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Neuronal PAS domain protein 1 regulates tyrosine hydroxylase level in dopaminergic neurons

✍ Scribed by Christina H.L. Teh; Chin Chieh Loh; Kevin K.Y. Lam; Jia Min Loo; Tie Yan; Tit Meng Lim

Book ID
102907487
Publisher
John Wiley and Sons
Year
2007
Tongue
English
Weight
508 KB
Volume
85
Category
Article
ISSN
0360-4012

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✦ Synopsis

Abstract

Catecholamines (dopamine, norepinephrine, and epinephrine) are all synthesized from a common pathway in which tyrosine hydroxylase (TH) is the rate‐limiting enzyme. Dopamine is the main neurotransmitter present in dopaminergic neurons of the ventral midbrain, where dysfunction of these neurons can lead to Parkinson's disease and schizophrenia. Neuronal PAS domain protein 1 (NPAS1) was identified as one of the genes up‐regulated during dopaminergic MN9D cell differentiation. We found that there was a corresponding decrease in TH level during MN9D differentiation. Overexpression and siRNA experiments revealed that NPAS1, in concert with ARNT, negatively regulates the expression of TH and that this regulation is mediated by a direct binding of NPAS1 on the TH promoter. Expression studies also confirmed a decrease in TH level in the ventral midbrain during mouse development, concomitant with an increase in NPAS1 level. These results suggest that NPAS1 plays a novel and important role in regulating TH level of dopaminergic neurons in the ventral midbrain during development. © 2007 Wiley‐Liss, Inc.

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