Cloning, Molecular Characteristics of ACBP Gene and Its Expression Profile Analysis in Binglangjiang Buffalo
SHENG Dan1, LIU Qin1, TENG Xiaohong1, ZHANG Yongyun2, JI Li3, MIAO Yongwang1
1. Faculty of Animal Science and Technology, Yunnan Agricultural University, Kunming 650201, China;
2. Teaching Demonstration Center of the Basic Experiments of Agricultural Majors, Yunnan Agricultural University, Kunming 650201, China;
3. Institute of Animal Husbandry, Yunnan Vocational and Technical College of Agriculture, Kunming 650212, China
Abstract：The coding product of ACBP gene is an important transport protein for long chain acyl coenzyme A esters in cells. Recently, it is found that this gene is closely related to lactation traits in common dairy cows, but it is rarely reported in water buffalo. The purpose of this study is to explore the sequence and gene expression characteristics of buffalo ACBP gene in order to reveal its function. The coding region of ACBP gene of Binglangjiang buffalo was cloned by RT-PCR method, and the gene was then subjected to analysis of functional bioinformatics and gene expression profiling. The sequence of complete coding region of ACBP gene in Binglangjiang buffalo was 264 bp in length which encoded a protein composed of 87 amino acid residues. This protein had a ACBP functional domain and contained 4 phosphorylated sites. It had no signal peptide and transmembrane region and was a hydrophilic protein located in the cell. The homology analysis of ACBP protein showed that Binglangjiang buffalo and the species of bovine subfamily were clustered together, which revealed the functional similarity of their ACBP gene.In the 13 tissues assayed, buffalo ACBP gene was highly expressed in the rumen, brain, heart during lactating stage and this gene was highly expressed in the rumen, heart, spleen during non-lactating stage. In addtition, ACBP gene was expressed in mammary gland, small intestine and liver during lactating stage, however it was not expressed in those tissues during non-lactating stage.The ACBP of buffalo and other species had similar amino acid composition and structural characteristics, which might participate in the transport of long chain acyl coenzyme A esters and plays an important role in the synthesis of milk fat.
[1] Van Aalten D M, Milne K G, Zou J Y, et al. Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein[J]. Journal of Molecular Biology, 2001, 309(1):181-192.
[2] Mogensen I B, Schulenberg H, Hansen H O, et al. A novel acyl-CoA-binding protein from bovine liver. Effect on fatty acid synthesis[J]. The Biochemical Journal, 1987, 241(1):189-192.
[3] Christian C A, Herbert A G, Holt R L, et al. Endogenous positive allosteric modulation of GABAA receptors by diazepam binding inhibitor[J]. Neuron, 2013, 78(6):1063-1091.
[4] Li Y, Hao Y, Owyang C. Diazepam-binding inhibitor mediates feedback regulation of pancreatic secretion and postprandial release of cholecystokinin[J]. The Journal of Clinical Investigation, 2000, 105(3):351-359.
[5] Burton M, Rose T M, Faergeman N J, et al. Evolution of the acyl-CoA binding protein (ACBP)[J]. The Biochemical Journal, 2005, 392(Pt 2):299-307.
[6] Kragelund B B, Højrup P, Jensen M S, et al. Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family[J]. Journal of Molecular Biology, 1996, 256(1):187-200.
[7] Taskinen J P, Van Aalten D M, Knudsen J, et al. High resolution crystal structures of unliganded and liganded human liver ACBP reveal a new mode of binding for the acyl-CoA ligand[J]. Proteins, 2007, 66(1):229-238.
[8] Hansen J S, Faergeman N J, Kragelund B B, et al. Acyl-CoA-binding protein (ACBP) localizes to the endoplasmic reticulum and Golgi in a ligand-dependent manner in mammalian cells[J]. The Biochemical Journal, 2008, 410(3):463-472.
[9] Yuzbasheva E Y, Mostova E B, Andreeva N I, et al. Co-expression of glucose-6-phosphate dehydrogenase and acyl-CoA binding protein enhances lipid accumulation in the yeast Yarrowia lipolytica[J]. New Biotechnology, 2017, 39(Pt A):18-21.
[10] Oikari S, Ahtialansaari T, Heinonen M V, et al. Downregulation of PPARs and SREBP by acyl-CoA-binding protein overexpression in transgenic rats[J]. Pflugers Archiv:European Journal of Physiology, 2008, 456(2):369-377.
[11] Oikari, Sanna. Evaluation of phenotypic changes of Acyl-CoA binding protein/diazepam binding inhibitor overexpression in transgenic mice and rats[J]. Confinia Neurologica, 2008, 27(1):45-52.
[12] 戴江河, 石昭意, 潘斌, 等. 水牛奶营养与功能研究进展[J]. 中国奶牛, 2017(6):10-13.
[13] 余选富, 王友文, 邵思远, 等. 槟榔江水牛生产性能测定及其种质评价[J]. 中国奶牛, 2018(3):27-30.
[14] Micheletto M C, Mendes L F, Basso L G, et al. Lipid membranes and acyl-CoA esters promote opposing effects on acyl-CoA binding protein structure and stability[J]. International Journal of Biological Macromolecules, 2017, 102:284-296.
[15] Neess D, Bek S, Engelsby H, et al. Long-chain acyl-CoA esters in metabolism and signaling:Role of acyl-CoA binding proteins[J]. Progress in Lipid Research, 2015, 59(3):1-25.
[16] Rosendal J, Ertbjerg P, Knudsen J. Characterization of ligand binding to acyl-CoA-binding protein[J]. The Biochemical Journal, 1993, 290(Pt 2):321-326.
[17] Bionaz M, Loor J J. Gene networks driving bovine milk fat synthesis during the lactation cycle[J]. BMC Genomics, 2008, 9(1):366.
[18] Faergeman N J, Wadum M, Feddersen S, et al. Acyl-CoA binding proteins; structural and functional conservation over 2000 MYA[J]. Molecular and Cellular Biochemistry, 2007, 299(1/2):55-65.
[19] Vock C, Döring F, Nitz I. Transcriptional regulation of HMG-CoA synthase and HMG-CoA reductase genes by human ACBP[J]. Cellular Physiology and Biochemistry, 2008, 22(5/6):515-524.
[20] Vock C, Biedasek K, Boomgaarden I, et al. ACBP knockdown leads to down-regulation of genes encoding rate-limiting enzymes in cholesterol and fatty acid metabolism[J]. Cellular Physiology and Biochemistry, 2010, 25(6):675-686.
[21] Neess D, Bek S, Bloksgaard M, et al. Delayed hepatic adaptation to weaning in ACBP-/-mice is caused by disruption of the epidermal barrier[J]. Cell Reports, 2013, 5(5):1403-1412.
[22] Gallego S F, Sprenger R R, Neess D, et al. Quantitative lipidomics reveals age-dependent perturbations of whole-body lipid metabolism in ACBP deficient mice[J]. Biochimica et Biophysica acta, 2017, 1862(2):145-155.
[23] Bek S, Neess D, Dixen K, et al. Compromised epidermal barrier stimulates Harderian gland activity and hypertrophy in ACBP-/-mice[J]. Journal of Lipid Research, 2015, 56(9):1738-1746.
[24] 南雪梅. 奶山羊乳腺物质代谢研究[D].哈尔滨:东北农业大学, 2010.
2018, Vol. 33 
