Differential ultracentrifugation enables deep plasma proteomics through enrichment of extracellular vesicles

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

Standard

Differential ultracentrifugation enables deep plasma proteomics through enrichment of extracellular vesicles. / Kverneland, Anders H.; Østergaard, Ole; Emdal, Kristina Bennet; Svane, Inge Marie; Olsen, Jesper Velgaard.

In: Proteomics, Vol. 23, No. 7-8, 2200039, 2023.

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

Harvard

Kverneland, AH, Østergaard, O, Emdal, KB, Svane, IM & Olsen, JV 2023, 'Differential ultracentrifugation enables deep plasma proteomics through enrichment of extracellular vesicles', Proteomics, vol. 23, no. 7-8, 2200039. https://doi.org/10.1002/pmic.202200039

APA

Kverneland, A. H., Østergaard, O., Emdal, K. B., Svane, I. M., & Olsen, J. V. (2023). Differential ultracentrifugation enables deep plasma proteomics through enrichment of extracellular vesicles. Proteomics, 23(7-8), [2200039]. https://doi.org/10.1002/pmic.202200039

Vancouver

Kverneland AH, Østergaard O, Emdal KB, Svane IM, Olsen JV. Differential ultracentrifugation enables deep plasma proteomics through enrichment of extracellular vesicles. Proteomics. 2023;23(7-8). 2200039. https://doi.org/10.1002/pmic.202200039

Author

Kverneland, Anders H. ; Østergaard, Ole ; Emdal, Kristina Bennet ; Svane, Inge Marie ; Olsen, Jesper Velgaard. / Differential ultracentrifugation enables deep plasma proteomics through enrichment of extracellular vesicles. In: Proteomics. 2023 ; Vol. 23, No. 7-8.

Bibtex

@article{ed4acdb24d2c458ab422ac451af52212,
title = "Differential ultracentrifugation enables deep plasma proteomics through enrichment of extracellular vesicles",
abstract = "Human plasma is a rich source of biomedical information and biomarkers. However, the enormous dynamic range of plasma proteins limits its accessibility to mass spectrometric (MS) analysis. Here, we show that enrichment of extracellular vesicles (EVs) by ultracentrifugation increases plasma proteome depth by an order of magnitude. With this approach, more than two thousand proteins are routinely and reproducibly quantified by label-free quantification and data independent acquisition (DIA) in single-shot liquid chromatography tandem mass spectrometry runs of less than one hour. We present an optimized plasma proteomics workflow that enables high-throughput with very short chromatographic gradients analyzing hundred samples per day with deep proteome coverage, especially when including a study-specific spectral library generated by repeated injection and gas-phase fractionation of pooled samples. Finally, we test the workflow on clinical biobank samples from malignant melanoma patients in immunotherapy to demonstrate the improved proteome coverage supporting the potential for future biomarker discovery.",
author = "Kverneland, {Anders H.} and Ole {\O}stergaard and Emdal, {Kristina Bennet} and Svane, {Inge Marie} and Olsen, {Jesper Velgaard}",
year = "2023",
doi = "10.1002/pmic.202200039",
language = "English",
volume = "23",
journal = "Proteomics",
issn = "1615-9853",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "7-8",

}

RIS

TY - JOUR

T1 - Differential ultracentrifugation enables deep plasma proteomics through enrichment of extracellular vesicles

AU - Kverneland, Anders H.

AU - Østergaard, Ole

AU - Emdal, Kristina Bennet

AU - Svane, Inge Marie

AU - Olsen, Jesper Velgaard

PY - 2023

Y1 - 2023

N2 - Human plasma is a rich source of biomedical information and biomarkers. However, the enormous dynamic range of plasma proteins limits its accessibility to mass spectrometric (MS) analysis. Here, we show that enrichment of extracellular vesicles (EVs) by ultracentrifugation increases plasma proteome depth by an order of magnitude. With this approach, more than two thousand proteins are routinely and reproducibly quantified by label-free quantification and data independent acquisition (DIA) in single-shot liquid chromatography tandem mass spectrometry runs of less than one hour. We present an optimized plasma proteomics workflow that enables high-throughput with very short chromatographic gradients analyzing hundred samples per day with deep proteome coverage, especially when including a study-specific spectral library generated by repeated injection and gas-phase fractionation of pooled samples. Finally, we test the workflow on clinical biobank samples from malignant melanoma patients in immunotherapy to demonstrate the improved proteome coverage supporting the potential for future biomarker discovery.

AB - Human plasma is a rich source of biomedical information and biomarkers. However, the enormous dynamic range of plasma proteins limits its accessibility to mass spectrometric (MS) analysis. Here, we show that enrichment of extracellular vesicles (EVs) by ultracentrifugation increases plasma proteome depth by an order of magnitude. With this approach, more than two thousand proteins are routinely and reproducibly quantified by label-free quantification and data independent acquisition (DIA) in single-shot liquid chromatography tandem mass spectrometry runs of less than one hour. We present an optimized plasma proteomics workflow that enables high-throughput with very short chromatographic gradients analyzing hundred samples per day with deep proteome coverage, especially when including a study-specific spectral library generated by repeated injection and gas-phase fractionation of pooled samples. Finally, we test the workflow on clinical biobank samples from malignant melanoma patients in immunotherapy to demonstrate the improved proteome coverage supporting the potential for future biomarker discovery.

U2 - 10.1002/pmic.202200039

DO - 10.1002/pmic.202200039

M3 - Journal article

C2 - 36398564

VL - 23

JO - Proteomics

JF - Proteomics

SN - 1615-9853

IS - 7-8

M1 - 2200039

ER -

ID: 327171858