WANG Zi-Sheng, QI Zhi-Tao, TIAN Jing-Yun, QIU Ming, ZHAO Wei-Hong, WANG Ai-Min, HUA. Cloning of hemoglobin-α1 from half-smooth tongue sole (Cynoglossus semilaevis) and its expression under short-term hypoxia. Zoological Research, 2011, 32(6): 641-646. doi: 10.3724/SP.J.1141.2011.06641
Citation:
WANG Zi-Sheng, QI Zhi-Tao, TIAN Jing-Yun, QIU Ming, ZHAO Wei-Hong, WANG Ai-Min, HUA. Cloning of hemoglobin-α1 from half-smooth tongue sole (Cynoglossus semilaevis) and its expression under short-term hypoxia. Zoological Research, 2011, 32(6): 641-646. doi: 10.3724/SP.J.1141.2011.06641
WANG Zi-Sheng, QI Zhi-Tao, TIAN Jing-Yun, QIU Ming, ZHAO Wei-Hong, WANG Ai-Min, HUA. Cloning of hemoglobin-α1 from half-smooth tongue sole (Cynoglossus semilaevis) and its expression under short-term hypoxia. Zoological Research, 2011, 32(6): 641-646. doi: 10.3724/SP.J.1141.2011.06641
Citation:
WANG Zi-Sheng, QI Zhi-Tao, TIAN Jing-Yun, QIU Ming, ZHAO Wei-Hong, WANG Ai-Min, HUA. Cloning of hemoglobin-α1 from half-smooth tongue sole (Cynoglossus semilaevis) and its expression under short-term hypoxia. Zoological Research, 2011, 32(6): 641-646. doi: 10.3724/SP.J.1141.2011.06641
Key Laboratory of Aquaculture and Ecology of Coastal Pool in Jiangsu Province, Department of Ocean Technology, Yancheng Institute of Technology, Yancheng Jiangsu 224051, China; 2. School of Biology and Chemical Engineering, Jiangsu University of Science and Technology, Zhenjiang Jiangsu 212018, China; 3. National Oceanographic Center, Qingdao Shandong 266071, China
Funds:This study was financially supported by Nature Science Foundation of Jiangsu Province (BK2011418), the Graduate Research and Innovation of Colleges and Universities in Jiangsu Province (CX09B_106Z) and Natural Science Foundation of the Jiangsu Higher Education Institutions of China (09KJD240004)
This study cloned the hemoglobin α1 from the marine teleost, the half-smooth tongue sole (Cynoglossus semilaevis), and then examined its expression under hypoxia exposure. The full-length of CsHb-α1 (594 bp) cDNA contains an open reading frame encoding 144 amino acids. Sequence analysis shows that the predicted CsHb-α1 amino acids shares high identities with that of other species. Real-time PCR showed that CsHb-α1 was highly expressed in the heart, liver, spleen, kidney and blood. Five to 120 min esposure and long-term (36 h) exposure to hypoxia (1.0 mg/L) significantly increased CsHb-α1 mRNA expression in most tissues compared to those fish held in normoxic conditions (dissolved oxygen (DO): 6.2 mg/L). These results suggested that the up-regulation of Hb-α1 is an important component for adaptation of half-smooth tongue sole to short-term hypoxia.
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