The identification of human aldo-keto reductase AKR7A2 as a novel cytoglobin-binding partner

Cytoglobin (CYGB), a member of the globin family, is thought to protect cells from reactive oxygen and nitrogen species and deal with hypoxic conditions and oxidative stress. However, its molecular mechanisms of action are not clearly understood. Through immunoprecipitation combined with a two-dimen...

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Autores principales: Li, Xin, Zou, Shanshan, Li, Zhen, Cai, Gaotai, Chen, Bohong, Wang, Ping, Dong, Wenqi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2016
Materias:
Short Communication
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5415844/
https://www.ncbi.nlm.nih.gov/pubmed/28536627
http://dx.doi.org/10.1186/s11658-016-0026-9
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author Li, Xin
Zou, Shanshan
Li, Zhen
Cai, Gaotai
Chen, Bohong
Wang, Ping
Dong, Wenqi
author_facet Li, Xin
Zou, Shanshan
Li, Zhen
Cai, Gaotai
Chen, Bohong
Wang, Ping
Dong, Wenqi
author_sort Li, Xin
collection PubMed
description Cytoglobin (CYGB), a member of the globin family, is thought to protect cells from reactive oxygen and nitrogen species and deal with hypoxic conditions and oxidative stress. However, its molecular mechanisms of action are not clearly understood. Through immunoprecipitation combined with a two-dimensional electrophoresis–mass spectrometry assay, we identified a CYGB interactor: aldo-keto reductase family 7 member A2 (AKR7A2). The interaction was further confirmed using yeast two-hybrid and co-immunoprecipitation assays. Our results show that AKR7A2 physically interacts with CYGB.
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spelling pubmed-54158442017-05-23 The identification of human aldo-keto reductase AKR7A2 as a novel cytoglobin-binding partner Li, Xin Zou, Shanshan Li, Zhen Cai, Gaotai Chen, Bohong Wang, Ping Dong, Wenqi Cell Mol Biol Lett Short Communication Cytoglobin (CYGB), a member of the globin family, is thought to protect cells from reactive oxygen and nitrogen species and deal with hypoxic conditions and oxidative stress. However, its molecular mechanisms of action are not clearly understood. Through immunoprecipitation combined with a two-dimensional electrophoresis–mass spectrometry assay, we identified a CYGB interactor: aldo-keto reductase family 7 member A2 (AKR7A2). The interaction was further confirmed using yeast two-hybrid and co-immunoprecipitation assays. Our results show that AKR7A2 physically interacts with CYGB. BioMed Central 2016-10-24 /pmc/articles/PMC5415844/ /pubmed/28536627 http://dx.doi.org/10.1186/s11658-016-0026-9 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Short Communication
Li, Xin
Zou, Shanshan
Li, Zhen
Cai, Gaotai
Chen, Bohong
Wang, Ping
Dong, Wenqi
The identification of human aldo-keto reductase AKR7A2 as a novel cytoglobin-binding partner
title The identification of human aldo-keto reductase AKR7A2 as a novel cytoglobin-binding partner
title_full The identification of human aldo-keto reductase AKR7A2 as a novel cytoglobin-binding partner
title_fullStr The identification of human aldo-keto reductase AKR7A2 as a novel cytoglobin-binding partner
title_full_unstemmed The identification of human aldo-keto reductase AKR7A2 as a novel cytoglobin-binding partner
title_short The identification of human aldo-keto reductase AKR7A2 as a novel cytoglobin-binding partner
title_sort identification of human aldo-keto reductase akr7a2 as a novel cytoglobin-binding partner
topic Short Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5415844/
https://www.ncbi.nlm.nih.gov/pubmed/28536627
http://dx.doi.org/10.1186/s11658-016-0026-9
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