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Global Proteomics Analysis of Circulating Extracellular Vesicles Isolated from Lung Transplant Recipients

[Image: see text] Lung transplant recipients (LTxRs) with acute rejection (AR) and chronic rejection (bronchiolitis obliterans syndrome [BOS]) induce circulating exosomes known to contain donor human leukocyte antigens and lung-associated self-antigens. Here, we sought to identify proteomic signatur...

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Autores principales: Bansal, Sandhya, McGilvrey, Marissa, Garcia-Mansfield, Krystine, Sharma, Ritin, Bremner, Ross M., Smith, Michael A., Hachem, Ramsey, Pirrotte, Patrick, Mohanakumar, Thalachallour
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2020
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7315412/
https://www.ncbi.nlm.nih.gov/pubmed/32596573
http://dx.doi.org/10.1021/acsomega.0c00859
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author Bansal, Sandhya
McGilvrey, Marissa
Garcia-Mansfield, Krystine
Sharma, Ritin
Bremner, Ross M.
Smith, Michael A.
Hachem, Ramsey
Pirrotte, Patrick
Mohanakumar, Thalachallour
author_facet Bansal, Sandhya
McGilvrey, Marissa
Garcia-Mansfield, Krystine
Sharma, Ritin
Bremner, Ross M.
Smith, Michael A.
Hachem, Ramsey
Pirrotte, Patrick
Mohanakumar, Thalachallour
author_sort Bansal, Sandhya
collection PubMed
description [Image: see text] Lung transplant recipients (LTxRs) with acute rejection (AR) and chronic rejection (bronchiolitis obliterans syndrome [BOS]) induce circulating exosomes known to contain donor human leukocyte antigens and lung-associated self-antigens. Here, we sought to identify proteomic signatures in circulating extracellular vesicles (EVs) that differentiate LTxRs in 4 groups: stable, AR, BOS, or respiratory viral infection (RVI). EVs were isolated from plasma from patients in each group via ultracentrifugation. EV protein cargoes were prepared for shotgun proteomics using liquid chromatography–tandem mass spectrometry. We identified 2 unique proteins for AR, 4 for RVI, 24 for BOS, and 8 for stable LTxRs. Differential analysis of AR, BOS, RVI, and stable proteins identified significantly deregulated proteins (p < 0.05, log(2)(fold change) > ±1) in each condition (31, 2, and 2, respectively). EVs from LTxRs with AR contained proteins involved in immunoglobulin, complement regulation, coagulation, and innate and adaptive immune response pathways. EVs from LTxRs with BOS revealed enriched immunoglobulin receptors and a carboxypeptidase N catalytic chain. EVs from LTxRs with RVI had an enriched macrophage-stimulating factor. We found unique signatures in LTxRs with AR, BOS, and RVI, highlighting complex immune mechanisms underlying lung allograft rejection. Proteomic signatures in LTxRs’ circulating EVs provided insights into immunological mechanisms of graft rejection and RVI.
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spelling pubmed-73154122020-06-26 Global Proteomics Analysis of Circulating Extracellular Vesicles Isolated from Lung Transplant Recipients Bansal, Sandhya McGilvrey, Marissa Garcia-Mansfield, Krystine Sharma, Ritin Bremner, Ross M. Smith, Michael A. Hachem, Ramsey Pirrotte, Patrick Mohanakumar, Thalachallour ACS Omega [Image: see text] Lung transplant recipients (LTxRs) with acute rejection (AR) and chronic rejection (bronchiolitis obliterans syndrome [BOS]) induce circulating exosomes known to contain donor human leukocyte antigens and lung-associated self-antigens. Here, we sought to identify proteomic signatures in circulating extracellular vesicles (EVs) that differentiate LTxRs in 4 groups: stable, AR, BOS, or respiratory viral infection (RVI). EVs were isolated from plasma from patients in each group via ultracentrifugation. EV protein cargoes were prepared for shotgun proteomics using liquid chromatography–tandem mass spectrometry. We identified 2 unique proteins for AR, 4 for RVI, 24 for BOS, and 8 for stable LTxRs. Differential analysis of AR, BOS, RVI, and stable proteins identified significantly deregulated proteins (p < 0.05, log(2)(fold change) > ±1) in each condition (31, 2, and 2, respectively). EVs from LTxRs with AR contained proteins involved in immunoglobulin, complement regulation, coagulation, and innate and adaptive immune response pathways. EVs from LTxRs with BOS revealed enriched immunoglobulin receptors and a carboxypeptidase N catalytic chain. EVs from LTxRs with RVI had an enriched macrophage-stimulating factor. We found unique signatures in LTxRs with AR, BOS, and RVI, highlighting complex immune mechanisms underlying lung allograft rejection. Proteomic signatures in LTxRs’ circulating EVs provided insights into immunological mechanisms of graft rejection and RVI. American Chemical Society 2020-06-12 /pmc/articles/PMC7315412/ /pubmed/32596573 http://dx.doi.org/10.1021/acsomega.0c00859 Text en Copyright © 2020 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Bansal, Sandhya
McGilvrey, Marissa
Garcia-Mansfield, Krystine
Sharma, Ritin
Bremner, Ross M.
Smith, Michael A.
Hachem, Ramsey
Pirrotte, Patrick
Mohanakumar, Thalachallour
Global Proteomics Analysis of Circulating Extracellular Vesicles Isolated from Lung Transplant Recipients
title Global Proteomics Analysis of Circulating Extracellular Vesicles Isolated from Lung Transplant Recipients
title_full Global Proteomics Analysis of Circulating Extracellular Vesicles Isolated from Lung Transplant Recipients
title_fullStr Global Proteomics Analysis of Circulating Extracellular Vesicles Isolated from Lung Transplant Recipients
title_full_unstemmed Global Proteomics Analysis of Circulating Extracellular Vesicles Isolated from Lung Transplant Recipients
title_short Global Proteomics Analysis of Circulating Extracellular Vesicles Isolated from Lung Transplant Recipients
title_sort global proteomics analysis of circulating extracellular vesicles isolated from lung transplant recipients
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7315412/
https://www.ncbi.nlm.nih.gov/pubmed/32596573
http://dx.doi.org/10.1021/acsomega.0c00859
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