Abstract
Antibodies to tyrosine hydroxylase (TH; EC 1.14.16.2) have been extremely useful in establishing the neuronal and cellular localization of TH (Pickel et al., 1975a,b) and, recently, in demonstrating that in situ phosphorylation of TH is important in regulating the catalytic activity of TH (Waymire et al., 1979). While in the process of raising antibodies to TH, we observed an interesting property of immunoglobulins (Ig) from a sheep that was injected with TH purified from rat pheochromocytoma. Mixture of a partially purified TH and sheep Ig (0–45% ammonium sulfate) resulted in a dramatic elevation of TH activity. The following experiments were performed to establish whether this effect resulted from a specific interaction of TH and antibodies directed against TH. The results indicate that this crude Ig fraction contains anti-TH antibodies, that the majority of anti-TH activity is associated with activation of TH, and that the anti-TH antibodies are not uniformly distributed across IgG subclasses.
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References
Ashe, W.K., Mage, M., Mage, R. and Notkins, A.L. (1968). Neutralization and sensitization of Herpes Simplex virus with antibody fragments from rabbits of different allotypes. J. Immunol. 101, 500–504.
Bradford, M.M. (1976). A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Analyt. Biochem. 72, 248–254.
Brown, J.P., Klitzman, J.M. and Hellstrom, I. (1978), Radioimmunoassay of murine leukemia virus p30 using Staphylococcus aureus as immunoadsorbent. J. Immunol. Meth. 21, 23–33,
Choo, K.H., Myer, J., Cotton, R.G.H., Camakaris, J. and Danks, D. M. (1981). Isolation of a phenylalanine hydroxylase-stimulating monoclonal antibody by rat-myeloma--rat-spleen-cell fusion. Biochem. J. 191, 665–668.
Chuang, D.-M. and Costa, E. (1974). Biosynthesis of tyrosine hydroxylase in rat adrenal medulla after exposure to cold. Proc. Natl. Acad. Sci. USA 71, 4570–4574.
Cinader, B. (1977). Meth. Immunol. Immunochem. 4, 313–375.
Duhamel, R.C., Meezan, E. and Brendel, K. (1980). The pH-dependent binding of goat IgG1 and IgG2 to protein A-Sepharose. Molec. Immunol. 17, 29–36.
Erlichman, J., Sarkar, D., Fleischer, N. and Rubin, C.S. (1980). Identification of two subclasses of type II cAMP-dependent protein kinases. J. Biol. Chem. 255, 8179–8184.
Ey, P.L., Prowse, S.J. and Jenkin, C.R. (1978). Isolation of pure IgGl, IgG2a, IgG2b immunoglobulins from mouse serum usin protein A-Sepharose. Immunochem. 15, 429–436.
Joh, T.H., Geghman, C. and Reis, D. (1973). Immunochemical demonstration of increased accumulation of tyrosine hydroxylase protein in sympathetic ganglia and adrenal medulla elicited by reserpine. Proc. Natl. Acad. Sci. USA 70, 2767–2771.
Kelly,. P.T. and Luttges, M.W. (1975). Electrophoretic separation of nervous system proteins on exponential gradient polyacrylamide gels. J. Neurochem. 24, 1077–1079.
Kessler, S.W. (1975). Rapid isolation of antigens from cells with a Staphylococcal protein A-antibody adsorbent. J. Immunol. 115, 1617–1624.
Kessler, S.W. (1976). Cell membrane antigen isolation with the Staphylococcal protein A-antibody adsorbent. J. Immunol. 117, 1482–1490.
Lloyd, T. and Kaufman, S. (1973). Production of antibodies to bovine adrenal tyrosine hydroxylase. Molec. Pharmacol. 9, 438–444.
Markey, K.A., Kondo, S., Shenkman, L. and Goldstein, M. (1980). Purification and characterization of tyrosine hydroxylase from a clonal pheochromocytoma cell line. Molec. Pharmacol. 17, 79–85.
Natali, P.G., Pellegrino, M.A., Walker, L., Ferrone, S. and Reisfeld, R.A. (1979). Antibody-coated protein A-bearing Staphylococcus aureus: A versitile and stable immune reagent. J. Immunol. Meth. 25, 255–264.
Okada, Y., Ikenaka, T., Yagura, T. and Yamamura, Y. (1963). Immunological heterogeneity of rabbit antibody fragments against Taka-amylase A. J. Biochem. (Tokyo) 54, 101–102.
O’Keefe, E. and Bennett, V. (1980). Use of immunoglobulin-loaded protein A-bearing Staphylococci as a primary solid phase immunoadsorbent in radioimmunoassay. J. Biol. Chem. 255, 561–568.
Park, D.H. and Goldstein, M. (1975). Purification of tyrosine hydroxylase from pheochromocytoma tumors. Life Sci. 18, 55–60.
Pickel, V.M., Joh, T.H., Field, P.M., Becker, C.G. and Reis, D.J. (1975a). Cellular localization of tyrosine hydroxylase by immunocytochemistry. J. Histochem. Cytochem. 23, 1–12.
Pickel, V.M., Joh, T.H. and Reis, D.J. (1975b). Ultrastructural localization of tyrosine hydroxylase in noradrenergic neurons of brain. Proc. Natl. Acad. Sci. USA 72, 659–663.
Pollock, M.R. (1964). Stimulating and inhibiting antibodies for bacterial penicillinase. Immunol. 7, 707–723.
Richmond, M.H. (1963). Purification andproperties of the exopenicillinase from Staphylococcus aureus. Biochem. J. 88, 452–459.
Ross, M.E., Joh, T.H. and Reis, D.J. (1981) Monoclonal antibodies to tyrosine hydroxylase: Production and characterization. Brain Res. 207, in press.
Spector, T. (1978). Refinement of the Coomassie blue method of protein quantitation. Analyt. Biochem. 86, 142–146.
Spiegelberg, H.L. (1964). Biological activities of immunoglobulins of different classes and subclasses. Adv. Immunol. 19, 259–294.
Stephens, J.K., Masserano, J.M., Vulliet, P.R., Weiner, N. and Nakame, P.K. (1981). Immunocytochemical localization of tyrosine hydroxylase in rat adrenal medulla by the peroxidase labelled antibody method. Brain Res. 207, in press.
Suzuki, T., Pelichova, H. and Cinader, B. (1969). Enzyme activation by antibody. J. Immunol. 103, 1366–1376.
Vulliet, P.R., Langan, T.A. and Weiner, N. (1980). Tyrosine hydroxylase: A substrate of cyclic AMP-dependent protein kinase. Proc. Natl. Acad. Sci. USA 77, 92–96.
Waymire, J.C., Bjur, R. and Weiner, N. (1971). Assay of tyrosine hydroxylase by coupled decarboxylation of DOPA formed from l–14C-L-tyrosine. Analyt. Biochem. 43, 588–600.
Waymire, J.C., Haycock, J.W., Meligeni, J.A. and Browning, M.D. (1979). Activation and phosphorylation of tyrosine hydroxylase by cAMP. In Catecholamines: Basic and Clinical Frontiers, (eds. E. Usdin, I.J. Kopin and J. Barchas), pp. 40–42, Pergamon Press, New York.
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Haycock, J.W., Waymire, J.C. (1981). Activating sheep antibodies to tyrosine hydroxylase. In: Usdin, E., Weiner, N., Youdim, M.B.H. (eds) Function and Regulation of Monoamine Enzymes: Basic and Clinical Aspects. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06276-8_13
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DOI: https://doi.org/10.1007/978-1-349-06276-8_13
Publisher Name: Palgrave Macmillan, London
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