To gain insight on the impart of high-grain diets on liver metabolism in ruminants, we employed a comparative proteomic approach to investigate the proteome-wide effects of diet in lactating dairy goats by conducting a proteomic analysis of the liver extracts of 10 lactating goats fed either a control diet or a high-grain diet. More than 500 protein spots were detected per condition by two-dimensional electrophoresis (2-DE). In total, 52 differentially expressed spots (≥2.0-fold changed) were excised and analyzed using MALDI TOF/TOF. Fifty-one protein spots were successfully identified. Of these, 29 proteins were upregulated, while 22 were downregulated in the high-grain fed vs. control animals. Differential expressions of proteins including alpha enolase, elongation factor 2, calreticulin, cytochrome b5, apolipoprotein A-I, catalase, was verified by mRNA analysis and/or Western blotting. Database searches combined with Gene Ontology (GO) analysis and KEGG pathway analysis revealed that the high-grain diet resulted in altered expression of proteins related to amino acids metabolism. These results suggest new candidate proteins that may contribute to a better understanding of the signaling pathways and mechanisms that mediate liver adaptation to high-grain diet.
References
[1]
Emmanuel DG, Dunn SM, Ametaj BN (2008) Feeding high proportions of barley grain stimulates an inflammatory response in dairy cows. J Dairy Sci 91: 606–614.
[2]
Laino P, Shelton D, Finnie C, De Leonardis AM, Mastrangelo AM, et al. (2010) Comparative proteome analysis of metabolic proteins from seeds of durum wheat (cv. Svevo) subjected to heat stress. Proteomics 10: 2359–2368.
[3]
Durand TC, Sergeant K, Renaut J, Planchon S, Hoffmann L, et al. (2011) Poplar under drought: comparison of leaf and cambial proteomic responses. J Proteomics 74: 1396–1410.
[4]
Guo G, Ge P, Ma C, Li X, Lv D, et al. (2012) Comparative proteomic analysis of salt response proteins in seedling roots of two wheat varieties. J Proteomics 75: 1867–1885.
[5]
Wang Z, Tong W, Wang Q, Bai X, Chen Z, et al. (2012) The temperature dependent proteomic analysis of Thermotoga maritima. PLoS One 7: e46463.
[6]
El-Aneed A, Banoub J (2006) Proteomics in the diagnosis of hepatocellular carcinoma: focus on high risk hepatitis B and C patients. Anticancer Res 26: 3293–3300.
[7]
Parent R, Beretta L (2005) Proteomics in the study of liver pathology. J Hepatol 43: 177–183.
[8]
Fella K, Gluckmann M, Hellmann J, Karas M, Kramer PJ, et al. (2005) Use of two-dimensional gel electrophoresis in predictive toxicology: identification of potential early protein biomarkers in chemically induced hepatocarcinogenesis. Proteomics 5: 1914–1927.
[9]
Chen J, Tang X, Zhang Y, Ma H, Zou S (2010) Effects of maternal treatment of dehydroepiandrosterone (DHEA) on serum lipid profile and hepatic lipid metabolism-related gene expression in embryonic chickens. Comp Biochem Physiol B Biochem Mol Biol 155: 380–386.
[10]
Jianzhen H, Haitian M, Liming Y, Sixiang Z (2007) Developmental changes of protein profiles in the embryonic Sanhuang chicken liver. J Vet Med A Physiol Pathol Clin Med 54: 464–469.
[11]
Zeng T, Jiang X, Li J, Wang D, Li G, et al. (2013) Comparative Proteomic Analysis of the Hepatic Response to Heat Stress in Muscovy and Pekin Ducks: Insight into Thermal Tolerance Related to Energy Metabolism. PLoS One 8: e76917.
[12]
Katayama H, Nagasu T, Oda Y (2001) Improvement of in-gel digestion protocol for peptide mass fingerprinting by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 15: 1416–1421.
[13]
Chen J, Huang J, Deng J, Ma H, Zou S (2012) Use of comparative proteomics to identify the effects of creatine pyruvate on lipid and protein metabolism in broiler chickens. Vet J 193: 514–521.
[14]
Bondzio A, Gabler C, Badewien-Rentzsch B, Schulze P, Martens H, et al. (2011) Identification of differentially expressed proteins in ruminal epithelium in response to a concentrate-supplemented diet. Am J Physiol-Gastr L 301: G260–G268.
[15]
Zhang W, Miao J, Wang S, Zhang Y (2013) The protective effects of beta-casomorphin-7 against glucose -induced renal oxidative stress in vivo and vitro. PLoS One 8: e63472.
[16]
Huang da W, Sherman BT, Tan Q, Collins JR, Alvord WG, et al. (2007) The DAVID Gene Functional Classification Tool: a novel biological module-centric algorithm to functionally analyze large gene lists. Genome Biol 8: R183.
[17]
Gygi SP, Rochon Y, Franza BR, Aebersold R (1999) Correlation between protein and mRNA abundance in yeast. Mol Cell Biol 19: 1720–1730.
[18]
Nurten R, Bermek E (1980) Interactions of elongation factor 2 (EF-2) with guanine nucleotides and ribosomes. Binding of periodate-oxidized guanine nucleotides to EF-2. Eur J Biochem 103: 551–555.
[19]
Obeid M, Tesniere A, Panaretakis T, Tufi R, Joza N, et al. (2007) Ecto-calreticulin in immunogenic chemotherapy. Immunol Rev 220: 22–34.
[20]
Yan Q, Murphy-Ullrich JE, Song Y (2011) Molecular and structural insight into the role of key residues of thrombospondin-1 and calreticulin in thrombospondin-1-calreticulin binding. Biochemistry 50: 566–573.
[21]
Michalak M, Groenendyk J, Szabo E, Gold LI, Opas M (2009) Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem J 417: 651–666.
[22]
Wang WA, Groenendyk J, Michalak M (2012) Calreticulin signaling in health and disease. Int J Biochem Cell Biol 44: 842–846.
[23]
Gelebart P, Opas M, Michalak M (2005) Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum. Int J Biochem Cell Biol 37: 260–266.
[24]
Michalak M, Mariani P, Opas M (1998) Calreticulin, a multifunctional Ca2+ binding chaperone of the endoplasmic reticulum. Biochem Cell Biol 76: 779–785.
[25]
Ryu SY, Hong GU, Kim DY, Ro JY (2012) Enolase 1 and calreticulin regulate the differentiation and function of mouse mast cells. Cell Signal 24: 60–70.
[26]
Porter TD (2002) The roles of cytochrome b5 in cytochrome P450 reactions. J Biochem Mol Toxicol 16: 311–316.
[27]
Schenkman JB, Jansson I (2003) The many roles of cytochrome b5. Pharmacol Ther 97: 139–152.
[28]
Ladias J, Karathanasis SK (1991) Regulation of the apolipoprotein AI gene by ARP-1, a novel member of the steroid receptor superfamily. Science 251: 561.
[29]
Segrest JP, Jones MK, Dashti N (1999) N-terminal domain of apolipoprotein B has structural homology to lipovitellin and microsomal triglyceride transfer protein: a "lipid pocket" model for self-assembly of apob-containing lipoprotein particles. J Lipid Res 40: 1401–1416.
[30]
Pi J, Zhang Q, Fu J, Woods CG, Hou Y, et al. (2010) ROS signaling, oxidative stress and Nrf2 in pancreatic beta-cell function. Toxicol Appl Pharmacol 244: 77–83.
[31]
Endo T, Fujii T, Sato K, Taniguchi N, Fujii J (2000) A pivotal role of Zn-binding residues in the function of the copper chaperone for SOD1. Biochem Biophys Res Commun 276: 999–1004.
[32]
Orr AL, Quinlan CL, Perevoshchikova IV, Brand MD (2012) A refined analysis of superoxide production by mitochondrial sn-glycerol 3-phosphate dehydrogenase. J Biol Chem 287: 42921–42935.
[33]
Kanehisa M, Goto S (2000) KEGG: kyoto encyclopedia of genes and genomes. Nucleic Acids Res 28: 27–30.