Effect of Pyridoxine Deficiency on Ornithine Aminotransferase in Rat Kidney and Liver
The hepatic and renal activities of ornithine aminotrans-ferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female rats given diet with or without pyridoxine. OAT activities were measured in the presence of pyridoxal phosphate. Diet without pyridoxine caus...
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Published in | Journal of Nutritional Science and Vitaminology Vol. 31; no. 6; pp. 553 - 561 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Japan
Center for Academic Publications Japan
1985
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ISSN | 0301-4800 1881-7742 |
DOI | 10.3177/jnsv.31.553 |
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Abstract | The hepatic and renal activities of ornithine aminotrans-ferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female rats given diet with or without pyridoxine. OAT activities were measured in the presence of pyridoxal phosphate. Diet without pyridoxine caused a decrease in hepatic OAT activity in males and no change in females and an increase in renal OAT activity in males and a decrease in females. The increased renal OAT activity in males was associated with increased immunochemically recognizable OAT, and was due to increased synthesis of OAT as shown by measurement of [3H]leucine incorporation in vivo. Thus OAT is regulated by nutritional conditions in different ways in liver and kidney. |
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AbstractList | The hepatic and renal activities of ornithine aminotransferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female rats given diet with or without pyridoxine. OAT activities were measured in the presence of pyridoxal phosphate. Diet without pyridoxine caused a decrease in hepatic OAT activity in males and no change in females and an increase in renal OAT activity in males and a decrease in females. The increased renal OAT activity in males was associated with increased immunochemically recognizable OAT, and was due to increased synthesis of OAT as shown by measurement of [3H]leucine incorporation in vivo. Thus OAT is regulated by nutritional conditions in different ways in liver and kidney. The hepatic and renal activities of ornithine aminotrans-ferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female rats given diet with or without pyridoxine. OAT activities were measured in the presence of pyridoxal phosphate. Diet without pyridoxine caused a decrease in hepatic OAT activity in males and no change in females and an increase in renal OAT activity in males and a decrease in females. The increased renal OAT activity in males was associated with increased immunochemically recognizable OAT, and was due to increased synthesis of OAT as shown by measurement of [3H]leucine incorporation in vivo. Thus OAT is regulated by nutritional conditions in different ways in liver and kidney. The hepatic and renal activities of ornithine aminotransferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female rats given diet with or without pyridoxine. OAT activities were measured in the presence of pyridoxal phosphate. Diet without pyridoxine caused a decrease in hepatic OAT activity in males and no change in females and an increase in renal OAT activity in males and a decrease in females. The increased renal OAT activity in males was associated with increased immunochemically recognizable OAT, and was due to increased synthesis of OAT as shown by measurement of [3H]leucine incorporation in vivo. Thus OAT is regulated by nutritional conditions in different ways in liver and kidney.The hepatic and renal activities of ornithine aminotransferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female rats given diet with or without pyridoxine. OAT activities were measured in the presence of pyridoxal phosphate. Diet without pyridoxine caused a decrease in hepatic OAT activity in males and no change in females and an increase in renal OAT activity in males and a decrease in females. The increased renal OAT activity in males was associated with increased immunochemically recognizable OAT, and was due to increased synthesis of OAT as shown by measurement of [3H]leucine incorporation in vivo. Thus OAT is regulated by nutritional conditions in different ways in liver and kidney. |
Author | IKEDA, Masuko OKADA, Mitsuko |
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References | 2) Pitot, H. C., and Peraino, C. (1963): Ornithine b-transaminase in the rat. Biochim. Biophys. Acta, 73, 222-231. 27) Okada, M., and Hirose, M. (1982): Regulation of aspartate amino-transferase activity associated with change of pyridoxal phosphate level. Arch. Biochem. Biophys., 193, 294-300. 37) O'Malley, B. W., and Means, A. R. (1974): Female steroid hormones and target cell nuclei. Science, 183, 610-620. 45) Dolan, K. P., Diaz-Gil, J. J., and Litwack, G. (1980): Interaction of pyridoxal 5'-phosphate with the liver glucocorticoid receptor-DNA complex. Arch. Biochem. Biophys., 201, 476-485. 39) Muller, R. E., Traish, A., Wotiz, H. H. (1980): Effect of pyridoxal 5'-phosphate on uterine estrogen receptor. I. Inhibition of nuclear binding in cell-free system and intact uterus. J. Biol. Chem., 255, 4062-4067. 1) Katunuma, N., Matsuda, Y., and Tomino, I. (1964): Studies on ornithine-ketoacid transaminase. I. Purification and properties. J. Biochem., 56, 499-503. 33) Gornall, A. G., Bardawill, C. S., and David, M. M. (1949): Determination of serum proteins by means of the biuret reaction. J. Biol. Chem., 117, 751-766. 3) Herzfeld, A., and Knox, W. E. (1968): The properties, developmental formation, and estrogen induction of ornithine aminotransferase in rat tissues. ,1. Biol. Chem., 243, 3327-3332. 22) Mueckler, M., and Pitot, H. C. (1983): Regulation of ornithine aminotransferase mRNA levels in rat kidney by estrogen and thyroid hormone. J. Biol. Chem., 258, 6109-6114. 21) Wu, C. (1979): Estrogen receptor translocation and ornithine aminotransferase in- duction by estradiol in rat kidney. Biochem. Biophys. Res. Commun., 89, 769-776. 49) Kominami, E., and Katunuma, N. (1976): Studies on new intracellular proteases in various organs of rats. Participation of proteases in degradation of ornithine amino- transferase in vitro and in vivo. Eur. J. Biochem., 62, 425-430. 23) Takami, M., Fujioka, M., Wada, H., and Taguchi, T. (1968): Studies on pyridoxine deficiency in rats. Proc. Soc. Exp. Biol. Med., 129, 110-117. 31) Peraino, C., Bunville, L. G., and Tahmisian, T. N. (1969): Chemical, physical and morphological properties of ornithine aminotransferase from rat liver. J. Biol. Chem., 244, 2241-2249. 40) Traish, A., Muller, R. E., and Wotiz, H. H. (1980): Effect of pyridoxal 5'-phosphate on uterine estrogen receptor. II. Inhibition of estrogen receptor transformation. J. Biol. Chem., 255, 4068-4072. 17) Herzferd, A., and Greengard, O. (1969): Endocrine modification of the developmental formation of ornithine aminotransferase in rat tissues. J. Biol. Chem., 244, 4894-4898. 42) Mueller, R. E. Traish, A., and Wotiz, H. H. (1980): Effect of pyridoxal 5'-phosphate on estrogen receptor activation and nuclear binding. Prog. Cancer Res. Ther.,14, 241-254. 4) Lyons, R. T., and Pitot, H. C. (1976): The regulation of ornithine aminotransferase synthesis by glucagon in the rat. Arch. Biochem. Biophys., 174, 262-272. 32) Strecker, H. J. (1965): The interconversion of glutamic acid and proline. J. Biol. Chem., 240, 1225-1230. 35) Mueckler, M. M., Moran, S., and Pitot, H. C. (1983): Transcriptional control of ornithine aminotransferase synthesis in rat kidney by estrogen and thyroid hormone. J. Biol. Chem., 259, 2302-2305. 18) Kobayashi, K., Kito, K., and Katunuma, N. (1976): Effect of estrogen on the turn- over rates of ornithine aminotransferase in rat liver and kidney. J. Biochem., 79, 787- 793. 43) Cake, M. H., DiSorbo, D. M., and Litwack, G. (1978): Effect of pyridoxal phosphate on the DNA binding site of activated hepatic glucocorticoid receptor. J. Biol. Chem., 253, 4886-4891. 13) Bulfield, G., and Hall, J. M. (1981): Ornithine aminotransferase levels in rats and mice differ in their response to oestrogen and testosterone. Comp. Biochem. Physiol., 69B, 295-297. 9) Pitot, H. C., and Peraino, C. (1964): Studies on the induction and repression of enzymes in rat liver. I. Inductions of threonine dehydrase and ornithine-5-transaminase by oral intubation of casein hydrolysate. J. Biol. Chem., 239, 1783-1788. 10) Peraino, C., Blake, R. L., and Pitot, H. C. (1965): Studies on the induction and repression of enzymes in rat liver. III. Induction of ornithine-b-transaminase and threonine dehydrase by oral intubation of free amino acids. J. Biol. Chem., 240, 3039-3043. 8) Pitot, H. C., and Peraino, C. (1963): Carbohydrate repression of enzyme induction in rat liver. J. Biol. Chem., 238, 1910-1912. 34) Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951): Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265-275. 29) Kondo, T., Nagata, K., Shibuya, M., and Okada, M. (1982): Effect of pyridoxine deficiency on the synthesis of aspartate aminotransferase in rat liver and muscle in vivo. J. Biochem., 92, 1087-1091. 41) Muldoon, T. G., and Cidolowski, J. A. (1980): Specific modification of rat uterine estrogen receptor by pyridoxal 5'-phosphate. J. Biol. Chem., 255, 3100-3107. 19) Lyons, R. T., and Pitot, H. C. (1977): Hormonal regulation of ornithine aminotrans- ferase biosynthesis in rat liver and kidney. Arch. Biochem. Biophys., 180, 472-479. 44) DiSorbo, D. M., Pholps, D. S., Ohl, V. S., and Litwack, G. (1980): Pyridoxal deficiency influences the behavior of the glucocorticoid receptor complex. J. Biol. Chem., 255, 3866-3870. 6) Volpe, P., Menna, T., and Pagano, G. (1974): Ornithine-5-transaminase heterogeneity and regulation. Eur. I Biochem., 44, 455-458. 26) Hunter, J. E., and Happer, A. E. (1976): Stability of some pyridoxal phosphate-dependent enzymes in vitamine Bb deficient rats. J. Nutr., 106, 653-664. 30) Kuroda, K., Hirose, M., and Okada, M. (1982): Increase of inactive form of aspartate aminotransferase in pyridoxine-deficient rat liver. J. Biochem., 92, 1079-1085. 48) Itoh, R., and Okada, M. (1973): Effect of dietary protein level on pyridoxal content in tissues and excretion of pyridoxac acid into urine in normal or pyridoxine-deficient rat. J. Nutr. Sci. Vitaminol., 19, 523-528. 47) Cidlowski, J. A. and Thanassi, J. W. (1978): Extraction of nuclear glucocorticoid receptor complexes with pyridoxal phosphate. Biochem. Biophys. Res. Commun., 82, 1140-1146. 15) Pitot, H. C., and Peraino, C. (1964): Studies on the induction and repression of enzymes in rat liver. II. Carbohydrate repression of dietary and hormonal induction of threonine dehydrase and ornithine b-transaminase. J. Biol. Chem., 239, 4308-4313. 28) Shibuya, M., Nagata, K., and Okada, M. (1982): Effect of pyridoxine deficiency on activities and amounts of aspartate aminotransferase isozymes in rat tissues. J. Biochem., 92, 1399-1402. 14) Katunuma, N., Okada, M., Matsuzawa, J., and Otuka, Y. (1965): Studies on ornithine-ketoacid transaminase. II. Role in metabolic pathway. J. Biochem., 57, 445-449. 36) Jensen, E. V., and DeSombre, E. R. (1973): Estrogen receptor interaction. Science, 182, 126-134. 12) Chee, P. Y., and Swick, R. W. (1976): Effect of dietary protein and tryptophan on the turnover of rat liver ornithine aminotransferase. J. Biol. Chem., 251, 1029-1034. 25) Katunuma, N. (1971): Protein, Nucleic Acid and Enzyme (in Japanese), 16, 239-241. 11) Nakajima, K., and Matsuzaka, H. (1970): Hormonal and dietary control of enzymes in the rat. J. Biochem., 67, 779-787. 16) Hunter, J. E., and Harper, A. E. (1977): Induction of pyridoxal phosphate-dependent enzymes in vitamin B6 deficient rat. J. Nutr., 107, 235-244. 46) Cidlowski, J. A., and Thanassi, J. W. (1979): Pyridoxal phosphate induced alterations in glucocorticoid receptor conformation. Biochemistry, 18, 2378-2384. 20) Wu, C. (1978): Estrogen induction of ornithine aminotransferase in rat kidney slices. Biochem. Biophys. Res. Commun., 82, 782-786. 24) Okada, M., and Ochi, A. (1970): The effect of dietary protein level on transaminase activities and fat deposition in vitamin B6-depleted rat liver. J. Biochem., 79, 787-793. 38) Mueller, G. C., Vonderhaar, B., Kim, U. H., and Mahieu, M. L. (1971): Estrogen action: An inroad to cell biology. Recent. Progr. Horm. Res., 21, 1-45. 5) Sanada, Y., Suemori, I., and Katunuma, N. (1970): Properties of ornithine amino- transferase from rat liver, kidney and small intestine. Biochim. Biophys. Acta, 220, 42-50. 7) Kalita, C. C., Kerman, J. D., and Strecker, H. J. (1976): Preparation and properties of ornithine-oxo-acid aminotransferase of rat kidney. Biochim. Biophys. Acta, 429, 780-797. |
References_xml | – reference: 12) Chee, P. Y., and Swick, R. W. (1976): Effect of dietary protein and tryptophan on the turnover of rat liver ornithine aminotransferase. J. Biol. Chem., 251, 1029-1034. – reference: 2) Pitot, H. C., and Peraino, C. (1963): Ornithine b-transaminase in the rat. Biochim. Biophys. Acta, 73, 222-231. – reference: 40) Traish, A., Muller, R. E., and Wotiz, H. H. (1980): Effect of pyridoxal 5'-phosphate on uterine estrogen receptor. II. Inhibition of estrogen receptor transformation. J. Biol. Chem., 255, 4068-4072. – reference: 30) Kuroda, K., Hirose, M., and Okada, M. (1982): Increase of inactive form of aspartate aminotransferase in pyridoxine-deficient rat liver. J. Biochem., 92, 1079-1085. – reference: 44) DiSorbo, D. M., Pholps, D. S., Ohl, V. S., and Litwack, G. (1980): Pyridoxal deficiency influences the behavior of the glucocorticoid receptor complex. J. Biol. Chem., 255, 3866-3870. – reference: 43) Cake, M. H., DiSorbo, D. M., and Litwack, G. (1978): Effect of pyridoxal phosphate on the DNA binding site of activated hepatic glucocorticoid receptor. J. Biol. Chem., 253, 4886-4891. – reference: 29) Kondo, T., Nagata, K., Shibuya, M., and Okada, M. (1982): Effect of pyridoxine deficiency on the synthesis of aspartate aminotransferase in rat liver and muscle in vivo. J. Biochem., 92, 1087-1091. – reference: 28) Shibuya, M., Nagata, K., and Okada, M. (1982): Effect of pyridoxine deficiency on activities and amounts of aspartate aminotransferase isozymes in rat tissues. J. Biochem., 92, 1399-1402. – reference: 21) Wu, C. (1979): Estrogen receptor translocation and ornithine aminotransferase in- duction by estradiol in rat kidney. Biochem. Biophys. Res. Commun., 89, 769-776. – reference: 45) Dolan, K. P., Diaz-Gil, J. J., and Litwack, G. (1980): Interaction of pyridoxal 5'-phosphate with the liver glucocorticoid receptor-DNA complex. Arch. Biochem. Biophys., 201, 476-485. – reference: 33) Gornall, A. G., Bardawill, C. S., and David, M. M. (1949): Determination of serum proteins by means of the biuret reaction. J. Biol. Chem., 117, 751-766. – reference: 32) Strecker, H. J. (1965): The interconversion of glutamic acid and proline. J. Biol. Chem., 240, 1225-1230. – reference: 48) Itoh, R., and Okada, M. (1973): Effect of dietary protein level on pyridoxal content in tissues and excretion of pyridoxac acid into urine in normal or pyridoxine-deficient rat. J. Nutr. Sci. Vitaminol., 19, 523-528. – reference: 18) Kobayashi, K., Kito, K., and Katunuma, N. (1976): Effect of estrogen on the turn- over rates of ornithine aminotransferase in rat liver and kidney. J. Biochem., 79, 787- 793. – reference: 31) Peraino, C., Bunville, L. G., and Tahmisian, T. N. (1969): Chemical, physical and morphological properties of ornithine aminotransferase from rat liver. J. Biol. Chem., 244, 2241-2249. – reference: 5) Sanada, Y., Suemori, I., and Katunuma, N. (1970): Properties of ornithine amino- transferase from rat liver, kidney and small intestine. Biochim. Biophys. Acta, 220, 42-50. – reference: 36) Jensen, E. V., and DeSombre, E. R. (1973): Estrogen receptor interaction. Science, 182, 126-134. – reference: 4) Lyons, R. T., and Pitot, H. C. (1976): The regulation of ornithine aminotransferase synthesis by glucagon in the rat. Arch. Biochem. Biophys., 174, 262-272. – reference: 42) Mueller, R. E. Traish, A., and Wotiz, H. H. (1980): Effect of pyridoxal 5'-phosphate on estrogen receptor activation and nuclear binding. Prog. Cancer Res. Ther.,14, 241-254. – reference: 22) Mueckler, M., and Pitot, H. C. (1983): Regulation of ornithine aminotransferase mRNA levels in rat kidney by estrogen and thyroid hormone. J. Biol. Chem., 258, 6109-6114. – reference: 41) Muldoon, T. G., and Cidolowski, J. A. (1980): Specific modification of rat uterine estrogen receptor by pyridoxal 5'-phosphate. J. Biol. Chem., 255, 3100-3107. – reference: 46) Cidlowski, J. A., and Thanassi, J. W. (1979): Pyridoxal phosphate induced alterations in glucocorticoid receptor conformation. Biochemistry, 18, 2378-2384. – reference: 3) Herzfeld, A., and Knox, W. E. (1968): The properties, developmental formation, and estrogen induction of ornithine aminotransferase in rat tissues. ,1. Biol. Chem., 243, 3327-3332. – reference: 10) Peraino, C., Blake, R. L., and Pitot, H. C. (1965): Studies on the induction and repression of enzymes in rat liver. III. Induction of ornithine-b-transaminase and threonine dehydrase by oral intubation of free amino acids. J. Biol. Chem., 240, 3039-3043. – reference: 26) Hunter, J. E., and Happer, A. E. (1976): Stability of some pyridoxal phosphate-dependent enzymes in vitamine Bb deficient rats. J. Nutr., 106, 653-664. – reference: 13) Bulfield, G., and Hall, J. M. (1981): Ornithine aminotransferase levels in rats and mice differ in their response to oestrogen and testosterone. Comp. Biochem. Physiol., 69B, 295-297. – reference: 27) Okada, M., and Hirose, M. (1982): Regulation of aspartate amino-transferase activity associated with change of pyridoxal phosphate level. Arch. Biochem. Biophys., 193, 294-300. – reference: 39) Muller, R. E., Traish, A., Wotiz, H. H. (1980): Effect of pyridoxal 5'-phosphate on uterine estrogen receptor. I. Inhibition of nuclear binding in cell-free system and intact uterus. J. Biol. Chem., 255, 4062-4067. – reference: 16) Hunter, J. E., and Harper, A. E. (1977): Induction of pyridoxal phosphate-dependent enzymes in vitamin B6 deficient rat. J. Nutr., 107, 235-244. – reference: 25) Katunuma, N. (1971): Protein, Nucleic Acid and Enzyme (in Japanese), 16, 239-241. – reference: 14) Katunuma, N., Okada, M., Matsuzawa, J., and Otuka, Y. (1965): Studies on ornithine-ketoacid transaminase. II. Role in metabolic pathway. J. Biochem., 57, 445-449. – reference: 6) Volpe, P., Menna, T., and Pagano, G. (1974): Ornithine-5-transaminase heterogeneity and regulation. Eur. I Biochem., 44, 455-458. – reference: 34) Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951): Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265-275. – reference: 37) O'Malley, B. W., and Means, A. R. (1974): Female steroid hormones and target cell nuclei. Science, 183, 610-620. – reference: 17) Herzferd, A., and Greengard, O. (1969): Endocrine modification of the developmental formation of ornithine aminotransferase in rat tissues. J. Biol. Chem., 244, 4894-4898. – reference: 49) Kominami, E., and Katunuma, N. (1976): Studies on new intracellular proteases in various organs of rats. Participation of proteases in degradation of ornithine amino- transferase in vitro and in vivo. Eur. J. Biochem., 62, 425-430. – reference: 20) Wu, C. (1978): Estrogen induction of ornithine aminotransferase in rat kidney slices. Biochem. Biophys. Res. Commun., 82, 782-786. – reference: 24) Okada, M., and Ochi, A. (1970): The effect of dietary protein level on transaminase activities and fat deposition in vitamin B6-depleted rat liver. J. Biochem., 79, 787-793. – reference: 9) Pitot, H. C., and Peraino, C. (1964): Studies on the induction and repression of enzymes in rat liver. I. Inductions of threonine dehydrase and ornithine-5-transaminase by oral intubation of casein hydrolysate. J. Biol. Chem., 239, 1783-1788. – reference: 23) Takami, M., Fujioka, M., Wada, H., and Taguchi, T. (1968): Studies on pyridoxine deficiency in rats. Proc. Soc. Exp. Biol. Med., 129, 110-117. – reference: 11) Nakajima, K., and Matsuzaka, H. (1970): Hormonal and dietary control of enzymes in the rat. J. Biochem., 67, 779-787. – reference: 38) Mueller, G. C., Vonderhaar, B., Kim, U. H., and Mahieu, M. L. (1971): Estrogen action: An inroad to cell biology. Recent. Progr. Horm. Res., 21, 1-45. – reference: 7) Kalita, C. C., Kerman, J. D., and Strecker, H. J. (1976): Preparation and properties of ornithine-oxo-acid aminotransferase of rat kidney. Biochim. Biophys. Acta, 429, 780-797. – reference: 8) Pitot, H. C., and Peraino, C. (1963): Carbohydrate repression of enzyme induction in rat liver. J. Biol. Chem., 238, 1910-1912. – reference: 19) Lyons, R. T., and Pitot, H. C. (1977): Hormonal regulation of ornithine aminotrans- ferase biosynthesis in rat liver and kidney. Arch. Biochem. Biophys., 180, 472-479. – reference: 35) Mueckler, M. M., Moran, S., and Pitot, H. C. (1983): Transcriptional control of ornithine aminotransferase synthesis in rat kidney by estrogen and thyroid hormone. J. Biol. Chem., 259, 2302-2305. – reference: 15) Pitot, H. C., and Peraino, C. (1964): Studies on the induction and repression of enzymes in rat liver. II. Carbohydrate repression of dietary and hormonal induction of threonine dehydrase and ornithine b-transaminase. J. Biol. Chem., 239, 4308-4313. – reference: 1) Katunuma, N., Matsuda, Y., and Tomino, I. 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Snippet | The hepatic and renal activities of ornithine aminotrans-ferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female... The hepatic and renal activities of ornithine aminotransferase (OAT) [L-ornithine 2-oxoacid aminotransferase, EC 2.6.1.13] were determined in male and female... |
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SubjectTerms | Animals Antigens, Surface - analysis Female hepatic and renal OAT Kidney - enzymology Kidney - immunology Kidney - metabolism Liver - enzymology Liver - immunology Liver - metabolism Male Membrane Proteins Ornithine-Oxo-Acid Transaminase - metabolism Protein Biosynthesis Proteins - analysis pyridoxal phosphate pyridoxine deficiency Rats Rats, Inbred Strains Sex Factors sexual difference synthesis of OAT Transaminases - metabolism Vitamin B 6 Deficiency - enzymology |
Title | Effect of Pyridoxine Deficiency on Ornithine Aminotransferase in Rat Kidney and Liver |
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