Hostname: page-component-586b7cd67f-vdxz6 Total loading time: 0 Render date: 2024-11-23T03:44:22.509Z Has data issue: false hasContentIssue false
  • English
  • Français

Effect of diet composition and ration size on key enzyme activities of glycolysis–gluconeogenesis, the pentose phosphate pathway and amino acid metabolism in liver of gilthead sea bream (Sparus aurata)

Published online by Cambridge University Press:  09 March 2007

I. Metón ,
D. Mediavilla ,
A. Caseras ,
E. Cantó ,
F. Fernández  and
I. V. Baanante
I. Metón
Affiliation:
Departament de Bioquímica i Biologia Molecular, Facultat de Farmàcia, Universitat de Barcelona, Barcelona, Spain
D. Mediavilla
Affiliation:
Departament de Bioquímica i Biologia Molecular, Facultat de Farmàcia, Universitat de Barcelona, Barcelona, Spain
A. Caseras
Affiliation:
Departament de Bioquímica i Biologia Molecular, Facultat de Farmàcia, Universitat de Barcelona, Barcelona, Spain
E. Cantó
Affiliation:
Departament de Bioquímica i Biologia Molecular, Facultat de Farmàcia, Universitat de Barcelona, Barcelona, Spain
F. Fernández
Affiliation:
Departament d'Ecologia, Facultat de Biologia, Universitat de Barcelona, Barcelona, Spain
I. V. Baanante*
Affiliation:
Departament de Bioquímica i Biologia Molecular, Facultat de Farmàcia, Universitat de Barcelona, Barcelona, Spain
*
†Corresponding author: Dr Isabel V. Baanante, fax +34 3 402 1896, email [email protected]
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

The effects of diet composition and ration size on the activities of key enzymes involved in intermediary metabolism were studied in the liver of gilthead sea bream (Sparus aurata). High-carbohydrate, low-protein diets stimulated 6-phosphofructo 1-kinase (EC 2.7.1.11), pyruvate kinase (EC 2.7.1.40), glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (EC 1.1.1.44) enzyme activities, while they decreased alanine aminotransferase (EC 2.6.1.2) activity. A high degree of correlation was found between food ration size and the activity of the enzymes 6-phosphofructo 1-kinase, pyruvate kinase, glucose-6-phosphate dehydrogenase (positive correlations) and fructose-1,6-bisphosphatase (EC 3.1.3.11) (negative correlation). These correlations matched well with the high correlation also found between ration size and growth rate in starved fish refed for 22 d. Limited feeding (5 g/kg body weight) for 22 d decreased the activities of the key enzymes for glycolysis and lipogenesis, and alanine aminotransferase activity. The findings presented here indicate a high level of metabolic adaptation to both diet type and ration size. In particular, adaptation of enzyme activities to the consumption of a diet with a high carbohydrate level suggests that a carnivorous fish like Sparus aurata can tolerate partial replacement of protein by carbohydrate in the commercial diets supplied in culture. The relationship between enzyme activities, ration size and fish growth indicates that the enzymes quickly respond to dietary manipulations of cultured fish.

Keywords

Sparus aurataGlycolysisGluconeogenesisAmino acids
Type
Research Article
Information
British Journal of Nutrition , Volume 82 , Issue 3 , September 1999 , pp. 223 - 232
Copyright
Copyright © The Nutrition Society 1999

References

Alexis, MN & Papaparaskeva-Papoutsoglou, E (1986) Aminotransferase activity in the liver and white muscle of Mugil capito fed diets containing different levels of protein and carbohydrate. Comparative Biochemistry and Physiology 83B, 245–249.Google Scholar
Baanante, IV, García de Frutos, P, Bonamusa, L & Fernández, F (1991) Regulation of fish glycolysis–gluconeogenesis. Role of fructose 2,6-P2 and PFK-2. Comparative Biochemistry and Physiology 100B, 11–17.Google Scholar
Barroso, JB, García-Salguero, L, Peragón, J, de la Higuera, M, & Lupiáñez, JA (1993) Effects of long-term starvation on the NADPH production systems in several different tissues of rainbow trout (Oncorhynchus mykiss) In Fish Nutrition in Practice, pp. 333–338 [Kaushik, SJ and Luquet, P, editors]. Paris: INRA.Google Scholar
Bastrop, R, Jurss, K & Wacke, R (1992) Biochemical parameters as a measure of food availability and growth in immature rainbow trout (Oncorhynchus mykiss). Comparative Biochemistry and Physiology 102A, 151–161.CrossRefGoogle Scholar
Bonamusa, L, García de Frutos, P, Fernández, F & Baanante, IV (1989) Enzymes as indicators of nutritional conditions in the gilthead sea bream fish, Sparus aurata. In International Aquaculture Conference, Aquaculture Europe '89, p. 37 [Billard, R and De Pauw, N, editors]. Bredene, Belgium.Google Scholar
Bonamusa, L, García de Frutos, P, Fernández, F & Baanante, IV (1992) Nutritional effects on key glycolytic–gluconeogenic enzyme activities and metabolite levels in the liver of the teleost fish Sparus aurata. Molecular Marine Biology and Biotechnology 1, 113–125.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
Brauge, C, Medale, F & Corraze, G (1994) Effects of dietary carbohydrate levels on growth, body composition and glycaemia in rainbow trout, Oncorhynchus mykiss, reared in seawater. Aquaculture 123, 109–120.CrossRefGoogle Scholar
Christiansen, DC & Klungsøyr, L (1987) Metabolic utilization of nutrients and the effects of insulin in fish. Comparative Biochemistry and Physiology 88B, 701–711.Google Scholar
Cornell, NW, Stegelman, JJ, Kerich, MJ & Woodwin, BR (1986) Metabolite and enzyme contents of freeze-clamped liver of the marine fish Stenotomus chrysops. Comparative Biochemistry and Physiology 85B, 669–674.Google Scholar
Cowey, CB, Higuera, M & Adron, JW (1977 a) The effect of dietary composition and of insulin on gluconeogenesis in rainbow trout (Salmo gairdneri). British Journal of Nutrition 38, 385–395.CrossRefGoogle ScholarPubMed
Cowey, CB, Knox, D, Walton, MJ & Adron, JW (1977 b) The regulation of gluconeogenesis by diet and insulin in rainbow trout (Salmo gairdneri). British Journal of Nutrition 38, 463–470.CrossRefGoogle ScholarPubMed
Cowey, CB & Walton, MJ (1989) Intermediary metabolism. In Fish Nutrition, pp. 260–321 [Halver, JE, editor]. San Diego, CA: Academic Press.Google Scholar
Fideu, MD, Soler, G & Ruiz-Amil, M (1983) Nutritional regulation of glycolysis in rainbow trout (Salmo gairdneri R.). Comparative Biochemistry and Physiology 74B, 795–799.Google Scholar
French, CJ, Mommsen, TP & Hochachka, PW (1981) Amino acid utilization in isolated hepatocytes from rainbow trout. European Journal of Biochemistry 113, 311–317.CrossRefGoogle ScholarPubMed
Furuichi, M & Yone, Y (1981) The utilization of carbohydrate by fishes. 3. Changes of blood-sugar and plasma-insulin levels of fishes in glucose-tolerance test. Bulletin of the Japanese Society of Scientific Fisheries 47, 761–764.CrossRefGoogle Scholar
Fynn-Aikins, K, Hughes, SG & Vandenberg, GW (1995) Protein retention and liver aminotransferase activities in Atlantic salmon fed diets containing different energy sources. Comparative Biochemistry and Physiology 111A, 163–170.CrossRefGoogle Scholar
García de Frutos, P, Bonamusa, L & Baanante, IV (1991) Metabolic changes in fish liver during the starved-to-fed transition. Comparative Biochemistry and Physiology 98A, 329–331.CrossRefGoogle Scholar
García de Frutos, P, Bonamusa, L, Fernández, F & Baanante, IV (1990) Fructose 2,6-bisphosphate in liver of Sparus aurata. Comparative Biochemistry and Physiology 96B, 63–65.Google Scholar
Gehnrich, S, Gekakis, N & Sul, HS (1988) Liver (b-type) phosphofructokinase mRNA. Journal of Biological Chemistry 263, 11755–11759.CrossRefGoogle ScholarPubMed
Guderley, H & Cardenas, JM (1980) Pyruvate kinases of salmon: purification and comparison with the isozymes from birds and mammals. Journal of Experimental Zoology 211, 185–198.CrossRefGoogle ScholarPubMed
Hilton, JW & Atkinson, JL (1982) Response of rainbow trout (Salmo gairdneri) to increased levels of available carbohydrate in practical trout diets. British Journal of Nutrition 47, 597–607.CrossRefGoogle ScholarPubMed
Hue, L & Rider, MH (1987) Role of fructose 2,6-bisphosphate in the control of glycolysis in mammalian tissues. Biochemical Journal 245, 313–324.CrossRefGoogle ScholarPubMed
Hung, SSO, Conte, FS & Hallen, EF (1993) Effects of feeding rates on growth, body composition and nutrient metabolism in striped bass (Morone saxatilis) fingerlings. Aquaculture 112, 349–361.CrossRefGoogle Scholar
Iritani, N (1992) Nutritional and hormonal regulation of lipogenic-enzyme gene expression in rat liver. European Journal of Biochemistry 205, 433–442.CrossRefGoogle ScholarPubMed
Kim, KI, Grimshaw, TW, Kayes, TB & Amundson, CH (1992) Effect of fasting or feeding diets containing different levels of protein or amino acids on the activities of the liver amino acid-degrading enzymes and amino acid oxidation in rainbow trout (Oncorhynchus mykiss). Aquaculture 107, 89–105.CrossRefGoogle Scholar
Likimani, TA & Wilson, RP (1982) Effects of diet on lipogenic enzyme activities in channel catfish hepatic and adipose tissue. Journal of Nutrition 112, 112–117.CrossRefGoogle ScholarPubMed
Lin, H, Romsos, DR, Tack, PI & Leveille, GA (1977) Influence of dietary lipid on lipogenic enzyme activities in coho salmon (Oncorhynchus kisutch (Walbaum)). Journal of Nutrition 107, 846–854.CrossRefGoogle ScholarPubMed
Lupiáñez, JA, Sánchez-Lozano, MJ, García-Rejón, L & de la Higuera, M (1989) Long-term effect of a high-protein/non carbohydrate diet on the primary liver and kidney metabolism in rainbow trout (Salmo gairdneri). Aquaculture 79, 91–101.CrossRefGoogle Scholar
Metón, I (1996) Nutritional regulation of key enzymes in glycolysis–gluconeogenesis: expression of 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase gene in liver of Sparus aurata, pp. 92–93, 114–115. Barcelona: Doctoral Thesis, University of Barcelona.Google Scholar
Metón, I, Caseras, A, Mediavilla, D, Fernández, F & Baanante, IV (1999) Molecular cloning of a cDNA encoding 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase from liver of Sparus aurata: nutritional regulation of enzyme expression. Biochimica et Biophysica Acta 1444, 153–165.CrossRefGoogle ScholarPubMed
Metón, I, Mediavilla, D & Baanante, IV (1995) Automated assay for fructose 2,6-bisphosphate. Analytical Letters 28, 1919–1935.CrossRefGoogle Scholar
Moon, TW & Johnston, IA (1981) Amino acid transport and interconversions in tissues of freshly caught and food-deprived plaice, Pleuronectes platessa L. Journal of Fish Biology 19, 653–663.CrossRefGoogle Scholar
Nagai, M & Ikeda, S (1973 a) Carbohydrate metabolism in fish -III. Effect of dietary composition on metabolism of glucose-U-14C and glutamate-U-14C in carp. Bulletin of the Japanese Society of Scientific Fisheries 38, 137–143.CrossRefGoogle Scholar
Nagai, M & Ikeda, S (1973 b) Carbohydrate metabolism in fish-IV. Effect of dietary composition on metabolism of acetate-U-14C and l-alanine-U-14C in carp. Bulletin of the Japanese Society of Scientific Fisheries 39, 633–643.CrossRefGoogle Scholar
Noguchi, T, Inoue, H & Tanaka, T (1985) Transcriptional and posttranscriptional regulation of l-type pyruvate kinase in diabetic rat liver by insulin and dietary fructose. Journal of Biological Chemistry 260, 14393–14397.CrossRefGoogle ScholarPubMed
Pelletier, D, Dutil, JD, Blier, P & Guderley, H (1994) Relation between growth rate and metabolic organization of white muscle, liver and digestive tract in cod, Gadus morhua. Journal of Comparative Physiology 164B, 179–190.CrossRefGoogle Scholar
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
Roberts, B & Anderson, PJ (1985) The purification and kinetic characterization of eel white muscle pyruvate kinase. Comparative Biochemistry and Physiology 80B, 51–56.Google Scholar
Shimeno, S, Ming, DC & Takeda, M (1993) Metabolic response to dietary carbohydrate and lipid ratios in Oreochromis niloticus. Nippon Suisan Gakkaishi 59, 827–833.CrossRefGoogle Scholar
Shimeno, S, Shikata, T, Hosokavwa, H, Masumoto, T & Kheyyali, D (1997) Metabolic response to feeding rates in common carp, Cyprinus carpio. Aquaculture 151, 371–377.CrossRefGoogle Scholar
Stabile, LP, Klautky, SA, Minor, SM & Salati, LM (1998) Polyunsaturated fatty acids inhibit the expression of the glucose-6-phosphate dehydrogenase gene in primary rat hepatocytes by nuclear posttranscriptional mechanism. Journal of Lipid Research 39, 1951–1963.CrossRefGoogle ScholarPubMed
Steffens, W (1989) Principles of Fish Nutrition, pp. 66–183. Chichester: Ellis Horwood Ltd.Google Scholar
Suárez, MD, Hidalgo, MC García Gallego, M, Sanz, A & de la Higuera, M (1995) Influence of the relative proportions of energy yielding nutrients on liver intermediary metabolism of the European eel. Comparative Biochemistry and Physiology 111A, 421–428.CrossRefGoogle Scholar
Towle, HC, Kaytor, EN & Shih, H-M (1997) Regulation of the expression of lipogenic enzyme genes by carbohydrate. Annual Review of Nutrition 17, 405–433.CrossRefGoogle ScholarPubMed
Wilson, RP (1994) Utilization of dietary carbohydrate by fish. Aquaculture 124, 67–80.CrossRefGoogle Scholar
Windham, WR (1997) Animal feed. In Official Methods of Analysis, 16th ed., pp. 4.1–4.46 [Cunnif, P, editor]. Gaithersburg, MD: AOAC International.Google Scholar
Yamauchi, T, Stegeman, JJ & Goldberg, E (1975) The effects of starvation and temperature acclimation on pentose phosphate dehydrogenases in brook trout liver. Archives of Biochemistry and Biophysics 167, 13–20.CrossRefGoogle ScholarPubMed