Hostname: page-component-586b7cd67f-dlnhk Total loading time: 0 Render date: 2024-11-27T20:56:06.845Z Has data issue: false hasContentIssue false
  • English
  • Français

Feed restriction and genetic selection on the expression and activity of metabolism regulatory enzymes in rabbits

Published online by Cambridge University Press:  07 June 2010

S. van Harten  and
L. A. Cardoso
S. van Harten*
Affiliation:
Instituto de Investigação Científica Tropical, Lisboa, Portugal & Centro Interdisciplinar de Investigação em Sanidade Animal, Lisboa, Portugal
L. A. Cardoso
Affiliation:
Instituto de Investigação Científica Tropical, Lisboa, Portugal & Centro Interdisciplinar de Investigação em Sanidade Animal, Lisboa, Portugal
Get access

Abstract

This work aims at the identification of relevant intermediate metabolism enzymes contributing to improved meat production due to genetic selection. A wild rabbit (WR) breed and a highly meat selected breed (New Zealand (NZ) rabbit) were used. Food restriction was used as an experimental condition so as to enhance differences within the metabolic pathways under study. During a period of 30 days, NZ and WR experimental breeds were subjected to, respectively, 40% and 60% ad libitum food restriction leading to 17.7% and 21.1% initial weight. Hepatic glycolytic, lipidic and protein regulatory enzyme activity, transcriptional and metabolite levels were determined. Insulin-like growth factor (IGF-1), triiodothyronine, and cortisol were also evaluated. In the glycolytic pathways, the NZ control rabbits presented a higher phosphofructokinase and pyruvate kinase activity level when compared to the WR, while the latter group showed a higher expression of glycogen synthase, although with less glycogen content. In the nitrogen metabolism, our results showed a lower activity level of glutamate dehydrogenase in WR when subjected to food restriction. Within the lipid metabolism, results showed that although WR had a significantly higher mRNA hepatic lipase, non-esterified fatty acid levels were similar between the experimental groups. NZ rabbits presented a better glycemia control and greater energy substrate availability leading to enhanced productivities in which triiodothyronine and IGF-1 played a relevant role.

Keywords

enzyme activityintermediate metabolismrabbitsregulatory enzymesfeed restriction
Type
Full Paper
Information
animal , Volume 4 , Issue 11 , November 2010 , pp. 1873 - 1883
Copyright
Copyright © The Animal Consortium 2010

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

Bergmeyer, HU 1984. D-glucose 1-phosphate. In Methods of enzymatic analysis; metabolites 1: carbohydrates (ed. HU Bergmeyer, J Bergmeyer and M Grassl), pp. 185–191. Verlag Chemie, Weinheim, Germany.Google Scholar
Bradford, MM 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248–254.CrossRefGoogle ScholarPubMed
Cardenas, JM, Dyson, RD 1973. Bovine pyruvate kinases. II. Purification of the liver isozyme and its hybridization with skeletal muscle pyruvate kinase. The Journal of Biological Chemistry 248, 6938–6944.CrossRefGoogle ScholarPubMed
Carter, WJ, Dang, AQ, Faas, FH, Lynch, ME 1991. Effects of clenbuterol on skeletal muscle mass, body composition, and recovery from surgical stress in senescent rats. Metabolism: Clinical and Experimental 40, 855–860.CrossRefGoogle ScholarPubMed
Caseras, A, Metón, I, Fernández, F, Baanante, IV 2000. Glucokinase gene expression is nutritionally regulated in liver of gilthead sea bream (Sparus aurata). Biochimica et Biophysica Acta (BBA) – Gene Structure and Expression 1493, 135–141.CrossRefGoogle ScholarPubMed
Collins-Lusweti, E 2000. The performance of the Nguni, Afrikander and Bonsmara cattle breeds in developing areas of Southern Africa. South African Journal of Animal Science 30 (suppl. 1), 28–29.Google Scholar
Dewil, E, Darras, VM, Spencer, GSG, Lauterio, TJ, Decuypere, E 1999. The regulation of GH-dependent hormones and enzymes after feed restriction in dwarf and control chickens. Life Sciences 64, 1359–1371.CrossRefGoogle ScholarPubMed
Dhahbi, JM, Mote, PL, Wingo, J, Tillman, JB, Walford, RL, Spindler, SR 1999. Calories and aging alter gene expression for gluconeogenic, glycolytic, and nitrogen-metabolizing enzymes. American Journal of Physiology. Endocrinology and Metabolism 277, E352–E360.CrossRefGoogle ScholarPubMed
Dhahbi, JM, Mote, PL, Wingo, J, Rowley, BC, Cao, SX, Walford, RL, Spindler, SR 2001. Caloric restriction alters the feeding response of key metabolic enzyme genes. Mechanisms of Ageing and Development 122, 1033–1048.CrossRefGoogle ScholarPubMed
Easterby, JS, O’Brien, MJ 1973. Purification and properties of pig-heart hexokinase. European Journal of Biochemistry 38, 201–211.Google Scholar
Fiske, CH, Subbarow, Y 1925. The colorimetric determination of phosphorus. The Journal of Biological Chemistry 66, 375–400.CrossRefGoogle Scholar
Granner, D, Pilkis, S 1990. The genes of hepatic glucose metabolism. The Journal of Biological Chemistry 265, 10173–10176.CrossRefGoogle ScholarPubMed
Hagopian, K, Ramsey, JJ, Weindruch, R 2003. Influence of age and caloric restriction on liver glycolytic enzyme activities and metabolite concentrations in mice. Experimental Gerontology 38, 253–266.CrossRefGoogle ScholarPubMed
Hers, HG 1959. Etudes enzymatiques sur fragments hépatiques. Application à la classification des glycogénoses. Revue Internationale d’Hépatologie 9, 35–55.Google Scholar
Hornick, JL, Van Eenaeme, C, Gérard, O, Dufrasne, I, Istasse, L 2000. Mechanisms of reduced and compensatory growth. Domestic Animal Endocrinology 19, 121–132.CrossRefGoogle ScholarPubMed
Hotta, K, Nakajima, H, Yamasaki, T, Hamaguchi, T, Kuwajima, M, Noguchi, T, Tanaka, T, Kono, N, Tarui, S 1991. Rat-liver-type phosphofructokinase mRNA. Structure, tissue distribution and regulation. European Journal of Biochemistry 202, 293–298.CrossRefGoogle ScholarPubMed
Kirchner, S, Seixas, P, Kaushik, S, Panserat, S 2005. Effects of low protein intake on extra-hepatic gluconeogenic enzyme expression and peripheral glucose phosphorylation in rainbow trout (Oncorhynchus mykiss). Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 140, 333–340.Google Scholar
Lamprecht, W, Heinz, F 1984. D-glycerate 2-phosphate and phosphoenolpyruvate. In Methods of enzymatic analysis; metabolites 1: carbohydrates (ed. HU Bergmeyer, J Bergmeyer and M Grassl), pp. 555–560. Verlag Chemie, Weinheim, Germany.Google Scholar
Li, R-Y, Zhang, Q-H, Liu, Z, Qiao, J, Zhao, S-X, Shao, L, Xiao, H-S, Chen, J-L, Chen, M-D, Song, H-D 2006. Effect of short-term and long-term fasting on transcriptional regulation of metabolic genes in rat tissues. Biochemical and Biophysical Research Communications 344, 562–570.CrossRefGoogle ScholarPubMed
Massey, TH, JrDeal, WC 1973. Unusual, metabolite-dependent solubility properties of phosphofructokinase. The basis for a new and rapid purification from liver, kidney, and other tissues. The Journal of Biological Chemistry 248, 56–62.CrossRefGoogle ScholarPubMed
McDowell, RE 1972. Bases biológicas de la producción animal en zonas tropicales. Editorial Acribia, Zaragoza, Spain.Google Scholar
Meton, I, Fernandez, F, Baanante, IV 2003. Short- and long-term effects of refeeding on key enzyme activities in glycolysis-gluconeogenesis in the liver of gilthead seabream (Sparus aurata). Aquaculture 225, 99–107.CrossRefGoogle Scholar
Michal, G 1984a. D-fructose 1,6-biphosphate, dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. In Methods of enzymatic analysis; metabolites 1: carbohydrates (ed. HU Bergmeyer, J Bergmeyer and M Grassl), pp. 342–350. Verlag Chemie, Weinheim, Germany.Google Scholar
Michal, G 1984b. D-glucose 6-phosphate and D-fructose 6-phosphate. In Methods of enzymatic analysis; metabolites 1: carbohydrates (ed. HU Bergmeyer, J Bergmeyer and M Grassl), pp. 191–197. Verlag Chemie, Weinheim, Germany.Google Scholar
Nissim, I 1999. Newer aspects of glutamine/glutamate metabolism: the role of acute pH changes. American Journal of Physiology. Renal Physiology 277, F493–F497.CrossRefGoogle Scholar
Nur, T, Sela, I, Webster, NJG, Madar, Z 1995. Starvation and refeeding regulate glycogen synthase gene expression in rat liver at the posttranscriptional level. The Journal of Nutrition 125, 2457–2462.Google ScholarPubMed
Oku, H, Koizumi, N, Okumura, T, Kobayashi, T, Umino, T 2006. Molecular characterization of lipoprotein lipase, hepatic lipase and pancreatic lipase genes: effects of fasting and refeeding on their gene expression in red sea bream Pagrus major. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 145, 168–178.CrossRefGoogle ScholarPubMed
Pilkis, SJ, Claus, TH 1991. Hepatic gluconeogenesis/glycolysis: regulation and structure/function relationships of substrate cycle enzymes. Annual Review of Nutrition 11, 465–515.CrossRefGoogle ScholarPubMed
Plaitakis, A, Zaganas, I 2001. Regulation of human glutamate dehydrogenases: implications for glutamate, ammonia and energy metabolism in brain. Journal of Neuroscience Research 66, 899–908.CrossRefGoogle ScholarPubMed
Rej, R 1984. Oxaloacetate. In Methods of enzymatic analysis; metabolites 1: carbohydrates (ed. HU Bergmeyer, J Bergmeyer and M Grassl), pp. 59–67. Verlag Chemie, Weinheim, Germany.Google Scholar
Rhind, SM, McMillen, SR, Duff, E, Kyle, CE, Wright, S 2000. Effect of long-term feed restriction on seasonal endocrine changes in Soay sheep. Physiology & Behavior 71, 343–351.Google Scholar
Rommers, JM, Boiti, C, Brecchia, G, Meijerhof, R, Noordhuizen, JPTM, Decuypere, E, Kemp, B 2004. Metabolic adaptation and hormonal regulation in young rabbit does during long-term caloric restriction and subsequent compensatory growth. Animal Science 79, 255–264.CrossRefGoogle Scholar
Schmidt, E, Schmidt, FW 1984. Glutamate dehydrogenase. In Methods of enzymatic analysis (ed. HU Bergmeyer), pp. 216–227. Verlag Chemie, Weinheim, Germany.Google Scholar
Soengas, JL, Polakof, S, Chen, X, Sangiao-Alvarellos, S, Moon, TW 2006. Glucokinase and hexokinase expression and activities in rainbow trout tissues: changes with food deprivation and refeeding. American Journal of Physiology. Regulatory, Integrative and Comparative Physiology 291, R810–R821.CrossRefGoogle ScholarPubMed
Tanaka, A, Inoue, A, Takeguchi, A, Washizu, T, Bonkobara, M, Arai, T 2005. Comparison of expression of glucokinase gene and activities of enzymes related to glucose metabolism in livers between dog and cat. Veterinary Research Communications 29, 477–485.CrossRefGoogle ScholarPubMed
Tillman, JB, Dhahbi, JM, Mote, PL, Walford, RL, Spindler, SR 1996. Dietary calorie restriction in mice induces carbamyl phosphate synthetase I gene transcription tissue specifically. The Journal of Biological Chemistry 271, 3500–3506.CrossRefGoogle ScholarPubMed
Ugochukwu, NH, Figgers, CL 2006. Modulation of the flux patterns in carbohydrate metabolism in the livers of streptozoticin-induced diabetic rats by dietary caloric restriction. Pharmacological Research 54, 172–180.CrossRefGoogle ScholarPubMed
Van Handel, E 1965. Estimation of glycogen in small amounts of tissue. Analytical Biochemistry 11, 256–265.CrossRefGoogle ScholarPubMed
Williamson, G, Payne, WJA 1980. An introduction to animal husbandry in the tropics. Longman Group, New York, NY, USA.Google Scholar
Zhao, S, Fernald, RD 2005. Comprehensive algorithm for quantitative real-time polymerase chain reaction. Journal of Computational Biology 12, 1047–1064.CrossRefGoogle ScholarPubMed