Isolation and Gene Expression of Yellow Grouper Ferritin Heavy Chain Subunit After Lipopolysaccharide Treatment |
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Authors: | Li Wang Yong Wei |
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Institution: | Key Laboratory of Animal Genetics and Breeding of State Ethnic Affairs Commission & Ministry of Education, College of Life Science and Technology, Southwest University for Nationalities, Chengdu, 610041, China. qinxin916@yahoo.com.cn |
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Abstract: | Ferritin is a ubiquitous and conserved iron storage protein that plays a central role in iron metabolism. The ferritin heavy chain subunit (FerH) homolog was isolated from yellow grouper (Epinephelus awoara) spleen using suppression subtractive hybridization and RACE-PCR. The nucleotide sequence of FerH full-length cDNA was 1173 bp and contained an open reading frame of 534 bp, encoding a putative protein of 177 amino acids. The encoded protein shows 78-94% identity with homologs. Based on phylogenetic analysis, yellow grouper FerH is highly conserved throughout evolution and is closer to European seabass than to other species. RT-PCR analysis demonstrated that FerH was widely expressed in various healthy tissues and significantly up-regulated in liver, spleen, and anterior kidney by lipopolysaccharide. The results suggest that yellow grouper FerH may play a role in immune response. |
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