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Activity of Adrenal Catecholamine-Producing Enzymes and Their Regulation after Stress

  • Richard Kvetňanský
  • Irwin J. Kopin
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 33)

Abstract

The pathway for biosynthesis of catecholamines from tyrosine was first proposed by Blaschko in 1939 (3), but only recently have separate enzymatic reactions been characterized. Conversion of tyrosine to dopa is catalyzed by the enzyme tyrosine hydroxylase (TH)(23), which is believed to be the rate-limiting step in the biosynthesis of the catecholamines (17). High levels of the relatively nonspecific aromatic L-amino acid decarboxylase (7,18) rapidly decarboxylate dopa to dopamine; decarboxylation therefore appears to play little or no role in regulation of catecholamine synthesis. Dopamine enters the chromaffin granules to be converted by the enzyme dopamine-beta-hydroxylase (DBH) to norepinephrine (16). Conversion of norepinephrine to epinephrine by phenyl-ethanolamine-N-methyltransferase (PNMT) is the final step in the biosynthesis of catecholamines in the adrenal medulla (1,8).

Keywords

Tyrosine Hydroxylase Adrenal Cortex Adrenal Medulla Splanchnic Nerve Intact Side 
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 1973

Authors and Affiliations

  • Richard Kvetňanský
    • 1
    • 2
  • Irwin J. Kopin
    • 1
    • 2
  1. 1.Institute of Experimental EndocrinologySlovak Academy of SciencesBratislavaCzechoslovakia
  2. 2.Laboratory of Clinical ScienceNational Institute of Mental HealthBethesdaUSA

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