Proteomic profiling of paired human liver homogenate and tissue derived extracellular vesicles
Date
2023
Authors
Useckaite, Z.
Newman, L.A.
Hopkins, A.M.
Klebe, S.
Colella, A.D.
Chegeni, N.
Williams, R.
Sorich, M.J.
Rodrigues, A.D.
Chataway, T.K.
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Journal article
Citation
Proteomics, 2023; 24(11):1-13
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Abstract
Advances in technologies to isolate extracellular vesicles (EVs) and detect/quantify their cargo underpin the novel potential of these circulating particles as a liquid biopsy to understand physiology and disease. One organ of particular interest in terms of utilizing EVs as a liquid biopsy is the liver. The extent to which EVs originating from the liver reflect the functional status of this organ remains unknown. This is an important knowledge gap that underpins the utility of circulating liver derived EVs as a liquid biopsy. The primary objective of this study was to characterize the proteomic profile of EVs isolated from the extracellular space of liver tissue (LEV) and compare this profile to that of paired tissue (LH).
LCMS analyses detected 2892 proteins in LEV and 2673 in LH. Of the 2673 proteins detected in LH, 1547 (58%) were also detected in LEV. Bioinformatic analyses demonstrated comparable representation of proteins in terms of biological functions and cellular compartments. Although, enriched representation of membrane proteins and associated functions was observed in LEV, while representation of nuclear proteins and associated functions was depleted in LEV. These data support the potential use of circulating liver derived EVs as a liquid biopsy for this organ
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Data source: Supporting information, https://doi.org/10.1002/pmic.202300025
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Copyright 2023 The Author(s). This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made. (https://creativecommons.org/licenses/by-nc-nd/4.0/)
Access Condition Notes: Open access publishing facilitated by Flinders University, as part of the Wiley - Flinders University agreement via the Council of Australian University Librarians.