Summary
The activity of the hepatic enzyme tyrosine aminotransferase (TAT) is the sum of many diverse regulatory factors. These include the developmental stage of the animal, the hormonal and nutritional environment of the animal (or tissue culture cell), other extrinsic and intrinsic regulatory cycles and factors (including cytoplasmic substances), and chromatin structure. Although TAT is subject to a number of post- translational modifications, alterations in catalytic activity always parallel changes in enzyme amount. In a few instances this is due to a selective change in TAT degradation, but most are due to changes in the rate of aminotransferase synthesis. Recent studies have shown that TAT synthesis is generally directly correlated with the activity, and presumably amount, of the mRNA that codes for tyrosine aminotransferase.
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References
Tanaka, K. and Ichihara, A., 1975. Biochim. Biophys. Acta 399: 302–312.
Belarbi, A., Beck, G., Bergmann, C. and Bollack, C., 1979. FEBS Lett. 104: 5965
Ohisalo, J. J., Andersson, B. M., Viljanen, A. A. and Anderson, S. M., 1982. Biochem. J. 204: 621–622.
Hargrove, J. L. and Granner, D. K., 1982. Biosynthesis and Degradation of Tyrosine Aminotransferase. In: The Transaminases (Christen, P. and Metzler, D., eds.), Wiley In- terscience, in press.
Lin, E. C. C. and Knox, W. E., 1957. Biochim. Biophys. Acta 26: 85–88.
Pitot, H. C., Peraino, C., Morse, P. A., Jr. and Potter, V. A., 1964. Natl. Cancer Inst. Monogr. 13: 229–245.
Thompson, E. B., Tomkins, G. M. and Curran, J. F., 1966. Proc. Natl. Acad. Sci. U.S.A. 56: 296–303.
Kenney, F. T., 1967. J. Biol. Chem. 242: 4367–4371.
Holten, J. F. and Kenney, F. T., 1967. J. Biol. Chem. 242: 4372–4377.
Wicks, W. D., Kenney, F. T. and Lee, K-L., 1969. J. Biol. Chem. 244: 6008–6013.
Peraino, C., Lamar, C. Jr. and Pitot, H. C., 1966. Adv. Enz. Reg. 4: 199–217.
Yuwiler, A., Wetterberg, L. and Geller, E., 1970. Biochim. Biophys. Acta 208: 428–433.
Yanage, S., Campbell, H. A. and Potter, V. R., 1975. Life Sci. 17: 1411–1422.
Nakamura, T., Noda, C. and Ichihara, A., 1981. Biochem. Biophys. Res. Commun. 99: 775–780.
Spencer, C. J., Heaton, J. H., Gelehrter, T. D., Richard¬son, K. I. and Garwin, J. L., 1978. J. Biol. Chem. 251: 7677–7682.
Reel, J. R., Lee, K-L and Kenney, F. T., 1970. J. Biol. Chem. 245: 5800–5805.
Sereni, F., Kenney, F. T. and Kretchmer, N., 1959. J. Biol. Chem. 234: 609–612.
Watanabe, M., Potter, V. R. and Pitot, H. C., 1968. J. Nutr. 95: 207–227.
Nickol, J. M., Lee, K-L, Hollinger, T. G. and Kenney, F. T., 1976. Biochem. Biophys. Res. Commun. 72: 687–693.
Roewekamp, W. G., Hofer, E. and Sekeris, C. E., 1976. Eur. J. Biochem. 70: 259–268.
Diesterhaft, M., Noguchi, T., Hargrove, J., Thornton, C. and Granner, D. K., 1977. Biochem. Biophys. Res. Commun. 79: 1015–1022.
Ernest, M. J. and Feigelson, P., 1978. J. Biol. Chem. 253: 319–322.
Scherer, G., Schmid, W., Strange, C. M., Roewekamp, W. and Schutz, G., 1983. Proc. Natl. Acad. Sci. U.S.A., in press.
Wicks, W. D., Van Wijk, R. and McKibbin, J. B., 1973. Adv. Enz. Reg. 11: 117–135.
Wicks, W. D., 1974. Adv. Cycl. Nucl. Res. 4: 335–438.
Wicks, W. D., Barnett, C. A. and McKibbin, J. B., 1973. Fed. Proc. 33: 1105–1111.
Roper, M. D. and Wicks, W. D., 1978. Proc. Natl. Acad. Sci. U.S.A. 75: 140–144.
Snoek, G. T., Van De Poll, K. W., Voorma, H. O. and Van Wijk, R., 1981. Eur. J. Biochem. 114: 27–31.
Chuah, C. C. and Oliver, I. T., 1972. Biochemistry II: 2547–2553.
Noguchi, T., Diesterhaft, M. and Granner, D. K., 1982. J. Biol. Chem. 257: 2386–2390.
Kenney, F. T., 1962. J. Biol. Chem. 237: 3495–3498.
Granner, D. K., Thompson, E. B. and Tomkins, G. M., 1970. J. Biol. Chem. 245: 1472–1478.
Kenney, F. T., 1967. Science 156: 525–528.
Goldberg, A. L. and St. John, A. C., 1976. Ann. Rev. Biochem. 45: 747–803.
Kenney, F. T., 1962. J. Biol. Chem. 237: 1610–1614.
Iwasaki, Y., Lamar, C., Danenberg, K. and Pitot, H. C., 1973. Eur. J. Biochem. 34: 347–357.
Hargrove, J. L., Diesterhaft, M., Noguchi, T. and Granner, D. K., 1980. J. Biol. Chem. 255: 71–78.
Hargrove, J. L. and Granner, D. K., 1981. Anal. Biochem. 104: 231–235.
Lee, K-L., Roberson, L. E. and Kenney, F. T., 1979. Anal. Biochem. 95: 188–193.
Barth, R. K., Gross, K. W., Gremke, L. D. and Hastie, N. D., 1982. Proc. Natl. Acad. Sci. U.S.A. 79: 500–504.
Donner, P., Wagner, H. and Kroger, H., 1978. Biochem. Biophys. Res. Commun. 80: 766–772.
Wagner, H., Donner, P. and Kroger, H., 1980. Biochim. Biophys. Acta 609: 53–60.
Gohda, E. and Pitot, H. C., 1980. J. Biol. Chem. 255: 7371–7379.
Hargrove, J. L., Gohda, E., Pitot, H. C. and Granner, D. K., 1982. Biochemistry 21: 283–289.
Pelham, H. R. B. and Jackson, R. J., 1976. Eur. J. Biochem. 67: 247–256.
Beck, J-P., Beck, G., Wong, K-Y. and Tomkins, G. M., 1972. Proc. Natl. Acad. Sci. U.S.A. 69: 3615–3619.
Kenney, F. T., Lee, K-L., Pomato, N. and Nickol, J. M., 1979. Cold Spring Harbor Conf. Cell Prolif. 6B: 905–917.
Olson, P. S., Thompson, E. B. and Granner, D. K., 1980. Biochemistry 19: 1705–1711.
Stiles, C. D., Lee, K-L. and Kenney, F. T., 1976. Proc. Natl. Acad. Sci. U.S.A. 73: 2634–2638.
Ernest, M. J., DeLap, L. and Feigelson, P., 1978. J. Biol. Chem. 253: 2895–2897.
Wicks, W. D. and Su, J-L., 1978. J. Cyclic Nucl. Res. 4: 113–122.
Lee, K-L., Hill, R. E. and Kenney, F. T., 1978. Fed. Proc. 37: 1620.
Gough, N. and Adams, J., 1978. Biochemistry 17: 5560–5566.
Beale, E. G„ Hartley, J. L. and Granner, D. K., 1982. J. Biol. Chem. 257: 2022–2028.
Chesnokov, V. N., Blinova, N. N. and Mertvetsov, N. P., 1978. Biochimiya 43: 625–629.
Yamamoto, K. and Alberts, B., 1976. Ann. Rev. Biochem. 45: 721–746.
Levitan, I. B. and Webb, T. E., 1970. J. Mol. Biol. 48: 339–348.
Diesterhaft, M., Noguchi, T. and Granner, D. K., 1980. Eur. J. Biochem. 108: 357–365.
Nickol, J. M., Lee, K-L. and Kenney, F. T., 1978. J. Biol. Chem. 253: 4009–4015.
Rousseau, G. G. and Schmit, J.-P., 1977. J. Steroid Biochem. 8: 911–919.
Granner, D. K., Diesterhaft, M., Noguchi, T., Olson, P., Hargrove, J. and Volentine, G., 1979. Cold Spring Harbor Conf. Cell Prolif. 6B: 889–904.
Wicks, W. D., 1969. J. Biol. Chem. 244: 3941–3950.
Granner, D. K., Lee, A. and Thompson, E. B., 1977. J. Biol. Chem. 252: 3891–3897.
Lee, K-L. and Nickol, J. M., 1974. J. Biol. Chem. 249: 6024–6026.
Stellwagen, R. H. and Kohli, K. K., 1981. Biochem. Biophys. Res. Commun. 102: 1209–1215.
Wimalasena, J. and Wicks, W. D., 1979. Mol. Pharmacol. 16: 449–461.
Wimalasena, J., Leichtling, B. H., Lewis, E. J., Langan, T. A. and Wicks, W. D., 1980. Arch. Biochem. Biophys. 205: 595–605.
Hill, R. E., Lee, K-L. and Kenney, F. T., 1981. J. Biol. Chem. 256: 1510–1513.
Noguchi, T., Diesterhaft, M. and Granner, D. K., 1977. J. Biol. Chem. 253: 1332–1335.
Maurer, R. A., 1981. Nature 294: 94–97.
Miles, M. F., Hung, P. and Jungmann, R. A., 1981. J. Biol. Chem. 256: 12545–12552.
Granner, D. K., 1976. Nature 259: 572–573.
Granner, D. K., 1979. In: Glucocorticoid Hormone Action, Monographs in Endocrinology 12: 593–611.
Beck, G., Beck, J-P., Bollack, C. and Belarbi, A., 1978. FEBS Lett. 93: 189–193.
Williams, J. G., Tsang, A. S. and Mahbubani, H, 1980. Proc. Natl. Acad. Sci. U.S.A. 77: 7171–7175.
Koide, Y., Beavo, J. A., Lapoor, C. L., Spruill, W. A., Huang, H-L., Levine, S. N., Ong, S-L., Bechtel, P. J., Yount, W. J. and Steiner, A. L., 1981. Endocrinology 109: 2226–2237.
Granner, D. K., Olson, P., Seifert, S., Block, C., Diesterhaft, M., Hargrove, J. and Noguchi, T., 1980. Annals N.Y. Acad. Sci. 349: 183–194.
Peavy, D. E., Taylor, J. M. and Jefferson, L. S., 1978. Proc. Natl. Acad. Sci. U.S.A. 75: 5879–5883.
Korc, M., Owerbach, D., Quinto, C. and Rutter, W. J., 1981. Science 213: 351–353.
Cimbala, M. A., Lamers, W. H., Nelson, K., Monahan, J. E., Yoo-Warren, H. and Hanson, R. W., 1982. J. Biol. Chem. 257: 7629–7636.
Andreone, T., Beale, E. and Granner, D. K., in press.
Garren, L. D., Howell, R. R., Tomkins, G. M. and Crocco, R. M., 1964. Proc. Natl. Acad. Sci. U.S.A. 52: 1121–1129.
Tomkins, G. M., Thompson, E. B., Hayashi, S., Gelehrter, T., Granner, D. and Peterkovsky, B., 1966. Cold Spring Harbor Symp. Quant. Biol. 31: 349–360.
Tomkins, G. M., Levinson, B. B., Baxter, J. D. and Deth- lefsen, L., 1972. Nature New Biology 88: 9–14.
Reel, J. R. and Kenney, F. T., 1968. Proc. Natl. Acad. Sci. U.S.A. 61: 200–206.
Hofer, E. and Sekeris, C., 1978. Eur. J. Biochem. 86: 547–554.
Ernest, M. J., DeLap, L. and Feigelson, P., 1978. J. Biol. Chem. 253: 2895–2897.
Ernest, M. J., 1982. Biochemistry, in press.
Nelson, K., Cimbala, M. and Hanson, R. W., 1980. J. Biol. Chem. 255: 8509–8515.
Yeoh, G. C. T., Bennett, F. A. and Oliver, I. T., 1979. Biochem. J. 180: 153–160.
Ruiz-Bravo, N., and Ernest, M. H., 1982. Proc. Natl. Acad. Sci. U.S.A. 79: 365–368.
Anderson, S. N., Raiha, N. C. R. and Ohisalo, J. J., 1980. Biochem. J. 186: 609–612.
Greengard, O., 1970. In: Biochemical Actions of Hor¬mones (Litwack, G., ed.), pp 53 - 87, Academic Press, New York.
Wicks, W. D., 1968. J. Biol. Chem. 243: 900–906.
Ho, K. K. W., Cake, M. H., Yeoh, G. C. T. and Oliver, I. T., 1981. Eur. J. Biochem. 118: 137–142.
Cake, M. H., Yeoh, G. C. T. and Oliver, I T., 1981. Biochem. J. 198: 301–307.
Potter, V. R., Gebert, R. A. and Pitot, H. C., 1966. Adv. Enz. Regulation 4: 247–265.
Civen, M., Ulrich, R., Trimmer, B. M. and Brown, C. B., 1967. Science 157: 1563–1564.
Wurtman, R. J. and Axelrod, J., 1967. Proc. Natl. Acad. Sci. U.S.A. 57: 1594–1598.
Shambaugh, G. E., Warner, D. A. and Beisel, W. R., 1967. Endocrinology 81: 811–818.
Civen, M., Brown, C. B. and Granner, D. K., 1970. Bio¬chem. Biophys. Res. Commun. 39: 290–295.
Lipsich, L. A., Kates, J. R. and Lucas, J. J., 1979. Nature 281: 74–76.
Cori, C. F„ Gluecksohn-Waelsch, S., Klinger, H. P., Pick, L., Schlagman, S. L., Teicher, L. S. and Wang-Chang, H-F., 1981. Proc. Natl. Acad. Sci. U.S.A. 78: 479–483.
Perry, S. T., Kulkarni, S. B., Lee, K-L. and Kenney, F. T., 1982. Cancer Res. 42: 473–476.
Rether, B., Belarbi, A. and Beck, G., 1978. FEBS Lett. 93: 194–199.
Hofer, E., Land, H., Sekeris, C. E. and Morris, H. P., 1978. Eur. J. Biochem. 91: 223–229.
Weiss, M. C. and Chaplain, M., 1971. Proc. Natl. Acad. Sci. U.S.A. 68: 3026–3030.
Thompson, E. B., Dannies, P. S., Buckler, C. E. and Tash- jian, A. H., Jr., 1980. J. Steroid Biochem. 12: 193–210.
Fan, J-W., Ivarie, R. D. and Levinson, B. B., 1977. J. Biol. Chem. 252: 7834–7841.
Glueckson-Waelsch, S., 1979. Cell 16: 225–237.
Gopalakrishnan, T.V. and Thompson, E. B., 1977. J. Cell Physiol. 93: 69–80.
Martin, D. W., Jr., Tomkins, G. Ki. and Granner, D. K., 1969. Proc. Natl. Acad. Sci. U.S.A. 62: 248–255.
Martin, D. W., Jr. and Tomkins, G. M., 1970. Proc. Natl. Acad. Sci. U.S.A. 65: 1064–1068.
Martin, D. W., Jr., Tomkins, G. M. and Bresler, M., 1969. Proc. Natl. Acad. Sci. U.S.A. 63: 842–849.
Sellers, L. and Granner, D. K., 1974. J. Cell. Biol. 60: 337–345.
Tomkins, G. M., 1971. In Vitro 6: 321–322.
Steinberg, R. A., Levinson, B. B. and Tomkins, G. M., 1975. Proc. Natl. Acad. Sci. U.S.A. 72: 2007–2011.
Lee, F., Mulligan, R. Berg, P. and Ringold, G., 1981. Nature 294: 228–232.
Payvar, F.,Wrange,O.,Carlstedt-Duke,J.,Okret,S.,Gus- tafson, J.-A. and Yamamoto, K. R., 1981. Proc. Natl. Acad. Sci. U.S.A. 78: 6628–6643.
Bloom, E., Matulich, D. T., Lan, N. C., Higgins, S. J., Simons, S. S. and Baxter, J. D., 1980. J. Steroid Biochem. 12: 175–184.
Rousseau, G. G., Baxter, J. D., Higgins, S. J. and Tom¬kins, G. M., 1973. J. Mol. Biol. 79: 539–554.
Ivarie, R. D. and O’Farrell, P. J., 1978. Cell 13: 41–55.
Lamers, W. J., Hanson, R. W. and Meisner, H. M., 1982. Proc. Natl. Acad. Sci. U.S.A. 79: 5137–5141.
Goldfine, I. D., Jones, A. L., Hradek, G. T. and Wong, K-Y., 1981. Endocrinology 108: 1821–1828.
Krebs, E. G., 1972. Current Topics Cell. Reg. 5: 99–133.
Pastan, I. and Perlman, R., 1970. Science 169: 339–344.
Rousseau, G. G., Higgins, S. J., Baxter, J. D. and Tomkins, G. M., 1974. J. Steroid Biochem. 5: 935–939.
Stellwagen, R. H. and Tomkins, G. M., 1971. J. Mol. Biol. 56: 167–182.
Gurr, J. A., Becker, J. E. and Potter, V. R., 1977. J. Cell. Physiol. 91: 271–288.
Tichonicky, L., Santana-Calderon, M. A., Defer, N., Gie- sen, E. M., Beck, G. and Kruh, J., 1981. Eur. J. Biochem. 120: 427–433
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Granner, D.K., Hargrove, J.L. (1983). Regulation of the synthesis of tyrosine aminotransferase: the relationship to mRNATAT . In: Najjar, V.A. (eds) Enzyme Induction and Modulation. Developments in molecular and cellular biochemistry, vol 3. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-3879-6_7
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