CONTRIBUTIONSMN formulated the MYDGF Protein site present hypothesis and he was responsible for writing
CONTRIBUTIONSMN formulated the present hypothesis and he was responsible for writing the report. NB made essential revision for the manuscript. The original figures were developed by MN.
Li et al. Cellular Molecular Biology Letters (2016) 21:25 DOI 10.1186/s11658-016-0026-Cellular Molecular Biology LettersSHORT COMMUNICATIONOpen AccessThe identification of human aldo-keto reductase AKR7A2 as a novel cytoglobinbinding partnerXin Li, Shanshan Zou, Zhen Li, Gaotai Cai, Bohong Chen, Ping Wang and Wenqi Dong Correspondence: [email protected] Department of Biopharmaceutics, School of Laboratory Medicine and Biotechnology, Southern Medical University, 1838 North Guangzhou Avenue, Guangzhou 510515, ChinaAbstractCytoglobin (CYGB), a member with the globin family members, is believed to safeguard cells from reactive oxygen and nitrogen species and cope with hypoxic conditions and oxidative HGF Protein supplier pressure. Nonetheless, its molecular mechanisms of action aren’t clearly understood. By means of immunoprecipitation combined using a two-dimensional electrophoresis ass spectrometry assay, we identified a CYGB interactor: aldo-keto reductase family members 7 member A2 (AKR7A2). The interaction was further confirmed utilizing yeast two-hybrid and co-immunoprecipitation assays. Our benefits show that AKR7A2 physically interacts with CYGB. Keywords and phrases: CYGB, AKR7A2, Protein-protein interactions, Yeast two-hybrid assay, Co-immunoprecipitation, 2-DE, Oxidative stressIntroduction Cytoglobin (CYGB), which can be a member of the globin family members, was discovered more than a decade ago in a proteomic screen of fibrotic liver [1]. It was originally named STAP (stellate activating protein). Human CYGB is often a 190-amino acid, 21-kDa protein [2], encoded by a single copy gene mapped at the 17q25.3 chromosomal segment [3]. It has a compact helical conformation, providing it the capacity to bind to heme, which allows reversible binding of gaseous, diatomic molecules, such as oxygen (O2), nitric oxide (NO) and carbon monoxide (CO), just like hemoglobin (Hb), myoglobin (Mb) and neuroglobin (Ngb) [4]. As opposed to those household members, which are respectively localized in the erythrocytes, muscle tissues and neurons and neuroendocrine tissue, CYGB is expressed across a broad spectrum of vertebrate organs and tissues with varying expression levels. It is actually located predominantly in the fibroblasts of connective tissue and in fibroblast-related cell lineages, including chondroblasts, osteoblasts, hepatic stellate cells (HSCs) and myofibroblasts, and it may play a part in fibrotic organ disorder [3, 5]. Given its similarity to other globins (especially Mb and Ngb), quite a few respiratory and stress-related activities for CYGB have been considered. These involve oxygen storage, transport and sensing, terminal oxidase activity, nitric oxide dioxygenase activity [6], and scavenging of reactive oxygen species (ROS) [7]. It truly is also believed to defend cells from reactive oxygen and nitrogen species and handle hypoxic situations and oxidative anxiety within the cells [8]. CYGB is related with various diseases,The Author(s). 2016 Open Access This article is distributed below the terms with the Inventive Commons Attribution four.0 International License (://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give suitable credit to the original author(s) plus the supply, give a hyperlink towards the Inventive Commons license, and indicate if alterations were produced. The Inventive Commons Public Domain De.