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Labile disulfide bonds are common at the leucocyte cell surface
Redox conditions change in events such as immune and platelet activation, and during viral infection, but the biochemical consequences are not well characterized. There is evidence that some disulfide bonds in membrane proteins are labile while others that are probably structurally important are not...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3352085/ https://www.ncbi.nlm.nih.gov/pubmed/22645650 http://dx.doi.org/10.1098/rsob.110010 |
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author | Metcalfe, Clive Cresswell, Peter Ciaccia, Laura Thomas, Benjamin Barclay, A. Neil |
author_facet | Metcalfe, Clive Cresswell, Peter Ciaccia, Laura Thomas, Benjamin Barclay, A. Neil |
author_sort | Metcalfe, Clive |
collection | PubMed |
description | Redox conditions change in events such as immune and platelet activation, and during viral infection, but the biochemical consequences are not well characterized. There is evidence that some disulfide bonds in membrane proteins are labile while others that are probably structurally important are not exposed at the protein surface. We have developed a proteomic/mass spectrometry method to screen for and identify non-structural, redox-labile disulfide bonds in leucocyte cell-surface proteins. These labile disulfide bonds are common, with several classes of proteins being identified and around 30 membrane proteins regularly identified under different reducing conditions including using enzymes such as thioredoxin. The proteins identified include integrins, receptors, transporters and cell–cell recognition proteins. In many cases, at least one cysteine residue was identified by mass spectrometry as being modified by the reduction process. In some cases, functional changes are predicted (e.g. in integrins and cytokine receptors) but the scale of molecular changes in membrane proteins observed suggests that widespread effects are likely on many different types of proteins including enzymes, adhesion proteins and transporters. The results imply that membrane protein activity is being modulated by a ‘redox regulator’ mechanism. |
format | Online Article Text |
id | pubmed-3352085 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-33520852012-05-29 Labile disulfide bonds are common at the leucocyte cell surface Metcalfe, Clive Cresswell, Peter Ciaccia, Laura Thomas, Benjamin Barclay, A. Neil Open Biol Research Redox conditions change in events such as immune and platelet activation, and during viral infection, but the biochemical consequences are not well characterized. There is evidence that some disulfide bonds in membrane proteins are labile while others that are probably structurally important are not exposed at the protein surface. We have developed a proteomic/mass spectrometry method to screen for and identify non-structural, redox-labile disulfide bonds in leucocyte cell-surface proteins. These labile disulfide bonds are common, with several classes of proteins being identified and around 30 membrane proteins regularly identified under different reducing conditions including using enzymes such as thioredoxin. The proteins identified include integrins, receptors, transporters and cell–cell recognition proteins. In many cases, at least one cysteine residue was identified by mass spectrometry as being modified by the reduction process. In some cases, functional changes are predicted (e.g. in integrins and cytokine receptors) but the scale of molecular changes in membrane proteins observed suggests that widespread effects are likely on many different types of proteins including enzymes, adhesion proteins and transporters. The results imply that membrane protein activity is being modulated by a ‘redox regulator’ mechanism. The Royal Society 2011-11 /pmc/articles/PMC3352085/ /pubmed/22645650 http://dx.doi.org/10.1098/rsob.110010 Text en http://creativecommons.org/licenses/by/3.0/ © 2011 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0/, which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Research Metcalfe, Clive Cresswell, Peter Ciaccia, Laura Thomas, Benjamin Barclay, A. Neil Labile disulfide bonds are common at the leucocyte cell surface |
title | Labile disulfide bonds are common at the leucocyte cell surface |
title_full | Labile disulfide bonds are common at the leucocyte cell surface |
title_fullStr | Labile disulfide bonds are common at the leucocyte cell surface |
title_full_unstemmed | Labile disulfide bonds are common at the leucocyte cell surface |
title_short | Labile disulfide bonds are common at the leucocyte cell surface |
title_sort | labile disulfide bonds are common at the leucocyte cell surface |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3352085/ https://www.ncbi.nlm.nih.gov/pubmed/22645650 http://dx.doi.org/10.1098/rsob.110010 |
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