A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics

  title={A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics},
  author={Brigitte Grima and Annie Lamouroux and Claudette Boni and J. F. Julien and France Javoy‐Agid and Jacques Mallet},
Catecholaminergic systems in discrete regions of the brain are thought to be important in affective psychoses, learning and memory, reinforcement and sleep–wake cycle regulation1. Tyrosine hydroxylase (TH) is the first enzyme in the pathway of catecholamine synthesis. Its importance is reflected in the diversity of the mechanisms that have been described which control its activity2; TH levels vary both during development and as a function of the activity of the nervous system. Recently, we… 
Human Tyrosine Hydroxylase Natural Allelic Variation: Influence on Autonomic Function and Hypertension
It is concluded that common variation in the proximal TH promoter is functional, giving rise to changes in autonomic function and consequently cardiovascular risk.
Multiple tyrosine hydroxylase transcripts and immunoreactive forms in the rat: Differential expression in the anterior pituitary and adrenal gland
There is alternative splicing of the TH primary transcript, and putative additional poisttranslational regulation may yield TH proteins with no enzymatic activity, at least in non‐catecholaminergic tissues.
Cloning and cell type-specific regulation of the human tyrosine hydroxylase gene promoter.
A Novel Rat Tyrosine Hydroxylase mRNA Species Generated by Alternative Splicing
Tyrosine hydroxylase catalyzes the first and rate‐limiting step in the biosynthesis of catecholamines, and alternative splicing of TH primary transcript has been described as a characteristic of higher primates and Drosophila.
The human tyrosine hydroxylase gene
  • T. Nagatsu
  • Biology
    Cellular and Molecular Neurobiology
  • 2004
The results of Southern blot analysis and the nucleotide sequence of the human TH genomic DAN indicate that the four types of human TH mRNA are produced through alternative splicing from a single gene.
Isolation and nucleotide sequence of a cDNA clone encoding bovine adrenal tyrosine hydroxylase: Comparative analysis of tyrosine hydroxylase gene products
Comparison of the size of bovine and rat TH mRNA and protein by northern blot and immunoblot analyses yielded differences consistent with those predicted from the nucleotide sequence data.
Exon 3 of tyrosine hydroxylase gene: lack of association with Japanese schizophrenic patients
The results indicate that exon 3 of the human TH gene lacks association with schizophrenia in Japanese patients, and any mutation changing the amino acid sequence Gly36-Arg37-Arg38 would result in the elevation of DA synthesis.


Localization of the human tyrosine hydroxylase gene to 11p15: gene duplication and evolution of metabolic pathways.
Consideration of this assignment of PAH to chromosome 12, together with the known distribution of other pairs of related genes on these two chromosomes, provides convincing evidence of their ancestral relationship and suggests a role for gene duplication in the diversification of metabolic pathways in the vertebrate ancestors of mammals.
Molecular Genetics of Tyrosine Hydroxylase
Amino acid sequence comparison with phenyl-alanine hydroxylase indicates that these enzymes share a high degree of homology.
Role of RNA and DNA in Brain Function
The characterisation of postsynaptic GABA receptors and the evidence for multiple forms of such sites are discussed and the development of antibodies to components of the GABA receptor complex illustrates the role molecular biology has to play in neurotransmitter receptor characterisation.
Linkage of tyrosine hydroxylase to four other markers on the short arm of chromosome 11.
It is shown that tyrosine hydroxylase is closely linked to insulin, beta-globin, D11S12 and Harvey-ras 1, members of a linkage group which has previously been localised to 11p, and a gene order based on multipoint mapping is suggested.
Complete coding sequence of rat tyrosine hydroxylase mRNA.
Several clones specific for tyrosine hydroxylase have been identified from a rat PC12 library by using the previously characterized clone pTH-1.2, the most complete of which is 1758 base pairs long and covers most of the length of the mRNA.
Time course of the changes of TH mRNA in rat brain and adrenal medulla after a single injection of reserpine.
The results suggest that induction of TH results from an enhanced transcription of the TH gene, the enzyme catalyzing the rate‐limiting step in the biosynthesis of catecholamines, in tissue from a single rat.