Cloning and Induced Expression of Acyl-CoA Binding Protein Gene from Sea Perch Lateolabrax japonicus

Abstract: Acyl-CoA-binding protein (ACBP) has been proposed to play a pivotal role in the intracellular trafficking and the utilization of long-chain fatty acyl-CoA esters. Full-length cDNA coding for Lateolabrax japonicus ACBP was isolated from liver total RNA by RACE techniques. It was shown to be 679 bp， which included a 83 bp of 5'-untranslated region (UTR)， a 326 bp 3'-UTR and a 270 bp open reading frame (ORF). The deduced ACBP was comprised of 89 amino acids with a theoretical isoelectric point of 5.44 and molecular weight of 10.14 kDa.The amino acid sequence comparision of ACBPs showed that Lateolabrax japonicus shared 87%， 84%， 78% and 68% identity with Medaka， sablefish， Atlantic salmon and human， respectively. Semi-quantitative RT-PCR and real-time PCR were used to characterize the expression profile of Acbp. The results showed that Lateolabrax japonicus Acbp was expressed in all ten tissues tested (muscle， heart， eye， brain， gill， liver， intestine， kidney， fat and spleen) with highest expression in kidney and liver， lowest in muscle， eye and brain. The Acbp expression in sea perch liver is down-regulated by fasting， up-regulated by insulin but not glucose.

CSTR: 32200.14.cjcb.2011.01.0004