Tyrosine Hydroxylase and Parkinson’s Disease

Haavik, Jan; Toska, Karen

doi:10.1007/bf02741387

Cited by 264Parkinson's Disease Mechanisms and TreatmentsNuclear Receptors and SignalingNeurological disorders and treatments

Tyrosine Hydroxylase and Parkinson’s Disease

Haavik, Jan, Toska, Karen·1998·Molecular Neurobiology

DOI 10.1007/bf02741387

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Abstract

A consistent neurochemical abnormality in Parkinson's disease (PD) is degeneration of dopaminergic neurons in substantia nigra, leading to a reduction of striatal dopamine (DA) levels. As tyrosine hydroxylase (TH) catalyses the formation of L-DOPA, the rate-limiting step in the biosynthesis of DA, the disease can be considered as a TH-deficiency syndrome of the striatum. Similarly, some patients with hereditary L-DOPA-responsive dystonia, a neurological disorder with clinical similarities to PD, have mutations in the TH gene and decreased TH activity and/or stability. Thus, a logical and efficient treatment strategy for PD is based on correcting or bypassing the enzyme deficiency by treatment with L-DOPA, DA agonists, inhibitors of DA metabolism, or brain grafts with cells expressing TH. A direct pathogenetic role of TH has also been suggested, as the enzyme is a source of reactive oxygen species (ROS) in vitro and a target for radical-mediated oxidative injury. Recently, it has been demonstrated that L-DOPA is effectively oxidized by mammalian TH in vitro, possibly contributing to the cytotoxic effects of DOPA. This enzyme may therefore be involved in the pathogenesis of PD at several different levels, in addition to being a promising candidate for developing new treatments of this disease.

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DA synthesis is limited by the rate-limiting enzyme TH, and motor symptoms of PD emerge when TH levels drop below a particular threshold.
“DA synthesis is limited by the rate-limiting enzyme TH, and motor symptoms of PD emerge when TH levels drop below a particular threshold [28,29].”
From Neuroprotective Effects of Bifidobacterium breve CCFM1067 in MPTP-Induced Mouse Models of Parkinson’s Disease (2022) · cites this paper as [28]
TH downregulation decreases DA production, in turn leading to Parkinson's disease.
“TH downregulation decreases DA production, in turn leading to PD [39].”
From Neuroprotective Effects of Sodium Butyrate by Restoring Gut Microbiota and Inhibiting TLR4 Signaling in Mice with MPTP-Induced Parkinson’s Disease (2023) · cites this paper as [39]

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Co-Transplantation of GDNF-Overexpressing Neural Stem Cells and Fetal Dopaminergic Neurons Mitigates Motor Symptoms in a Rat Model of Parkinson’s Disease
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Trimethylamine N-Oxide Exacerbates Neuroinflammation and Motor Dysfunction in an Acute MPTP Mice Model of Parkinson’s Disease
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MPP+-Lesioned Mice: an Experimental Model of Motor, Emotional, Memory/Learning, and Striatal Neurochemical Dysfunctions
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Lycopodium Attenuates Loss of Dopaminergic Neurons by Suppressing Oxidative Stress and Neuroinflammation in a Rat Model of Parkinson’s Disease
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Docosahexaenoic acid protects motor function and increases dopamine synthesis in a rat model of Parkinson's disease via mechanisms associated with increased protein kinase activity in the striatum
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The complex role of inflammation and gliotransmitters in Parkinson's disease
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Potential benefits of incorporating Astragalus membranaceus into the diet of people undergoing disease treatment: An overview
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A Synopsis on the Role of Tyrosine Hydroxylase in Parkinson’s Disease
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Current Status of Tyrosine Hydroxylase in Management of Parkinson’s Disease
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Human tyrosine hydroxylase in Parkinson’s disease and in related disorders
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Authors: Haavik, J., & Toska, K.
Affiliations: University of Bergen (NO)
ORCID: Haavik, Jan
Venue: Molecular Neurobiology
Publisher: Springer Science and Business Media LLC
Published: 1998-06
Volume: 16
Issue: 3
Pages: 285-309
ISSN: 0893-7648 (ISSN-L)
1559-1182
DOI: 10.1007/bf02741387
OpenAlex: W2000631088
Cited by: 263
References: 190
Citations by year: 2026: 11 · 2025: 9 · 2024: 20 · 2023: 17 · 2022: 17 · 2021: 14 · 2020: 15 · 2019: 16 · 2018: 13 · 2017: 10 · 2016: 12 · 2015: 10 · 2014: 22 · 2013: 13 · 2012: 14
FWCI: 0.55
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Molecular Neurobiology (publishedVersion)
PubMed (publishedVersion)
Funders: Norges Forskningsråd
Topics: Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
Health Sciences › Medicine › Neurology › Neurological disorders and treatments
Keywords: tyrosine hydroxylase, Parkinson's disease, dopaminergic neuron loss, substantia nigra, striatal dopamine, L-DOPA, dopamine synthesis, L-DOPA oxidation, reactive oxygen species, oxidative damage, dopamine agonists, enzyme deficiency
MeSH terms: Animals, Antiparkinson Agents, Brain, Dystonia, Humans, Monoamine Oxidase, Mutation, Parkinson Disease, Tyrosine 3-Monooxygenase, Alternative Splicing

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Tyrosine Hydroxylase and Parkinson’s Disease

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