Isolation and gene expression of yellow grouper ferritin heavy chain subunit after lipopolysaccharide treatment.
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.
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
Li
L
Wang
Yong
Y
Wei
D000818:Animals; D001052:Apoferritins / Q000235:genetics* / Q000378:metabolism; D001492:Bass / Q000235:genetics; D029941:Fish Proteins / Q000235:genetics* / Q000378:metabolism; D015870:Gene Expression; D008070:Lipopolysaccharides / Q000494:pharmacology*; D010802:Phylogeny; D021122:Protein Subunits / Q000235:genetics / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction
D029941:Fish Proteins; D008070:Lipopolysaccharides; D021122:Protein Subunits; D001052:Apoferritins