Genome-Wide Analysis of the FABP Gene Family in Liver of Chicken (Gallus gallus): Identification,Dynamic Expression Profile, and RegulatoryMechanism

The fatty acid-binding protein (FABP) gene family, which encodes a group of fatty acid-trafficking molecules that affect cellular functions, has been studied extensively in mammals. However, little is known about the gene structure, expression profile, and regulatory mechanism of the gene family in chickens. In the present study, bioinformatics-based methods were used to identify the family members and investigate their evolutionary history and features of gene structure. Real-time PCR combined with in vivo and in vitro experiments were used to examine the spatiotemporal expression pattern, and explore the regulatory mechanism of FABP genes. The results show that nine members of the FABP gene family, which branched into two clusters and shared a conserved FATTYACIDBP domain, exist in the genome of chickens. Of these, seven FABP genes, including FABP1, FABP3-7, and FABP10 were abundantly expressed in the liver of hens. The expression levels of FABP1, FABP3, and FABP10 were significantly increased, FABP5 and FABP7 were significantly decreased, and FABP4 and FABP6 remained unchanged in hens at the peak laying stage in comparison to those at the pre-laying stage. Transcription of FABP1 and FABP3 were activated by estrogen via estrogen receptor (ER) α, whilst FABP10 was activated by estrogen via ERβ. Meanwhile, the expression of FABP1 was regulated by peroxisome proliferator activated receptor (PPAR) isoforms, of which tested PPARα and PPARβ agonists significantly inhibited the expression of FABP1, while tested PPARγ agonists significantly increased the expression of FABP1, but downregulated it when the concentration of the PPARγ agonist reached 100 nM. The expression of FABP3 was upregulated via tested PPARβ and PPARγ agonists, and the expression of FABP7 was selectively promoted via PPARγ. The expression of FABP10 was activated by all of the three tested PPAR agonists, but the expression of FABP4-6 was not affected by any of the PPAR agonists. In conclusion, members of the FABP gene family in chickens shared similar functional domains, gene structures, and evolutionary histories with mammalian species, but exhibited varying expression profiles and regulatory mechanisms. The results provide a valuable resource for better understanding the biological functions of individual FABP genes in chickens.

Download Full-text

Cloning of the heart fatty acid-binding protein (H-FABP) gene and its tissue-specific expression profile in the Lanzhou fat-tailed sheep, Ovis aries

Small Ruminant Research ◽

10.1016/j.smallrumres.2012.12.016 ◽

2013 ◽

Vol 112 (1-3) ◽

pp. 114-122 ◽

Cited By ~ 6

Author(s):

J.L. Bai ◽

H.W. Xu ◽

R.X. Zang ◽

H.J. He ◽

Y. Cai ◽

...

Keyword(s):

Fatty Acid ◽

Expression Profile ◽

Fatty Acid Binding Protein ◽

Ovis Aries ◽

Specific Expression ◽

Fatty Acid Binding ◽

Tissue Specific ◽

Tissue Specific Expression ◽

Acid Binding Protein ◽

Fabp Gene

Download Full-text

Up-regulation of the expression of the gene for liver fatty acid-binding protein by long-chain fatty acids

Biochemical Journal ◽

10.1042/bj3190483 ◽

1996 ◽

Vol 319 (2) ◽

pp. 483-487 ◽

Cited By ~ 47

Author(s):

Claire MEUNIER-DURMORT ◽

Hélène POIRIER ◽

Isabelle NIOT ◽

Claude FOREST ◽

Philippe BESNARD

Keyword(s):

Fatty Acids ◽

Fatty Acid ◽

Fatty Acid Binding Protein ◽

Fold Increase ◽

Long Chain Fatty Acids ◽

Liver Fatty Acid ◽

Fatty Acid Binding ◽

Acid Binding Protein ◽

Fabp Gene ◽

Long Chain

The role of fatty acids in the expression of the gene for liver fatty acid-binding protein (L-FABP) was investigated in the well-differentiated FAO rat hepatoma cell line. Cells were maintained in serum-free medium containing 40 µM BSA/320 µM oleate. Western blot analysis showed that oleate triggered an approx. 4-fold increase in the cytosolic L-FABP level in 16 h. Oleate specifically stimulated L-FABP mRNA in time-dependent and dose-dependent manners with a maximum 7-fold increase at 16 h in FAO cells. Preincubation of FAO cells with cycloheximide prevented the oleate-mediated induction of L-FABP mRNA, showing that protein synthesis was required for the action of fatty acids. Run-on transcription assays demonstrated that the control of L-FABP gene expression by oleate was, at least in part, transcriptional. Palmitic acid, oleic acid, linoleic acid, linolenic acid and arachidonic acid were similarly potent whereas octanoic acid was inefficient. This regulation was also found in normal hepatocytes. Therefore long-chain fatty acids are strong inducers of L-FABP gene expression. FAO cells constitute a useful tool for studying the underlying mechanism of fatty acid action.

Download Full-text

435-bp liver regulatory sequence in the liver fatty acid binding protein (L-FABP) gene is sufficient to modulate liver regional expression in transgenic zebrafish

Developmental Dynamics ◽

10.1002/dvdy.10324 ◽

2003 ◽

Vol 227 (3) ◽

pp. 347-356 ◽

Cited By ~ 50

Author(s):

Guor Mour Her ◽

Yang-Hui Yeh ◽

Jen-Leih Wu

Keyword(s):

Fatty Acid ◽

Fatty Acid Binding Protein ◽

Binding Protein ◽

Transgenic Zebrafish ◽

Regulatory Sequence ◽

Liver Fatty Acid ◽

Protein L ◽

Fatty Acid Binding ◽

Acid Binding Protein ◽

Fabp Gene

Download Full-text

Association of the heart fatty acid-binding protein gene with quality of carcass and meat traits in pigs

Arquivo Brasileiro de Medicina Veterinária e Zootecnia ◽

10.1590/s0102-09352008000200020 ◽

2008 ◽

Vol 60 (2) ◽

pp. 408-413 ◽

Cited By ~ 1

Author(s):

F.C. Figueiredo ◽

P.S. Lopes ◽

A.P.G. Pinto ◽

D.A.F. Paiva ◽

P.T. Mendonça ◽

...

Keyword(s):

Fatty Acid ◽

Fatty Acid Binding Protein ◽

Binding Protein ◽

Large White ◽

Fatty Acid Binding ◽

Acid Binding Protein ◽

Genetic Groups ◽

Pcr Products ◽

Fabp Gene

The heart fatty acid-binding protein (HFABP) gene was sequenced in parental animals of a F2 crossing of boars of the Brazilian native Piau breed with commercial sows (Landrace x Large White Pietrain). Primers used for PCR were designed to amplify four exons of the gene. The PCR products were sequenced and compared with the GenBank sequences. Differences between the generated sequences and the GenBank sequences were observed for both genetic groups. A total of 246 F2 animals were genotyped using the Hinf I restriction enzyme. Two genotypes were identified, 198 being animals HH and 48 Hh. The Hinf I SNP was significantly associated with weights of loin (bone-in) (P<0.05), jowl (P<0.05), sirloin (P<0.10), and kidneys (P<0.01). These results showed the potential of the H-FABP gene in marker-assisted selection programs for carcass traits in pigs.

Download Full-text

In vivo studies of liver-type fatty acid binding protein (L-FABP) gene expression in liver of transgenic zebrafish (Danio rerio)

FEBS Letters ◽

10.1016/s0014-5793(03)00157-1 ◽

2003 ◽

Vol 538 (1-3) ◽

pp. 125-133 ◽

Cited By ~ 129

Author(s):

Guor Mour Her ◽

Chia-Chang Chiang ◽

Wen-Ya Chen ◽

Jen-Leih Wu

Keyword(s):

Gene Expression ◽

Fatty Acid ◽

Danio Rerio ◽

Fatty Acid Binding Protein ◽

In Vivo Studies ◽

Transgenic Zebrafish ◽

Fatty Acid Binding ◽

Acid Binding Protein ◽

Fabp Gene

Download Full-text

Divergent evolution of cis-acting peroxisome proliferator-activated receptor elements that differentially control the tandemly duplicated fatty acid-binding protein genes, fabp1b.1 and fabp1b.2, in zebrafish

Genome ◽

10.1139/gen-2016-0033 ◽

2016 ◽

Vol 59 (6) ◽

pp. 403-412 ◽

Cited By ~ 6

Author(s):

Robert B. Laprairie ◽

Eileen M. Denovan-Wright ◽

Jonathan M. Wright

Keyword(s):

Fatty Acid ◽

Promoter Activity ◽

Fatty Acid Binding Protein ◽

Differential Regulation ◽

Peroxisome Proliferator ◽

Duplicated Genes ◽

Fatty Acid Binding ◽

Acid Binding Protein ◽

Selective Agonist ◽

Ppar Agonists

Gene duplication is thought to facilitate increasing complexity in the evolution of life. The fate of most duplicated genes is nonfunctionalization: functional decay resulting from the accumulation of mutations. According to the duplication–degeneration–complementation (DDC) model, duplicated genes are retained by subfunctionalization, where the functions of the ancestral gene are sub-divided between duplicate genes, or by neofunctionalization, where one of the duplicates acquires a new function. Here, we report the differential regulation of the zebrafish tandemly duplicated fatty acid-binding protein genes, fabp1b.1 and fabp1b.2, by peroxisome proliferator-activated receptors (PPAR). fabp1b.1 mRNA levels were induced in tissue explants of liver, but not intestine, by PPAR agonists. fabp1b.1 promoter activity was induced to a greater extent by rosiglitazone (PPARγ-selective agonist) compared to WY 14,643 (PPARα-selective agonist) in HEK293A cells. Mutation of a peroxisome proliferator response element (PPRE) at –1232 bp in the fabp1b.1 promoter reduced PPAR-dependent activation. fabp1b.2 promoter activity was not affected by PPAR agonists. Differential regulation of the duplicated fabp1b promoters may be the result of PPRE loss in fabp1b.2 during a meiotic crossing-over event. Retention of PPAR inducibility in fabp1b.1 and not fabp1b.2 suggests unique regulation and function of the fabp1b duplicates.

Download Full-text