Genes for neurotransmitter synthesis, storage, and uptake. Academic Article uri icon

Overview

abstract

  • We found that the catecholamine biosynthetic enzymes tyrosine hydroxylase (TH) (EC 1.14.16.2), dopamine beta-hydroxylase (EC 1.14.17.1), and phenylethanolamine N-methyltransferase (EC 2.1.1.28) share similar protein domains in their primary structures and that they share common gene coding sequences. In a recent report we also demonstrated that antiserums directed against choline acetyltransferase (EC 2.3.1.6), glutamic acid decarboxylase (EC 4.1.1.15), and TH cause specific complement-mediated lysis of cholinergic, gamma-aminobutyric acid-ergic, and dopaminergic subpopulations of synaptosomes, respectively. This interaction of specific antibodies to the specific subpopulation of synaptosomal membrane, e.g., recognition of antibody to TH to only the dopaminergic subpopulation of synaptosomal membrane protein, indicates that the neurotransmitter enzyme and membrane protein of its own synaptosomes may also share common protein domains. Therefore, we postulate that the specific neurotransmitter biosynthetic enzyme and a certain membrane protein of the nerve endings may share similar gene coding sequences, and that expression of these proteins may determine the phenotype of the neuron.

publication date

  • September 1, 1985

Research

keywords

  • Dopamine beta-Hydroxylase
  • Glutamate Decarboxylase
  • Neurotransmitter Agents
  • Phenylethanolamine N-Methyltransferase
  • Serine Endopeptidases
  • Tyrosine 3-Monooxygenase

Identity

Scopus Document Identifier

  • 0022000870

PubMed ID

  • 2863177

Additional Document Info

volume

  • 44

issue

  • 12