期刊
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY
卷 207, 期 -, 页码 36-42出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cbpa.2017.02.010
关键词
Macro brachium nipponense; Membrane-bound hemoglobin; Hypoxia; Oxidative stress; Gill
资金
- National Fundamental Research Program, China [31672633]
- Open Funding Project of the Key Laboratory of Exploration and Utilization of Aquatic Genetic Resources [K2016-02]
- National Twelfth Five-Year Plan for Science & Technology Support [2012BAD25B07]
- Fund of Independent Innovation of Agricultural Sciences of Jiangsu Province [CX (15)1012-4]
- three aquatic projects of Jiangsu Province [D2015-16]
- Science and Technology Development Fund of Wuxi [CLE02N1514]
Most hemoglobins are respiratory proteins and are ubiquitous in animals, bacteria, fungi, protists, and plants. In this study, we describe a membrane-bound hemoglobin in the oriental river prawn Macrobrachium nipponense (MnHb), which also expresses hemocyanin. MnHb cDNA was cloned using the rapid amplification of cDNA ends (RACE) approach, which afforded a 1201 bp gene encoding a 193 amino acid polypeptide. Bioinformatic evaluation suggested MnHb is membrane anchored by N-myristoylation, and immunofluorescence confirmed its location in the membrane of chief cells in the gill. The effect of hypoxia on MnHb expression was investigated, and reverse transcription PCR (RT-PCR) and Western blotting showed that MnHb was expressed almost exclusively in the gill. Quantitative RT-PCR revealed a significant increase in expression after 6 h of hypoxia, and levels peaked at 24 h due to oxidative stress. Exposure of cultured prawns to the stress inducer H2O2 significantly up regulated the expression of MnHb in a dose-dependent manner. MnHb may have a role in protecting cell membrane lipids from damage by reactive oxygen species. (C) 2017 Elsevier Inc. All rights reserved.
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