https://doi.org/10.1007/978-1-4939-6850-3_7

Vancouver

Schlage P, auf dem Keller U. Multidimensional analysis of protease substrates and their cellular origins in mixed secretomes from multiple cell types. In Protein Terminal Profiling . Vol. 1574. Humana Press. 2017. p. 91-104. (Methods in Molecular Biology, Vol. 1574). https://doi.org/10.1007/978-1-4939-6850-3_7

Author

Schlage, Pascal ; auf dem Keller, Ulrich. / Multidimensional analysis of protease substrates and their cellular origins in mixed secretomes from multiple cell types. Protein Terminal Profiling . Vol. 1574 Humana Press, 2017. pp. 91-104 (Methods in Molecular Biology, Vol. 1574).

Bibtex

@inbook{7a17f6312d1142198d226a99f69e6841,
title = "Multidimensional analysis of protease substrates and their cellular origins in mixed secretomes from multiple cell types",
abstract = "Although extracellular proteases are confronted with substrate proteins expressed by multiple cell types in vivo, in most protease substrate discovery approaches, the test protease is exposed to a test proteome (secretome) derived only from a single cell type. This limits the potential substrate space and prohibits the formation of protein complexes constituted of components derived from multiple cellular origins. Mixing of secretomes collected from multiple cell types addresses this issue, but information on the cellular origin of a substrate protein is lost. Here, we describe a protocol and the corresponding data analysis workflow for a multidimensional substrate discovery approach termed SILAC-iTRAQ-TAILS that is based on hyperplexed terminal amine isotopic labeling of substrates (TAILS), allowing identification of substrates and concomitant assignment to cellular origins in mixed secretomes within the same experiment.",
keywords = "iTRAQ, Protease substrate, Secretome, SILAC, TAILS",
author = "Pascal Schlage and {auf dem Keller}, Ulrich",
year = "2017",
doi = "10.1007/978-1-4939-6850-3_7",
language = "English",
isbn = "978-1-4939-6849-7",
volume = "1574",
pages = "91--104",
booktitle = "Protein Terminal Profiling",
publisher = "Humana Press",
address = "United States",

}

RIS

TY - CHAP

T1 - Multidimensional analysis of protease substrates and their cellular origins in mixed secretomes from multiple cell types

AU - Schlage, Pascal

AU - auf dem Keller, Ulrich

PY - 2017

Y1 - 2017

N2 - Although extracellular proteases are confronted with substrate proteins expressed by multiple cell types in vivo, in most protease substrate discovery approaches, the test protease is exposed to a test proteome (secretome) derived only from a single cell type. This limits the potential substrate space and prohibits the formation of protein complexes constituted of components derived from multiple cellular origins. Mixing of secretomes collected from multiple cell types addresses this issue, but information on the cellular origin of a substrate protein is lost. Here, we describe a protocol and the corresponding data analysis workflow for a multidimensional substrate discovery approach termed SILAC-iTRAQ-TAILS that is based on hyperplexed terminal amine isotopic labeling of substrates (TAILS), allowing identification of substrates and concomitant assignment to cellular origins in mixed secretomes within the same experiment.

AB - Although extracellular proteases are confronted with substrate proteins expressed by multiple cell types in vivo, in most protease substrate discovery approaches, the test protease is exposed to a test proteome (secretome) derived only from a single cell type. This limits the potential substrate space and prohibits the formation of protein complexes constituted of components derived from multiple cellular origins. Mixing of secretomes collected from multiple cell types addresses this issue, but information on the cellular origin of a substrate protein is lost. Here, we describe a protocol and the corresponding data analysis workflow for a multidimensional substrate discovery approach termed SILAC-iTRAQ-TAILS that is based on hyperplexed terminal amine isotopic labeling of substrates (TAILS), allowing identification of substrates and concomitant assignment to cellular origins in mixed secretomes within the same experiment.

KW - iTRAQ

KW - Protease substrate

KW - Secretome

KW - SILAC

KW - TAILS

U2 - 10.1007/978-1-4939-6850-3_7

DO - 10.1007/978-1-4939-6850-3_7

M3 - Book chapter

SN - 978-1-4939-6849-7

VL - 1574

SP - 91

EP - 104

BT - Protein Terminal Profiling

PB - Humana Press

ER -