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An Interplay of S-Nitrosylation and Metal Ion Binding for Astrocytic S100B Protein
Mammalian S100B protein plays multiple important roles in cellular brain processes. The protein is a clinically used marker for several pathologies including brain injury, neurodegeneration and cancer. High levels of S100B released by astrocytes in Down syndrome patients are responsible for reduced...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4861259/ https://www.ncbi.nlm.nih.gov/pubmed/27159591 http://dx.doi.org/10.1371/journal.pone.0154822 |
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author | Bajor, Małgorzata Zaręba-Kozioł, Monika Zhukova, Liliya Goryca, Krzysztof Poznański, Jarosław Wysłouch-Cieszyńska, Aleksandra |
author_facet | Bajor, Małgorzata Zaręba-Kozioł, Monika Zhukova, Liliya Goryca, Krzysztof Poznański, Jarosław Wysłouch-Cieszyńska, Aleksandra |
author_sort | Bajor, Małgorzata |
collection | PubMed |
description | Mammalian S100B protein plays multiple important roles in cellular brain processes. The protein is a clinically used marker for several pathologies including brain injury, neurodegeneration and cancer. High levels of S100B released by astrocytes in Down syndrome patients are responsible for reduced neurogenesis of neural progenitor cells and induction of cell death in neurons. Despite increasing understanding of S100B biology, there are still many questions concerning the detailed molecular mechanisms that determine specific activities of S100B. Elevated overexpression of S100B protein is often synchronized with increased nitric oxide-related activity. In this work we show S100B is a target of exogenous S-nitrosylation in rat brain protein lysate and identify endogenous S-nitrosylation of S100B in a cellular model of astrocytes. Biochemical studies are presented indicating S-nitrosylation tunes the conformation of S100B and modulates its Ca(2+) and Zn(2+) binding properties. Our in vitro results suggest that the possibility of endogenous S-nitrosylation should be taken into account in the further studies of in vivo S100B protein activity, especially under conditions of increased NO-related activity. |
format | Online Article Text |
id | pubmed-4861259 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-48612592016-05-13 An Interplay of S-Nitrosylation and Metal Ion Binding for Astrocytic S100B Protein Bajor, Małgorzata Zaręba-Kozioł, Monika Zhukova, Liliya Goryca, Krzysztof Poznański, Jarosław Wysłouch-Cieszyńska, Aleksandra PLoS One Research Article Mammalian S100B protein plays multiple important roles in cellular brain processes. The protein is a clinically used marker for several pathologies including brain injury, neurodegeneration and cancer. High levels of S100B released by astrocytes in Down syndrome patients are responsible for reduced neurogenesis of neural progenitor cells and induction of cell death in neurons. Despite increasing understanding of S100B biology, there are still many questions concerning the detailed molecular mechanisms that determine specific activities of S100B. Elevated overexpression of S100B protein is often synchronized with increased nitric oxide-related activity. In this work we show S100B is a target of exogenous S-nitrosylation in rat brain protein lysate and identify endogenous S-nitrosylation of S100B in a cellular model of astrocytes. Biochemical studies are presented indicating S-nitrosylation tunes the conformation of S100B and modulates its Ca(2+) and Zn(2+) binding properties. Our in vitro results suggest that the possibility of endogenous S-nitrosylation should be taken into account in the further studies of in vivo S100B protein activity, especially under conditions of increased NO-related activity. Public Library of Science 2016-05-09 /pmc/articles/PMC4861259/ /pubmed/27159591 http://dx.doi.org/10.1371/journal.pone.0154822 Text en © 2016 Bajor et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Bajor, Małgorzata Zaręba-Kozioł, Monika Zhukova, Liliya Goryca, Krzysztof Poznański, Jarosław Wysłouch-Cieszyńska, Aleksandra An Interplay of S-Nitrosylation and Metal Ion Binding for Astrocytic S100B Protein |
title | An Interplay of S-Nitrosylation and Metal Ion Binding for Astrocytic S100B Protein |
title_full | An Interplay of S-Nitrosylation and Metal Ion Binding for Astrocytic S100B Protein |
title_fullStr | An Interplay of S-Nitrosylation and Metal Ion Binding for Astrocytic S100B Protein |
title_full_unstemmed | An Interplay of S-Nitrosylation and Metal Ion Binding for Astrocytic S100B Protein |
title_short | An Interplay of S-Nitrosylation and Metal Ion Binding for Astrocytic S100B Protein |
title_sort | interplay of s-nitrosylation and metal ion binding for astrocytic s100b protein |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4861259/ https://www.ncbi.nlm.nih.gov/pubmed/27159591 http://dx.doi.org/10.1371/journal.pone.0154822 |
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