Activity and Expression of Glutamate Oxaloacetate Transaminase during the Reproductive Cycle of a Fresh Water Fish Labeo rohita

Fisheries Science

Volumn 64, Issue 4, 1998, Pages 621-626

  Srivastava, Anand Shanker ^a   Oohara, Ichiro ^b   Suzuki, Tohru ^b   Singh, Surendra Nath ^a  

^a BANARAS HINDU UNIVERSITY   (India)

^b FISHERIES RESEARCH AGENCY   (Japan)

Author keywords

Aspartate aminotransferase; AspT; Fish; GOT; GPT; Isoenzymes; Reproductive cycle

Indexed keywords

EID: 0013186004     PISSN: 09199268     EISSN: None     Source Type: Journal    
DOI: 10.2331/fishsci.64.621     Document Type: Article

References (49)

1. P. P. Cohen: Transamination with purified enzyme preparations. J. Biol. Chem., 136, 565-584 (1940).
2. E. J. Shrawder and M. M. Carrion: Simultaneous isolation and characterization of chicken supernatant and mitochondrial isoenzyme of aspartate transaminase. J. Biol. Chem., 248, 2140-2146 (1973).
3. A. E. Braunstein and E. E. Snell: In "Transaminases" (ed. by P. Christen and D. E. Metzler) Wiley and Sons, New York, 1985, pp. 2-35.
4. A. J. L. Cooper and A. Meister: In "Transaminases" (ed. by P. Christen and D. E. Metzler) Willy and Sons, New York, 1985, pp. 534-563.
5. P. Christen, U. Graf-Hausner, F. Bossa, and S. Doonan: In "Transaminases" (ed. by P. Christen and D. E. Metzler) Willy and Sons, New York, 1985, pp. 173-185.
6. Y. Horio, H. Fukui, M. Taketoshi, T. Tanaka, and H. Wada: Induction of cytosolic aspartate aminotransferase by glucagon in primary cultured rat hepatocytes. Biochem. Biophys. Res. Commun., 153, 410-416 (1988).
7. S. Doonan, F. Martini, S. Angelaccio, S. Pascarella, D. Barra, and F. Bossa: The complete amino acid sequence of cytosolic and mitochondrial aspartate aminotransferase from horse heart, and inference on evolution of the isoenzymes. J. Mol. Evol., 23, 328-335 (1986).
8. P. J. Morin, G. S. Subramanian, and T. D. Gilmore: AAT1, a gene encoding a mitochondrial aspartate aminotransferase in Saccharomyces cerevisiae. Fish Physiol. Biochem., 1171, 211-214 (1992).
9. Y. Elgersma, C. W. T. Van Roermund, R. J. A. Wanders, and H. F. Tabak: Peroxisomal and mitochondrial carnitine acetyltransferase of Saccharomyces cerevisiae are encoded by a single gene. EMBO J., 14, 3472-3479 (1995).
10. S. E. Wilkie, R. Lambert, and M. J. Warren: Chloroplastic aspartate aminotransferase from Arabidopsis Thailand: an examination of the relationship between the structure of the gene and the spatial structure of the protein. Bichem. J., 319, 969-976 (1996).
11. N. Verleur, Y. Elgersma, C. W. T. Van Roermund, H. F. Tabak, and R. J. A. Wanders: Cytosolic aspartate aminotransferase encoded by the AAT2 gene is targeted to the peroxysomes in oleate-grown Saccharomyces cerevisiae. Eur. J. Biochem., 247, 972-980 (1997).
12. L. H. Bertland and N. O. Kaplan: Chicken heart soluble aspartate aminotransferase. Purification and properties. Biochemistry, 7(1), 134-142 (1968).
13. L. H. Bertland and N. O. Kaplan: Studies on the conformations of the multiple forms of chicken heart soluble aspartate aminotransferase. Biochemistry, 9(13), 2653-2665 (1970).
14. M. M. Carrion, C. Turano, E. Chiancone, F. Bossa, A. Giartosio, F. Riva, and P. Fasella: Isolation and characterization of multiple forms of glutamate aspartate aminotransferase from pig heart. J. Biol. Chem., 242, 2397-2409 (1967).
15. C. M. Michuda and M. M. Carrion: Distinctions in the equilibrium kinetic constant of the mitochondrial and supernatant isoenzymes of aspartate transaminase. J. Biol. Chem., 244, 5920-5927 (1969).
16. C. M. Michuda and M. M. Carrion: The isoenzymes of glutamate-aspartate transaminase. Mechanism of inhibition of dicarboxylic acids. J. Biol. Chem., 245, 262-269 (1970).
17. D. G. Butler: Structure and function of adrenal gland of fishes. Am. Zool., 13, 839-879 (1973).
18. L. C. Folmer and W. Dickhoff: The parr-smolt transformation (smoltification) and sea water adaptation in salmonids. A review of selected literature. Aquaculture, 21, 1-37 (1980).
19. C. Setoyama, S. Ding, B. K. Choudhury, T. Joh, H. Takeshima, T. Suzuki, and K. Shimada: Regulatory regions of the mitochondrial and cytosolic isoenzymes genes participating in the malate-aspartate shuttle. J. Biol. Chem., 265, 1293-1299 (1990).
20. S. Feilleux-Duche, M. Garlatti, M. Aggerbeck, J. Bauguet, J. Hanoune, and R. Barouki: Phorbal esterase inhibit the glucocorticoid mediated stimulation of cytosolic aspartate aminotransferase gene transcription. J. Biochem., 297, 497-502 (1994).
21. T. Inubushi, M. Shikiji, K. Endo, H. Kakegawa, Y. Kishino, and N. Katunuma: Hormonal and dietary regulation of lysosomal cysteine proteinases in liver under gluconeogenesis conditions. Biol. Chem., 377, 539-542 (1996).
22. F. Abruzzese, M. Greco, E. Perlino, S. Doonan, and E. Marra: Lack of correlation between mRNA expression and enzymatic activity of the aspartate aminotransferase isoenzymes in various tissues of the rat. FEBS letters, 366, 170-172 (1995).
23. R. P. Wilson: Nitrogen metabolism in channel catfish Ictalurus panctatus-1. Tissue distribution of aspartate and alanine aminotransferase and glutamate dehydrogenase. Comp. Biochem. Physiol., 46B, 617-624 (1973).
24. R. P. Wilson, D. M. Gatlin, and W.E. Poe: Postprandial changes in serum amino acids of channel catfish fed diets containing different levels of protein and energy. Aquaculture, 49, 101-110 (1985).
25. M. N. Alex and E. P. Papoutsoglou: Aminotransferase activity in liver and white muscle of Mugil capito fed diets containing different levels of proteins and carbohydrates. Comp. Biochem. Physiol., 82B, 245-249 (1986).
26. G. D. Foster and T. W. Moon: Hypo metabolism with fasting in yellow perch (perca flavescans). A study of enzymes hepatocytes metabolism and tissue size. Physiol. Zool., 64, 259-275 (1991).
27. E. D. Marquez: A comparison of glutamic-oxaloacetate transaminase, lactate dehydrogenase, alpha-hydroxybutyrate dehydrogenase, and creatine phosphokinase activities in non-spawning, pre-spawning, and spawning pink salmon. Comp. Biochem. Physiol., 54B, 121-123 (1976).
28. C. Medda, B. Bhattacharyya, S. K. Sarkar, S. Ganguly, and T. K. Basu: Effect of rotenone on activity of some enzymes and their recovery in fresh water carp fingerlings of Labeo rohita. J. Environ. Biol., 16, 55-60 (1995).
29. C. F. Boyde and Hui: The release of aspartate transaminase from mitochondria by dilute ionic solutions. Biochem. Biophys. Res. Commun., 46, 231-236 (1972).
30. I. W. Sizer and W. T. Jenkins: Glutamic aspartic transaminase from pig ventricles. Methods in Enzymology, 5, 677-684 (1962).
31. O. H. Lowry, N. J. Rosenbrough, A. L. Farr, and R. J. Randall: Protein measurement with the folin phenol reagent. J. Biol. Chem., 193, 265-275 (1951).
32. R. Rej: Immunochemical quantitation of isoenzymes of aspartate aminotransferase and lactate dehydrogenase. Clin. Biochem., 16(1), 17-19 (1983).
33. M. Sarkar, P. R. Subbarayan, and M. Vinayaka: Transfer RNA analysis during the reproductive cycle of fresh water teleost Heteropneustes fossilis. Mol. Biol. Rep., 20, 9-13 (1994).
34. H. A. Krebs, A. H. Bennett, P. De Gasquit, T. Gascoyne, and T. Yoshida: The effect of diet on the gluconeogenic capacity of rat kidney cortex slices. J. Biochem., 86, 22-27 (1963).
35. G. De Rossa and R. W. Swick: Metabolic implications of the distribution of the alanine aminotransferase isoenzymes. J. Biol. Chem., 250, 7961-7967 (1975).
36. B. Masola, T. J. Peters, and D. F. Everd: Transamination pathways influencing L-glutamate and L-glutamate oxidation by rat erythrocytes mitochondria and sub cellular aspartate aminotransferase. Biochem. Biophys. Acta, 843, 137-143 (1985).
37. J. Kent, C. l. Prosser, and G. Graham: Alterations in liver composition of Channel catfish (Ictaluras puntatus) during seasonal acclimatization. Physio Zool., 65, 867-884 (1992).
38. J. Lin and G. N. Somero: Temperature dependent changes in expression of thermostable and thermolabile isoenzymes of cytosolic malate dehydrogenase in the eurythermal goby fish (Gillichtys mirabilis). Physiol. Zool., 68(1), 114-128 (1995).
39. M. Pave-Preux, N. Ferry, H. J. Bouguet, and R. barouki: Nucleotide sequence and glucocorticoid regulation of the mRNA for the isoenzymes of rat aspartate aminotransferase. J. Biol. Chem., 263, 17459-17466 (1988).
40. C. Toussaint, B. B. Lemercier, M. Garlatti, J. Hanoune, and R. Barouki: Testes specific transcription start site in the aspartate aminotransferase housekeeping gene promoter. J. Biol. Chem., 269, 13318-13324 (1994).
41. A. S. Srivastava, S. K. Trigun, and S. N. Singh: Activity of cytosolic and mitochondrial alanine aminotransferase during pre-spawning phase in air- breathing and non-air breathing fishes. J. Sci. Res., 47, 163-171 (1997).
42. W. R. Driedzic, B. D. Sidell, J. M. Stewart, and I. A. Johnston: Maximum activities of enzymes of energy metabolism in cephalopod systemic and branchial hearts. Physiol. Zool., 63, 615-629 (1990).
43. R. Balaza: Control of glutamate oxidation in brain and liver mitochondrial systems. J. Biochem., 95, 497-508 (1965).
44. N. Westergaard, T. Varming, L. Peng, U. Sonnewald, L. Hertz, and A. Schowsboe: Uptake, release and metabolism of alanine in neurons and astrocytes in primary cultures. J. Neurosci. Res., 35, 540-545 (1993).
45. B. Safer and R. Williamson: Mitochondrial-cytosolic interactions in perfused rat heart: Role of coupled transamination in regulation of citric acid cycle intermediates. J. Biol. Chem., 243, 2570-2579 (1973).
46. M. Erecinska, D. Nelson, I. Nissim, Y. Daikhin, and M. Yudkoff: Cerebral alanine transport and alanine aminotransferase reactions: Alanine as a source of neural glutamate. J. Neurochem., 62, 1953-1964 (1994).
47. K. Urich: Nutritional aspects of amino acid metabolism, In "Comparative Animal Biochemistry". Elsevier Press, Netherlands, 1994.
48. J. M. Doyle, M. E. Schinina, F. Bossa, and S. Doonan: The amino acid sequence of cytosolic aspartate aminotransferase from human liver. Biochem. J., 270, 651-657 (1990).
49. V. H. Cronin, B. Maras, D. Barra, and S. Doonan: The amino acid sequence of the aspartate aminotransferase from baker's yeast (Saccharomyces cervisiae). J. Biochem., 277, 335-340 (1991).