Serotonin pp 231-251 | Cite as

Regulatory Properties of Neuronal Tryptophan Hydroxylase

  • Michel Hamon
  • Sylvie Bourgoin
  • Françoise Artaud
  • David Nelson
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 133)

Abstract

Extensive studies for the past 10 years on the control of serotonin (5-HT) synthesis in central serotoninergic neurons have led to the conclusion that most regulatory mechanisms involve the first step of the biosynthetic pathway, i.e. tryptophan hydroxylation. This reaction is catalyzed by a highly specific enzyme, tryptophan hydroxylase (L-tryptophan-5-monooxygenase, EC 1.14.16.4), which is not saturated by tryptophan under physiological conditions. Thence, fluctuations in the concentration of this precursor amino-acid in the vicinity of the enzyme as well as changes in the intrinsic activity of tryptophan hydroxylase can both produce significant alterations in the rate of 5-HT synthesis in the central nervous system (CNS) (see Hamon and Glowinski, 1974 for review).

Keywords

Tyrosine Hydroxylase Kainic Acid Tryptophan Hydroxylase Tryptophan Hydroxy Ferrous Ammonium Sulfate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Plenum Press, New York 1981

Authors and Affiliations

  • Michel Hamon
    • 1
  • Sylvie Bourgoin
    • 1
  • Françoise Artaud
    • 1
  • David Nelson
    • 1
  1. 1.Groupe NB, INSERM U.114Collège de FranceParis cedex 05France

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