Cargando…
Redox Proteomics and Platelet Activation: Understanding the Redox Proteome to Improve Platelet Quality for Transfusion
Blood banks use pathogen inactivation (PI) technologies to increase the safety of platelet concentrates (PCs). The characteristics of PI-treated PCs slightly differ from those of untreated PCs, but the underlying reasons are not well understood. One possible cause is the generation of oxidative stre...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5343922/ https://www.ncbi.nlm.nih.gov/pubmed/28208668 http://dx.doi.org/10.3390/ijms18020387 |
_version_ | 1782513454834253824 |
---|---|
author | Sonego, Giona Abonnenc, Mélanie Tissot, Jean-Daniel Prudent, Michel Lion, Niels |
author_facet | Sonego, Giona Abonnenc, Mélanie Tissot, Jean-Daniel Prudent, Michel Lion, Niels |
author_sort | Sonego, Giona |
collection | PubMed |
description | Blood banks use pathogen inactivation (PI) technologies to increase the safety of platelet concentrates (PCs). The characteristics of PI-treated PCs slightly differ from those of untreated PCs, but the underlying reasons are not well understood. One possible cause is the generation of oxidative stress during the PI process. This is of great interest since reactive oxygen species (ROS) act as second messengers in platelet functions. Furthermore, there are links between protein oxidation and phosphorylation, another mechanism that is critical for cell regulation. Current research efforts focus on understanding the underlying mechanisms and identifying new target proteins. Proteomics technologies represent powerful tools for investigating signaling pathways involving ROS and post-translational modifications such as phosphorylation, while quantitative techniques enable the comparison of the platelet resting state versus the stimulated state. In particular, redox cysteine is a key player in platelet activation upon stimulation by different agonists. This review highlights the experiments that have provided insights into the roles of ROS in platelet function and the implications for platelet transfusion, and potentially in diseases such as inflammation and platelet hyperactivity. The review also describes the implication of redox mechanism in platelet storage considerations. |
format | Online Article Text |
id | pubmed-5343922 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-53439222017-03-16 Redox Proteomics and Platelet Activation: Understanding the Redox Proteome to Improve Platelet Quality for Transfusion Sonego, Giona Abonnenc, Mélanie Tissot, Jean-Daniel Prudent, Michel Lion, Niels Int J Mol Sci Review Blood banks use pathogen inactivation (PI) technologies to increase the safety of platelet concentrates (PCs). The characteristics of PI-treated PCs slightly differ from those of untreated PCs, but the underlying reasons are not well understood. One possible cause is the generation of oxidative stress during the PI process. This is of great interest since reactive oxygen species (ROS) act as second messengers in platelet functions. Furthermore, there are links between protein oxidation and phosphorylation, another mechanism that is critical for cell regulation. Current research efforts focus on understanding the underlying mechanisms and identifying new target proteins. Proteomics technologies represent powerful tools for investigating signaling pathways involving ROS and post-translational modifications such as phosphorylation, while quantitative techniques enable the comparison of the platelet resting state versus the stimulated state. In particular, redox cysteine is a key player in platelet activation upon stimulation by different agonists. This review highlights the experiments that have provided insights into the roles of ROS in platelet function and the implications for platelet transfusion, and potentially in diseases such as inflammation and platelet hyperactivity. The review also describes the implication of redox mechanism in platelet storage considerations. MDPI 2017-02-11 /pmc/articles/PMC5343922/ /pubmed/28208668 http://dx.doi.org/10.3390/ijms18020387 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Sonego, Giona Abonnenc, Mélanie Tissot, Jean-Daniel Prudent, Michel Lion, Niels Redox Proteomics and Platelet Activation: Understanding the Redox Proteome to Improve Platelet Quality for Transfusion |
title | Redox Proteomics and Platelet Activation: Understanding the Redox Proteome to Improve Platelet Quality for Transfusion |
title_full | Redox Proteomics and Platelet Activation: Understanding the Redox Proteome to Improve Platelet Quality for Transfusion |
title_fullStr | Redox Proteomics and Platelet Activation: Understanding the Redox Proteome to Improve Platelet Quality for Transfusion |
title_full_unstemmed | Redox Proteomics and Platelet Activation: Understanding the Redox Proteome to Improve Platelet Quality for Transfusion |
title_short | Redox Proteomics and Platelet Activation: Understanding the Redox Proteome to Improve Platelet Quality for Transfusion |
title_sort | redox proteomics and platelet activation: understanding the redox proteome to improve platelet quality for transfusion |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5343922/ https://www.ncbi.nlm.nih.gov/pubmed/28208668 http://dx.doi.org/10.3390/ijms18020387 |
work_keys_str_mv | AT sonegogiona redoxproteomicsandplateletactivationunderstandingtheredoxproteometoimproveplateletqualityfortransfusion AT abonnencmelanie redoxproteomicsandplateletactivationunderstandingtheredoxproteometoimproveplateletqualityfortransfusion AT tissotjeandaniel redoxproteomicsandplateletactivationunderstandingtheredoxproteometoimproveplateletqualityfortransfusion AT prudentmichel redoxproteomicsandplateletactivationunderstandingtheredoxproteometoimproveplateletqualityfortransfusion AT lionniels redoxproteomicsandplateletactivationunderstandingtheredoxproteometoimproveplateletqualityfortransfusion |