Hostname: page-component-cd9895bd7-mkpzs Total loading time: 0 Render date: 2024-12-25T02:32:42.862Z Has data issue: false hasContentIssue false
  • English
  • Français

Expression of HMGR and corresponding cholesterol content in tissues of two pig breeds

Published online by Cambridge University Press:  01 October 2009

G.-F. Liu ,
W.-N. Fang ,
H.-C. Lin ,
X.-F. Wang ,
J.-L. Fu  and
A.-G. Wang
G.-F. Liu
Affiliation:
College of Animal Science and Technology, China Agricultural University, Beijing, 100193, China Key Laboratory of Animal Genetics and Breeding, Ministry of Agriculture, Beijing, 100193, China
W.-N. Fang
Affiliation:
College of Animal Science and Technology, China Agricultural University, Beijing, 100193, China
H.-C. Lin
Affiliation:
College of Animal Science and Technology, China Agricultural University, Beijing, 100193, China Institute of Animal Science and Veterinary Medicine, Shandong Academy of Agricultural Science, Jinan, 250100, China
X.-F. Wang
Affiliation:
Animal Husbandry & Veterinary Service Station, Beijing, 100107, China
J.-L. Fu*
Affiliation:
College of Animal Science and Technology, China Agricultural University, Beijing, 100193, China Key Laboratory of Animal Genetics and Breeding, Ministry of Agriculture, Beijing, 100193, China
A.-G. Wang*
Affiliation:
College of Animal Science and Technology, China Agricultural University, Beijing, 100193, China Key Laboratory of Animal Genetics and Breeding, Ministry of Agriculture, Beijing, 100193, China
*
E-mail: [email protected]
E-mail: [email protected]
Get access

Abstract

The 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) is an essential enzyme in cholesterol biosynthesis. To study the expression of HMGR and corresponding cholesterol content in liver, adipose and muscle, six Chinese local breed (Huai pig) and Landrace pigs were selected. The results indicated that significant differences of cholesterol content in adipose (P < 0.01), liver (P < 0.05) and muscle (P < 0.01) tissues were detected between pigs of differing genetic backgrounds. HMGR mRNA expression were noted for adipose, liver and muscle of the two vastly differing genetics. Moreover cholesterol content differed (P < 0.01) among tissues across breed. Likewise, HMGR mRNA expression was different between adipose and liver tissues, muscle and liver tissues in both breeds; however, no difference was noted between adipose and muscle tissues. Results from this study indicate that cholesterol content and HMGR mRNA expression are higher in Huai pig tissues suggesting this gene is expressed in a breed- and tissue-dependent manner in pigs. Understanding the causes of variation in HMGR gene expression may provide crucial information about cholesterol biosynthesis.

Keywords

3-hydroxy-3-methylglutaryl-CoA reductasecholesterolmRNA expressionpig
Type
Full Paper
Information
animal , Volume 3 , Issue 10 , October 2009 , pp. 1436 - 1441
Copyright
Copyright © The Animal Consortium 2009

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Baum, JA, Teng, H, Erdman, JW Jr, Weigel, RM, Klein, BP, Persky, VW, Freels, S, Surya, P, Bakhit, RM, Ramos, E, Shay, NF, Potter, SM 1998. Long-term intake of soy protein improves blood lipid profiles and increases mononuclear cell low-density-lipoprotein receptor messenger RNA in hypercholesterolemic, postmenopausal women. The American journal of Clinical Nutrition 68, 545–551.CrossRefGoogle ScholarPubMed
Dodds, WJ 1982. The pig model for biomedical research. Federation Proceeding 41, 247–256.Google Scholar
Dorado, M, Martin Gomez, EM, Jimenez-Colmenero, F, Masoud, TA 1999. Cholesterol and fat contents of Spanish commercial pork cuts. Meat Science 51, 321–323.CrossRefGoogle ScholarPubMed
Duckworth, PF, Vlahcevic, ZR, Studer, EJ, Gurley, EC, Heuman, DM, Beg, ZH, Hylemon, PB 1991. Effect of hydrophobic bile acid on 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity and mRNA levels in the rat. The Journal of Biological Chemistry 266, 9413–9418.CrossRefGoogle Scholar
Favy, DA, Lafarge, S, Rio, P, Vissac, C, Bignon, YJ, Bernard-Gallon, D 2000. Real-time PCR quantification of full-length and exon 11 spliced BRCA1 transcripts in human breast cancer cell lines. Biochemical and Biophysical Research Communications 274, 73–78.CrossRefGoogle ScholarPubMed
Fink, L, Seeger, W, Ermert, L, Hanze, J, Stahl, U, Grimminger, F, Kummer, W, Bohle, RM 1998. Real-time quantitative RT-PCR after laser-assisted cell picking. Nature Medicine 4, 1329–1333.CrossRefGoogle ScholarPubMed
Ha, SH, Kim, JB, Hwang, YS, Lee, SW 2003. Molecular characterization of three 3-hydroxy-3-methylglutaryl-CoA reductase genes including pathogen-induced Hmg2 from pepper (Capsicum annuum). Biochima Biophysica Acta 1625, 253–260.CrossRefGoogle Scholar
Harris, KB, Pond, WG, Mersmann, HJ, Smith, EO, Cross, HR, Savell, JW 2004. Evaluation of fat sources on cholesterol and lipoproteins using pigs selected for high or low serum cholesterol. Meat Science 66, 55–61.CrossRefGoogle ScholarPubMed
Humphries, SE, Tata, F, Henry, I, Barichard, F, Holm, M, Junien, C, Williamson, R 1985. The isolation, characterization, and chromosomal assignment of the gene for human hydroxyl 3-methylglutaryl coenzyme A reductase (HMG-CoA reductase). Human Genetics 71, 254–258.CrossRefGoogle Scholar
Istvan, ES, Deisenhofer, J 2000. The structure of the catalytic portion of human HMG-CoA reductase. Biochimica Biophysica Acta 1529, 9–18.CrossRefGoogle ScholarPubMed
Jiang, JH, Kai, GY, Cao, XY, Chen, FM, He, DN, Liu, Q 2006. Molecular cloning of a HMG-CoA reductase gene from Eucommia ulmoides Oliver. Bioscience Reports 26, 171–181.CrossRefGoogle ScholarPubMed
Lee, KT, Kim, DN, Thomas, WA 1986. Atherosclerosis in swine. CRC Press, Boca Raton, FL, USA.Google Scholar
Leveille, GA, Romsos, DR, Yeh, Y, O’Hea, EK 1975. Lipid biosynthesis in the chick. A consideration of site of synthesis, influence of diet and possible regulatory mechanisms. Poultry Science 54, 1075–1093.CrossRefGoogle Scholar
Lord, E, Murphy, BD, Desmarais, JA, Ledoux, S, Beaudry, D, Palin, MF 2006. Modulation of peroxisome proliferator-activated receptorδ and γtranscripts in swine endometrial tissue during early gestation. Reproduction 131, 929–942.CrossRefGoogle Scholar
Luskey, KL, Stevens, B 1985. Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved domains responsible for catalytic activity and sterol-regulated degradation. The Journal of Biological Chemistry 260, 10271–10277.CrossRefGoogle Scholar
Myant, NB 1990. Current approaches to the genetics of coronary heart disease (CHD) including an account of work done at Hammersmith Hospital. Bollettino della Società italiana di biologia sperimentale 66, 1015–1041.Google Scholar
Ness, GC 2003. Physiological and pharmacological regulation of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase. Current Medicinal Chemistry-Imunology, Endocrine & Metabolic Agents 3, 219–227.Google Scholar
Pond, WG, Mersmann, HJ, Young, LD 1986. Heritability of plasma cholesterol and triglyceride concentrations in swine. Proceedings of the Society for Experimental Biology and Medicine 182, 221–224.CrossRefGoogle ScholarPubMed
Rasmusseen, LM, Hanzen, PR, Nabipour, MT, Olesen, P, Kristiansen, MT, Ledet, T 2001. Diverse effects of inhibition of 3-hydroxy-3-methylglutaryl-CoA reductase on the expression of VCAM-1 and E-selectin in endothelial cells. The Biochemical Journal 360, 363–370.CrossRefGoogle Scholar
Sato, K, Ohuchi, A, Sook, SH, Toyomizu, M, Akiba, Y 2003. Changes in mRNA expression of 3-hydroxy-3-methylglutaryl coenzyme A reductase and cholesterol 7 alpha-hydroxylase in chickens. Biochimica Biophysica Acta 1630, 96–102.CrossRefGoogle Scholar
Scandinavian Simvastatin Survival Study 1994. Randomised trial of cholesterol lowering in 4444 patients with coronary heart disease: the Scandinavian Simvastatin Survival Study (4S). Lancet 344, 1383–1389.Google Scholar
Shepherd, J, Cobbe, SM, Ford, I, Isles, CG, Lorimer, AR, MacFarlane, PW, McKillop, JH, Packard, CJ 1995. Prevention of coronary heart disease with pravastatin in men with hypercholesterolemia. West of Scotland Coronary Prevention Study Group. The New England Journal of Medicine 333, 1301–1307.CrossRefGoogle ScholarPubMed
Simonet, WS, Ness, GC 1988. Transcriptional and post-transcriptional regulation of rat hepatic 3-hydroxy-3-methylglutaryl-CoA reductase by thyroid hormones. The Journal of Biological Chemistry 263, 12448–12453.CrossRefGoogle ScholarPubMed
Stanton, HC, Mersmann, HJ 1986. Swine in cardiovascular research. CRC Press, Boca Raton,FL, USA.Google Scholar
Sundaresan, S, Yang-Feng, TL, Francke, U 1989. Genes for HMG-CoA reductase and serotonin 1a receptor are on mouse chromosome 13. Somatic Cell and Molecular Genetics 15, 465–469.CrossRefGoogle ScholarPubMed
Tabas, I 2002. Cholesterol in health and disease. The Journal of Clinical Investigation 110, 583–590.CrossRefGoogle ScholarPubMed
The Lipid Research Clinics Coronary Primary Prevention Trial results (LRC-CPPT) 1984. II. The relationship of reduction in incidence of coronary heart disease to cholesterol lowering. The Journal of American Medical Association 251, 365–374.CrossRefGoogle Scholar
Tobert, JA 2003. Lovastatin and beyond: the history of the HMG-CoA reductase inhibitors. Nature Reviews Drug Discovery 2, 517–526.CrossRefGoogle ScholarPubMed
Use Bulletin 2 1997. ABI Prism 7700 Sequence Detection System. The Perkin Elmer Corporation, P/N 4303859 Rev. A, Stock No. 777802-001. Foster City, CA.Google Scholar
Van, TA, Van, GT, Scheek, LM, Groener, JE, Sassen, LM, Lamers, JM, Verdouw, PD 1991. Lipoprotein structure and metabolism during progression and regression of atherosclerosis in pigs fed with fish oil-derived fatty acids. Advances in Experimental Medicine and Biology 285, 417–421.Google Scholar
Wang, XF 2006. Molecular cloning, expression analysis, chromosome mapping and polymorphism analysis of porcine HMGR gene. PhD, China Agricultural University.Google Scholar