Summary
Multiple measures on statistical patterns from a kinetic scattering paradigm for the activities of rat brainstem medial and dorsal raphé nuclear tryptophan hydroxylase preparations are consistent with the previous hypothesis (J. Neural Transmission 45∶1–15, 1979) that the lithium ion induces a state of kinetic bistability in the system. In this context, the lithium-induced sigmoid tetrahydrobiopterin-reaction velocity function is interpreted as a jump between two stable states of differing catalytic potential with a less kinetically accessible domain between them. These dynamics are qualitatively portrayed in three dimensions by Thom's classical cusp catastrophe.
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References
Arecchi, F. T., Lisi, F. Hopping mechanism generating 1/f noise in non-linear systems. Phys. Rev. Lett.49, 94–98 (1982).
Brigbam, E. O. The Fast Fourier Transform, pp. 50–74. Englewood Cliffs, N.J.: Prentice-Hall. 1974.
Bullard, W. P., Gutherie, P. B., Russo, P. V., Mandell, A. J. Regional and subcellular distribution and some factors in the regulation of reduced pterins in rat brain. J. Pharmacol. Exp. Ther.206, 4–20 (1978).
Careri, G., Fasella, P., Gratton, E. Statistical time events in enzymes: a physical assessment. CRC Crit. Rev. Biochem.3, 141–164 (1975).
Cooper, A. Thermodynamic fluctuations in protein molecules. Proc. Natl. Acad. Sci. U.S.A.13, 2740–2741 (1976).
Edelfors, S. The influence of lithium on water binding ability, consistency, and macromolecules in the rat brain. Acta Pharmacol. Toxicol.40, 126–133 (1977).
Fernstrom, J. D., Wurtman, R. J. Brain serotonin content: physiological regulation by plasma neutral amino acids. Science178, 414–416 (1972).
Friedman, P. A., Kappelman, A. H., Kaufman, S. Partial purification and characterization of tryptophan hydroxylase from rabbit hind brain. J. Biol. Chem.247, 4165–4173 (1972).
Fukushima, T., Nixon, J. C. Analysis of reduced forms of biopterin in biological tissues and fluids. Anal. Biochem.102, 176–188 (1980).
Geyer, M. A., Puerto, A., Dawsey, W. J., Knapp, S., Bullard, W. P., Mandell, A. J. Histologic and enzymatic studies of the mesolimbic and mesostriatal serotonergic pathways. Brain Research106, 241–256 (1976).
Glansdorff, P., Prigogine, I. Thermodynamic Theory of Stucture, Stability, and Fluctuations, pp. 61–125. New York: Wiley. 1971.
Gurd, F. R. N., Rothgeb, T. M. Motions in proteins. Adv. Prot. Chem.33, 73–165 (1979).
Haken, H. Synergetics, pp. 191–224, 263–292. New York: Springer. 1978.
Hasegawa, H., Yanagisawa, M., Ichiyama, A. Three discrete activity states of mastocytoma tryptophan-5-monooxygenase. In: Oxygenases and Oxygen Metabolism (Nozaki, M., Yamamoto, S., Ishimura, Y., Coon, M. J., Ernster, L., Estabrook, R. W., eds.), pp. 293–304. New York: Academic Press. 1982.
Ichiyama, A., Nakamura, S., Nishizuka, Y., Hayaishi, O. Enzymic studies on the biosynthesis of serotonin in mammalian brain. J. Biol. Chem.245, 1699–1708 (1970).
Knapp, S. Tryptophan hydroxylase: variational kinetics. J. Histochem. Cytochem.30, 847–851 (1982).
Knapp, S., Mandell, A. J. Parachlorophenylalanine: its three phase sequence of interactions with two forms of brain tryptophan hydroxylase. Life Sci.11, 861–871 (1972 a).
Knapp, S., Mandell, A. J. Narcotic drugs: effects on the serotonin biosynthetic systems of the brain. Science177, 1209–1211 (1972 b).
Knapp, S., Mandell, A. J. Short and long-term lithium administration: effects on the brain's serotonergic biosynthetic systems. Science180, 645–647 (1973).
Knapp, S., Mandell, A. J. Effects of lithium chloride on parameters of biosynthetic capacity for 5-hydroxytryptamine in rat brain. J. Pharmacol. Exp. Ther.193, 812–823 (1975).
Knapp, S., Mandell, A. J. Coincidence of blockade of synaptosomal 5-hydroxytryptamine uptake and decrease in tryptophan hydroxylase activity: effects of fenfluramine. J. Pharmacol. Exp. Ther.198, 123–132 (1976).
Knapp, S., Mandell, A. J. Conformational influences on brain tryptophan hydroxylase by submicromolar calcium: opposite effects of equimolar lithium. J. Neural Transmission45, 1–15 (1979).
Knapp, S., Mandell, A. J., Bullard, W. P. Calcium activation of brain tryptophan hydroxylase. Life Sci.16, 1583–1594 (1975).
Knapp, S., Mandell, A. J., Russo, V. P., Vitto, A., Stewart, K. D. Strain differences in kinetic and thermal stability of two mouse brain tryptophan hydroxylase activities. Brain Research230, 317–336 (1981).
Koshland, D. E., Nemethy, G., Filmer, D. Comparison of experimental binding data and theoretical models in protein-containing subunits. Biochemistry5, 365–385 (1966).
Kubo, R., Matsuo, K., Kitahara, K. Fluctuation and relaxation of macrovariables. J. Stat. Phys.9, 51–96 (1973).
Kuhn, D. M. Deactivation of tyrosine hydroxylase by reduced pteridines. Trans. Am. Soc. Neurochem.14, 175 (1983).
Lovenberg, W., Levine, R., Miller, L. The hydroxylase cofactor and catecholamine synthesis. In: Function and Regulation of Monoamine Enzymes: Basic and Clinical Aspects (Usdin, E., Weiner, N., Youdim, M., eds.), pp. 225–230. London: Macmillan. 1982.
Lowry, O. H., Rosebrough, N. J., Carr, A. L., Randall, R. J. Protein measurement with the Folin phenol reagent. J. Biol. Chem.193, 165–175 (1951).
Mandelbrot, B. B. How long is the coast of Britain? Statistical self-similarity and fractional dimension. Science155, 636–638 (1967).
Mandell, A. J. Redundant mechanisms regulating brain tyrosine and tryptophan hydroxylases. Ann. Rev. Pharmacol. Toxicol.18, 461–493 (1978).
Mandell, A. J., Russo, P. V. Striatal tyrosine hydroxylase activity: multiple conformational kinetic oscillators and product concentration frequencies. J. Neurosci.1, 380–389 (1981).
Mandell, A. J., Russo, P. V., Knapp, S. Strange stability in hierarchically coupled neuropsychobiological systems. In: Evolution of Order and Chaos in Physics, Chemistry, and Biology (Haken, H., ed.), pp. 270–286. Berlin-Heidelberg-New York: Springer. 1982.
Minorsky, N. Nonlinear Oscillations, pp. 40–70, 101–117. New York: Van Nostrand. 1962.
Monod, J., Wyman, J., Changeux, J.-P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol.12, 88–118 (1965).
Nakata, H., Fujisawa, F. Purification and properties of tryptophan-5-monooxygenase from rat brain-stem. Eur. J. Biochem.122, 41–47 (1982).
Pain, R. H. The conformation and stability of folded protein. In: Characterization of Protein Conformation and Function (Franks, F., ed.), pp. 19–36. London: Symposium Press. 1978.
Russo, P. V. A mathematical model for the effect of tetrahydrobiopterin level on tyrosine hydroxylase kinetic fluctuations. Psychopharmacol. Bull18, 31–34 (1982).
Siegel, S. Nonparametric Statistics, p. 271. New York: McGraw-Hill. 1956.
Vitto, A., Mandell, A. J. Stability properties of activated tryptophan hydroxylase from rat midbrain. J. Neurochem.37, 601–607 (1981).
Yamaguchi, T., Sawada, M., Kato, T., Nagatsu, T. Demonstration of tryptophan-5-monooxygenase activity in human brain by highly sensitive high performance liquid chromatography with fluorometric detection. Biochem. Internatl.2, 295–303 (1981).
Zeeman, E. C. Catastrophe Theory, pp. 1–79. Reading, Mass.: Addison-Wesley. 1977.
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This work was supported by a grant from the National Institute on Drug Abuse, DA-00265-11. Appreciation is expressed to Patrick V. Russo for programming the computer calculations and to Arnetta Fitch for technical and Barbara Blomgren for editorial assistance.
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Knapp, S., Mandell, A.J. Scattering kinetics in a complex tryptophan hydroxylase preparation from rat brainstem raphe nuclei: Statistical evidence that the lithium-induced sigmoid velocity function reflects two states of available catalytic potential. J. Neural Transmission 58, 169–182 (1983). https://doi.org/10.1007/BF01252803
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DOI: https://doi.org/10.1007/BF01252803