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Published on: August 10, 2012
Stress-induced catecholaminergic function: transcriptional and post-transcriptional control.
1Laboratory of Molecular and Developmental Neurobiology, Department of Psychiatry, Harvard Medical School, McLean Hospital, Belmont, MA 02478, USA. dona_wong@hms.harvard.edu
Stress (Amsterdam, Netherlands)
|May 22, 2007
Summary
Stress impacts catecholamine enzymes tyrosine hydroxylase (TH) and phenylethanolamine N-methyltransferase (PNMT). Gene activation occurs, but mRNA, protein, and activity levels change discordantly, influenced by stress type and duration.
Area of Science:
- Neuroscience
- Biochemistry
- Endocrinology
Background:
- Stress response involves catecholamine biosynthesis.
- Tyrosine hydroxylase (TH) and phenylethanolamine N-methyltransferase (PNMT) are key enzymes.
- Understanding their regulation under stress is crucial.
Purpose of the Study:
- To review the effects of diverse stressors on TH and PNMT.
- To examine differential enzyme responses in the central vs. peripheral nervous system.
- To explore regulatory mechanisms affecting enzyme activity.
Main Methods:
- Literature review of studies on stress, TH, and PNMT.
- Analysis of changes in mRNA, protein, and enzyme activity.
- Investigation of transcriptional and post-transcriptional regulation.
Main Results:
- Stress activates TH and PNMT gene expression.
- Enzyme responses vary by stressor, duration, and location (CNS vs. periphery).
- Discordance between mRNA induction and protein/activity levels is common.
Conclusions:
- Stress induces catecholamine enzyme gene expression via transcriptional activation.
- Post-transcriptional and post-translational factors create complex regulatory outcomes.
- These mechanisms modulate epinephrine levels during stress.
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