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Molecular Cloning, Tissue Distribution, and Hypoxia and Ammonia Stress Response of the p38 MAPK of Black Seabream (Acanthopagrus schlegelii)

Molecular Cloning, Tissue Distribution, and Hypoxia and Ammonia Stress Response of the p38 MAPK of Black Seabream (Acanthopagrus schlegelii)

Jing Wang1, Tiejin Tong1, Yuanchao Zou2, Xiaoling Xu1, Qiang Wu1 and Qingchao Shi2*

1Agricultural College, Yibin Vocational and Technical College, Yibin 644000, China
2Key Laboratory of Sichuan Province for Fishes Conservation and Utilization in the Upper Reaches of the Yangtze River, Neijiang Normal University, Neijiang 641000, Sichuan Province, P. R. China
 
*      Corresponding author: [email protected]

Fig. 1.

The cDNA and deduced protein sequences of black seabream. The start (ATG) and stop (TAA) codons are indicated in bold, the MAPK superfamily homology domain of p38 MAPK is shaded in gray, and the predicted TGY phosphorylation motif and ATRW substrate-binding site are indicated by black boxes.

Fig. 2.

Multiple sequence alignment of the p38 MAPK protein of black seabream and other species. 

Fig. 3.

Phylogenetic tree of the p38 MAPK proteins of black seabream and other organisms.

Fig. 4.

Relative expression of p38 MAPK mRNA in the different tissues of black seabream.

Fig. 5.

Relative mRNA expression levels of p38 MAPK in the (A) spleen, (B) head kidney, (C) gills, and (D) liver tissues of black seabream at different time points under ammonia stress.

Fig. 6.

Relative mRNA expression levels of p38 MAPK in the (A) spleen, (B) head kidney, (C) gills, and (D) liver tissues of black seabream at different time points under hypoxia stress.

Pakistan Journal of Zoology

April

Pakistan J. Zool., Vol. 57, Iss. 2, pp. 501-1001

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