Molecular Cloning and Expression of Glutathione Peroxidase and Glutathione S-transferases Genes From Sea Vrchin(Strongylocentrotus intermedius)

In this study, homology-base technique and RACE technique were used to clone Glutathione peroxidase and Glutathione S-transferases genes in Strongylocentrotus intermedius and the stucture of these genes were analysized. Glutathione peroxidase was the intracellular proteins which full-length cDNA was 1042 bp with an ORF of 657 bp encoding 219 amino acids without transmembrane domain and signal peptide. There were three casein kinase Ⅱ phosphorylation sites, a glycosaminoglycan site, five protease C phosphorylation sites and two N-meat funny Nichole acylation site. The RT-PCR detection discovered higher-level of GPX mRNA expression after different time of LPS stimulation. The highest GPX expression level, was recorded 9 hours after LPS stimulation in the sea urchin, starvation for 32 hours, the expression returned to the normal levels. Glutathione S-transferases was the intracellular proteins which fulllength cDNA was 1931 bp with an ORF of 684 bp encoding 228 amino acids without transmembrane domain and signal peptide. There were four casein kinase II phosphorylation sites, an N -glycosylation site, a protease C phosphorylation site and an N -meat funny Nichole acylation site. The highest expression level, of GST was recorded 12 hours after LPS stimulation in the sea urchin, starvation 36 hours, the expression returned to the normal levels. The result indicated that GPX and GST were constitutive and inducible acutephase protein and could play an important role in the immune responses.