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Poult Sci 2006. 85:1890-1895
© 2006 Poultry Science Association
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GENETICS

Tissue Expression and Association with Fatness Traits of Liver Fatty Acid-Binding Protein Gene in Chicken1

Q. Wang*, H. Li*,2, N. Li{dagger}, L. Leng* and Y. Wang*

* College of Animal Science and Technology, Northeast Agricultural University, Harbin 150030, China; and {dagger} National Laboratories for Agribiotechnology, China Agricultural University, Beijing 100094, China

2 Corresponding author: lihui{at}neau.edu.cn


   ABSTRACT
TOP
 ABSTRACT
INTRODUCTION
 MATERIALS AND METHODS
 RESULTS
 DISCUSSION
 REFERENCES
 
Fatty acid-binding proteins belong to a superfamily of lipid-binding proteins that exhibit a high affinity for long-chain fatty acids and appear to function in metabolism and intracellular transportation of lipids. The current study was designed to investigate expression characterization and association with growth and composition traits of the liver fatty acid-binding protein (L-FABP) gene in the chicken. Northern blot analysis indicated that the gene, similar to the mammal L-FABP gene, was expressed only in liver and intestinal tissues. The mRNA levels of the chicken L-FABP gene in liver and intestine had significant differences between the broilers and Baier layers. The China Agricultural University F2 population was used in the present study. Body weight and body composition traits were measured in the populations. Primers for the coding region and 5' upstream region of the L-FABP gene were designed according to chicken genomic and cDNA sequence. Polymorphisms were detected by DNA sequencing, and the PCR single-strand conformation polymorphisms method was developed to genotype the F2 population. The results indicated that the L-FABP gene polymorphisms were associated with abdominal fat weight and percentage of abdominal fat, and the L-FABP gene could be a candidate locus or linked to a major gene(s) that affects fatness traits in the chicken. The results of the current study provided basic molecular information for studying the role of the L-FABP gene in the regulation of lipid metabolism in avian species.

Key Words: liver fatty acid-binding protein gene • tissue expression • polymorphism • fatness trait • chicken


   INTRODUCTION
TOP
 ABSTRACT
 INTRODUCTION
MATERIALS AND METHODS
 RESULTS
 DISCUSSION
 REFERENCES
 
Modern broilers selected for rapid growth exhibit higher body fat deposition (Mallard and Douaire, 1988; Griffin, 1996). Fat is considered a by-product of meat and has low commercial value. It is not a cost-effective body component from a view of energy utilization, and much fat deposition can depress feed efficiency. Although several strategies of selection for leanness in poultry production have been described, it is still difficult to measure body fat content (Mallard and Douaire, 1988; Jennen et al., 2004). Molecular genetic information can be used to enhance genetic improvement of animal species. Identifying the quantitative trait nucleotide responsible for the economically important traits will facilitate poultry breeding programs.

Fatty acid-binding proteins (FABP), which are small molecular weight proteins with high binding affinities for long-chain fatty acids (Ockner et al., 1972), are the members of a superfamily of lipid-binding proteins that occur intracellularly in invertebrates and vertebrates. These proteins are involved in intracellular fatty acid movement (Tipping and Ketterer, 1981), cell growth and differentiation, cellular signaling, gene transcription, and protection of enzymes from the toxic effects of free fatty acids (Glatz and Veerkamp, 1985; Zimmerman and Veerkamp, 2002). They may also play a role in the modulation of enzyme activity and signal transduction (Grinstead et al., 1983).

In mammals, the intracellular or cytoplasmic FABP form a group of at least 9 distinct proteins, which are liver FABP (L-FABP), intestinal FABP, heart FABP, adipocyte FABP, epidermal FABP, ileal FABP, brain FABP, myelin FABP, and testicular FABP (Zimmerman and Veerkamp, 2002). Their molecular weights range from 14 to 15 kDa, with 126 to 134 amino acids, and are named according to the tissues from which they are isolated (Ockner et al., 1972). All FABP types show similar structural features, containing 10 antiparallel ß strands (ßA to ßJ) that form a ß barrel. The bound ligand is found within the barrel in a central internal water-filled cavity. The overall organization of all members of the FABP family is identical, containing 4 exons and 3 introns. The exon-intron positions are similar, but the intron length is variable among the genes (Zimmerman and Veerkamp, 2002).

Molecular cloning and structural studies have increased the knowledge of the evolutionary and cellular diversity of FABP, and, recently, studies on knockout mice have provided direct evidence for their physiological role in the uptake and transport of long-chain fatty acids and their interaction with other transport systems and enzymes (Zimmerman and Veerkamp, 2002). The L-FABP gene ablation dramatically enhanced many of the effects of dietary cholesterol to greatly induce hepatic cholesterol (primarily cholesterol ester) and triacylglycerol accumulation as well as to potentiate BW gain (primarily as fat tissue mass; Martin et al., 2006). The liver weight of L-FABP gene knockout mice increased significantly, and these mice exhibited macroscopic steatosis (Seneshaw et al., 2005). The L-FABP gene knockout mice fed a diet with and without 1% phytol (a metabolic precursor to phytanic acid) exhibited a gender-dependent lipid phenotype. Livers of phytol-fed L-FABP mice enhanced the accumulation of lipid droplets and exhibited more necrosis than their counterparts in female, but not male, mice (Atshaves et al., 2005).

Although the role of L-FABP in the metabolism of fatty acids has been studied in mammals, the physiological functions need to be demonstrated in avian species. To address this issue, the current study was designed to characterize the chicken L-FABP gene tissue expression, to identify polymorphisms of the gene in different populations, to evaluate the associations of the polymorphism of the gene with growth and body composition traits, and to provide the basic molecular information for studying the role of the gene in the regulation of fatty acid metabolism in chickens.


   MATERIALS AND METHODS
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS AND METHODS
RESULTS
 DISCUSSION
 REFERENCES
 
Bird Material and Phenotypic Traits
Broilers derived from lines at Northeast Agricultural University divergently selected for abdominal fat and Baier layers were used as tissue expression analysis in the current experiment. The Baier layer is a Chinese local egg-laying breed that has yellow feathers, a yellow beak, yellow feet, and white ears. Adult weights are 1,450 g for the cock and 1,190 g for the hen. Six broilers and 6 Baier layers were slaughtered at 2, 6, and 12 wk of age (3 of each sex), respectively, and leg muscle, breast muscle, abdominal fat, liver, heart, intestine (jejunum part), glandular stomach, and brain samples were harvested at 2 wk of age. In addition, kidney and ovaries (female) were taken at 6 and 12 wk of age, and lung, spleen, muscular stomach, and testicles (male) were also taken at 12 wk of age. All the tissues harvested were stored at –80°C until use.

A China Agricultural University (CAU) F2 population was used for association analysis between growth and body composition traits and the L-FABP gene in the current study. The CAU F2 population was established by crossing broilers with silkies. Unrelated F1 birds were mated (1 sire to 5 dams) to produce 33 half-sib families with an average of 75 F2 offspring per family in 6 hatches. The 445 F2 individuals, including males and females produced from 4 reciprocal F1 families, were sampled for the current study. Birds had free access to feed and water. Commercial corn-soybean-based diets that met all NRC (1994) requirements were provided in the study. From hatch to 3 wk of age, birds received a starter feed (3,000 kcal of ME/kg and 210 g/kg of CP), and from 3 to 12 wk of age, birds were fed a grower diet (3,100 kcal of ME/kg and 190 g/kg of CP). Body weight was measured at hatch and weekly up to 12 wk of age. Body composition traits were recorded at 12 wk of age. These measurements included pectoralis major weight, leg muscle weight, abdominal fat weight (AFW), and liver weight. All the traits were also expressed as percentage of BW at 12 wk of age.

DNA and RNA Extraction and cDNA Synthesis
Genomic DNA was extracted using phenol-chloroform from venous blood collected in EDTA-Na2-coated tubes and was stored at –20°C. The RNA was extracted with the Trizol reagent (Invitrogen, Rockville, MD) according to the instructions of the manufacturer from each tissue at different weeks of age, then was resuspended in diethyl pyrocarbonate-treated water. The reverse transcription reactions were carried out using the Takara RNA PCR Kit, Version 2.1 (Takara Biotechnology Co. Ltd., Dalian, China). The reverse transcription reaction contained 1 µg of total RNA derived from the liver tissue of 3 broilers and 3 Baier layers in a final volume of 20 µL, respectively.

Northern Blot Analysis
Total RNA (15 µg of each sample) isolated from the different tissues of chickens at 2, 6, and 12 wk of age was electrophoresed and transferred to nylon membranes. A 390-bp L-FABP cDNA fragment was used as probe after labeling by random priming with [{alpha}32P]dCTP (3000 Ci.mmol–1)2, which was obtained using primers LFF1 (5'-TCA CTG GAA AGT ACG AGC -3') and LFR1 (5'-GCA TGC AGG GTC TCT AGA TT-3'), according to the chicken L-FABP gene sequence(Genbank accession no. AF380999 [GenBank] ). The expression of the chicken glyceraldehyde-3-phosphate dehydrogenase (GAPDH) gene was used as a control. A 491-bp fragment was used as probe after labeling by random priming with [{alpha}32P]dCTP (3000 Ci.mmol–1)2, which was obtained using primers GF (5'-TGA CGT GCA GCA GGA ACA C-3') and GR (5'-CAG TTG GTG GTG CAC GAT G -3'), according to the chicken GAPDH gene sequence(Genbank accession no. K01458 [GenBank] ). The ribosomal RNA (5-, 18-, and 28S) markers were used as standards for calculation of the transcript size. The membrane was prehybridized at 42°C in ULTRAhyb (Ambion, Austin, TX) for 60 min, and then the denatured probe (95°C for 10 min) was added at a concentration of 1 x 106 cpm/mL to hybridize with the targeted mRNA transcript overnight at 42°C. Following hybridization, the membrane was washed twice in 2 x SSC (300 mM NaCl and 30 mM Na citrate, at pH 7.0) containing 0.1% Na dodecyl sulfate for 15 min at 42°C and twice in 0.2 x SSC containing 0.1% Na dodecyl sulfate for 5 min and 15 min, respectively. The membrane was dried in air then radioautography. The bands were analyzed with the Laboratory Imaging and Analysis System (UVP Inc. Upland, CA).

DNA Sequencing of Chicken L-FABP Gene
One fragment of 390 bp including coding sequence and another fragment of 1,086 bp including the 5' upstream region of chicken L-FABP gene were amplified. Primers for coding region amplification were LFF1 (5'-TCA CTG GAA AGT ACG AGC-3') and LFR1 (5'-GCA TGC AGG GTC TCT AGA TT-3'), and the primers for 5' upstream region amplification were LFF2 (5'-AAC TTC GGG AGA TGT CAA CA-3') and LFR2 (5'-TTC ATG GGA CTG GAG CTC GTA C-3'). The PCR components were 1 x PCR reaction buffer (10 mM Tris-HCl, 50 mM KCl, and 1.5 mM MgCl2, pH 8.3), 200 µM each deoxynucleotide triphosphate, 0.25 µM each primer, 2 µL of cDNA (for the coding sequence) or 50 ng of DNA (for the 5' upstream region), and 1 U of Taq DNA polymerase (TaKaRa Biotechnology Co. Ltd., Dalian, China) in a final volume of 25 µL. The thermal cycling was 94°C for 5 min, followed by 30 cycles of 94°C for 50 s, 54°C for 1 min (for the coding sequence) or 56°C for 1 min (for the 5' upstream region), and 72°C for 1 min. The PCR products were purified by Gel Extraction Mini Kit (Watson Biotechnologies Inc., Shanghai, China) and then sequenced in forward and reverse directions with an ABI 3730 sequencer (BioAsia Biotechnology Co. Ltd., Shanghai, China). Restriction enzyme sites in these sequences were detected by the DNAMAN package, Version 4.0 (Lynnon BioSoft, Vaudreuil-Dorion, Quebec, Canada).

Genotyping of Chicken L-FABP Gene
Polymorphisms of the L-FABP gene 5' upstream regions were genotyped by the PCR single-strand conformation polymorphisms (SSCP) method. A genomic fragment of 196 bp responsible for the polymorphism sites of the L-FABP gene was amplified by using primers LFF3 (5'-CAT TTG TTT ATG GAT GCC ACG-3') and LFR3 (5'-TAA GGA CCT TTT GCC CTA A-3'). The PCR components included 1 x PCR reaction buffer, 200 µM each deoxynucleotide triphosphate, 0.25 µM each primer, 1 µL of genomic DNA (50 ng/µL), and 0.5 U of Taq DNA polymerase in a final volume of 10 µL. The thermal profiles were 94°C for 5 min, followed by 32 cycles of 94°C for 30 s, 58°C for 30 s, and 72°C for 30 s. One microliter of the PCR products was mixed with 5 µL of loading buffer (98% formamide, 0.025% bromophenol blue, 0.025% xylene cyanol, 10 mM EDTA, and 10% glycerol) after PCR according to the above, then the mixture was denatured in 98°C for 10 min, placed on ice for 5 min, and a silver stain method was developed to display the bands. Individual PCR-SSCP band patterns were determined by a 14% polyacrylamide gel with 5% glycerol electrophoresis for 8 to 9 h at 10 V/cm and silver nitrate staining under visible light.

Statistical Analysis
Data of differential expression of the chicken L-FABP gene between 2 breeds were analyzed by the t-test of SAS 6.12 (SAS Institute Inc., Cary, NC). Data of individual genotypes were subjected to the GLM procedures of JMP (SAS Institute Inc.) with the genotype and sex as fixed effects and hatch, family, and dam as random effects, according to the model


Formula

where Y = the dependent variable; µ = population mean; G = genotype; S = sex; h = hatch; f = family; d = dam; and e = the random error. The interaction G by S was not significant for any traits and therefore was not included in the model. Statistical significance threshold was P < 0.05, unless otherwise specified.


   RESULTS
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS AND METHODS
 RESULTS
DISCUSSION
 REFERENCES
 
Tissue Expression Pattern of Chicken L-FABP Gene
Northern blot analysis with pool RNA from 3 males and 3 females indicated that 2 transcripts of approximately 2.5 and 0.8 kb for the L-FABP gene were clearly visible. The chicken L-FABP gene was expressed only in liver and intestine among all the tissues tested from chickens at 2, 6, and 12 wk of age (Figure 1Go).


Figure 1
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  		Figure 1. Northern blot of the chicken liver fatty acid-binding protein in different tissues at 2 (panel A), 6 (panel B), and 12 (panel C) wk of age. L = liver; T = testis; B = brain; I = intestine; K = kidney; S = spleen; Lu = lung; H = heart; MS = muscle stomach; GS = gland stomach; LM = leg muscle; BM = breast muscle; O = ovary; and F = fat.

 
Differential Expression of Chicken L-FABP Gene Between 2 Breeds
The quantification of L-FABP mRNA levels expressed relative to GAPDH mRNA in liver and intestinal tissues were investigated with 18 male birds from the 2 breeds. Northern blot analysis indicated that the L-FABP mRNA levels of the Baier layers were higher (P < 0.05) than those of broilers in liver at 6 and 12 wk of age (Figure 2Go) and in intestine at 6 wk of age (Figure 3Go).


Figure 2
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  		Figure 2. Hepatic expression of liver fatty acid-binding protein (L-FABP) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) genes evaluated by northern blot. Northern blot of L-FABP in liver tissue of 2-, 6-, and 12-wk-old broiler and Baier layers (panel A). 2B = 2-wk-old broiler; 2L = 2-wk-old Baier layer; 6B = 6-wk-old broiler; 6L = 6-wk-old Baier layer; 12B = 12-wk-old broiler; and 12L = 12-wk-old Baier layer. Quantitative analysis of L-FABP in liver tissue of 2-, 6-, and 12-wk-old broiler and Baier layers (panel B). B = broiler; L = Baier layer. Double asterisks (**) indicate significant difference (P < 0.01).

 

Figure 3
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  		Figure 3. Intestinal expression of liver fatty acid-binding protein (L-FABP) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) genes evaluated by northern blot. Northern Blot of L-FABP in intestinal tissue of 2-, 6-, and 12-wk-old broiler and Baier layers (panel A). 2B = 2-wk-old broiler; 2L = 2-wk-old Baier layer; 6B = 6-wk-old broiler; 6L = 6-wk-old Baier layer; 12B = 12-wk-old broiler; and 12L = 12-wk-old Baier layer. Quantitative analysis of L-FABP in intestinal tissue of 2-, 6-, and 12-wk-old broiler and Baier layers (panel B). B = broiler; L = Baier layer. Double asterisks (**) indicate significant difference (P < 0.01).

 
Identification of Polymorphism and PCR-SSCP Analysis
All of the coding sequence and the 5' upstream region of the chicken L-FABP gene had been amplified successfully by using either cDNA or genomic DNA samples. Sequence alignment of the chicken L-FABP sequences revealed that there was no polymorphism in the coding region. However, 2 novel mutations were found at base 204 and 205 upstream of the ATG initiation codon of the L-FABP gene. There was a G to A substitution at position 204 and a T to C substitution at position 205. The results of SSCP showed that there were 6 genotypes in the F2 offspring, named AA, BB, CC, AB, AC, and BC, respectively (Figure 4Go). Three kinds of homozygote individuals (AA, BB, and CC) had been sequenced respectively. The sequence of the AA genotype was TG, BB genotype was CA, and CC genotype was CG in the 2 mutations (Figure 5Go). The result of the motif search for nucleotides showed that the mutations had not changed protein-binding sites or the transcript start site for the chicken L-FABP gene.


Figure 4
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  		Figure 4. Polymerase chain reaction single-strand conformation polymorphisms pattern for the liver fatty acid-binding protein gene.

 

Figure 5
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  		Figure 5. Sequence comparison of different genotypes in the chicken liver fatty acid-binding protein gene.

 
Association of L-FABP Gene Polymorphisms with Growth and Body Composition
The genotypes based on the 2 mutations of the chicken L-FABP gene were used in the genetic analysis of the population. There was a significant association (P < 0.05) between the polymorphisms and fatness traits (AFW and percentage of AFW) in F2 birds of the CAU F2 population (Table 1Go).


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  		Table 1. Effects (P-value) of liver fatty acid-binding protein (L-FABP) polymorphisms on chicken growth and body composition traits
 
Effects (least square means) of the L-FABP genotypes on fatness traits in F2 offspring of the CAU F2 population are shown in Table 2Go. The AFW was lower (P < 0.05) in F2 birds of the CC genotype than of the AA, AB, AC, BB, and BC genotypes. The percentage of AFW in F2 birds was lower in the CC genotype than in the AA, AB, and AC genotypes.


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  		Table 2. Effects (least square means) of liver fatty acid-binding protein (L-FABP) genotype on body composition traits in the China Agricultural University (CAU) F2 population
 

   DISCUSSION
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS AND METHODS
 RESULTS
 DISCUSSION
REFERENCES
 
The chicken L-FABP gene was expressed only in liver and intestine tissues and existed in 2 transcripts, which was similar to that previously reported in rats or humans (Veerkamp et al., 1991; Schroeder et al., 1998). These results suggest that the function of the chicken L-FABP gene may be similar to that of the mammalian L-FABP gene mammals and play an important role in lipid metabolism.

Microarray analysis of liver genes indicated that L-FABP gene expression was higher (1.66-fold) in the hyperthyroid (triiodothyronine-treated and lean) chickens than in the hypothyroid (propylthiouracil-treated and fat) chickens (Wang et al., 2002; Cogburn et al., 2003). The current results showed that mRNA levels of chicken L-FABP were different between breeds at 6 to 12 wk of age in liver tissue, with the Baier layers having higher levels than broilers. The broilers were derived from a founder meat-type chicken population and had been selected for abdominal fatness at 7 wk of age for 7 generations. The Baier layer is a Chinese local breed chicken. Lipid metabolism is obviously different between these 2 breeds. The AFW and percentage of AFW of the broilers were 17-and 4-fold than those of Baier layers at 12 wk of age, respectively (unpublished data). Liver is an important organ for lipid metabolism in the avian species. The higher expression of the L-FABP gene in the livers of the Baier layers than in the broilers might result in increased fatty acids transportation into mitochondria or peroxisomes and enhanced fatty acids oxidation and reduced depot fat. So the differential expression of the L-FABP gene could have an effect on fat deposition in the chicken.

In addition, the current results showed the polymorphisms of the 5' upstream region of the L-FABP gene were related (P < 0.05) with AFW and percentage of AFW at 12 wk of age in the CAU F2 population. In an F2 cross among outbred lines, however, the linkage disequilibrium was substantial, and the associations of the L-FABP polymorphisms with AFW and percentage of AFW in the F2 population might have been produced by linkage disequilibrium between the L-FABP polymorphisms and another mutation in the L-FABP locus or another linked gene directly involved in the regulation of these phenotypic traits. As it currently stands, there was some hint that the L-FABP gene may be associated with fat traits, but this was tentative and difficult to assess with the current information.

Based on tissue distribution and differential expression of the chicken L-FABP gene, the current results will allow L-FABP gene assessment as an important candidate gene in chicken QTL detection programs focusing on phenotypes related to fat traits.


   ACKNOWLEDGMENTS
 
We thank the members of the Poultry Farm located at Northeast Agricultural University for managing the birds. We also thank Xuemei Deng, Zhiquan Tang, and other coworkers.


   FOOTNOTES
 
1 This research was supported by the National Natural Science Foundation Key Project (no.30430510) and Program for New Century Excellent Talents in University (no. NCET-04-0343). Back

Received for publication April 21, 2006. Accepted for publication June 26, 2006.


   REFERENCES
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS AND METHODS
 RESULTS
 DISCUSSION
 REFERENCES
 
Atshaves, B. P., A. L. McIntosh, H. R. Payne, J. Mackie, A. B. Kier, and F. Schroeder. 2005. Effect of branched-chain fatty acid on lipid dynamics in mice lacking liver fatty acid binding protein gene. Am. J. Physiol. Cell Physiol. 288:C543–C558.[Abstract/Free Full Text]

Cogburn, L. A., X. Wang, W. Carre, L. Rejto, T. E. Porter, S. E. Aggrey, and J. Simon. 2003. Systems-wide chicken DNA microarrays, gene expression profiling, and discovery of functional genes. Poult. Sci. 82:939–951.[Abstract/Free Full Text]

Glatz, J. F., and J. H. Veerkamp. 1985. Intracellular fatty-acid binding proteins. Int. J. Biochem. 17:13–22.[ISI][Medline]

Griffin, H. 1996. Understanding genetic variation in fatness in chickens. Pages 35–38 in Annual Report 95–96. Roslin Institute, Edinburgh, UK.

Grinstead, G. F., J. M. Trzaskos, J. T. Billheimer, and J. L. Gaylor. 1983. Cytosolic modulators of activities of microsomal enzymes of cholesterol biosynthesis. Effects of Acyl-CoA inhibition and cytosolic Z-protein. Biochim. Biophys. Acta 751:41–51.[Medline]

Jennen, D. G. J., A. L. J. Vereijken, H. Bovenhuis, R. P. M. A. Crooijmans, A. Veenendaal, J. J. van der Poel, and M. A. M. Groenen. 2004. Detection and localization of quantitative trait loci affecting fatness in broilers. Poult. Sci. 83:295–301.[Abstract/Free Full Text]

Mallard, J., and M. Douaire. 1988. Strategies of selection for leanness in meat production. Pages 3–23 in Leanness in Domestic Birds: Genetic, Metabolic and Hormonal Aspects. B. Leclerq and C. C. Whitehead, ed. Butterworth-Heinemann, Oxford, UK.

Martin, G. G., B. P. Atshaves, A. L. McIntosh, J. T. Mackie, A. B. Kier, and F. Schroeder. 2006. Liver fatty acid binding protein gene ablation potentiates hepatic cholesterol accumulation in cholesterol-fed female mice. Am. J. Physiol. Gastrointest. Liver Physiol. 290:G36–G48.[Abstract/Free Full Text]

National Research Council. 1994. Nutrient Requirements of Poultry. Natl. Acad. Press, Washington, DC.

Ockner, R. K., J. A. Manning, R. B. Poppenhausen, and W. K. Ho. 1972. A binding protein for fatty acids in cytosol of intestinal mucosa, liver, myocardium and other tissues. Science 177:56–58.[Abstract/Free Full Text]

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Seneshaw, M., D. Klass, E. Preiss, G. Adler, N. Davidson, and M. Fuchs. 2005. Impaired hepatobiliary lipid metabolism in liver fatty acid binding protein 1 (FABP1). Knockout Mice. Z. Gastroenterol. 43:40. (Abstr.)

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Wang, X., W. Carre, L. Rejto, and L. A. Cogburn. 2002. Global gene expression profiling in liver of thyroid manipulated and/or growth hormone (GH) injected broiler chickens. Poult. Sci. 81(Suppl. 1):63. (Abstr)

Zimmerman, A. W., and J. H. Veerkamp. 2002. New insights into the structure and function of fatty acid-binding proteins. Cell. Mol. Life Sci. 59:1096–1116.[ISI][Medline]





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