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Related Experiment Videos

Serine/threonine phosphatase inhibitors decrease adrenergic arylalkylamine n-acetyltransferase induction in the rat

R Spessert1, M Rapp, L Vollrath

  • 1Department of Anatomy, Johannes Gutenberg University, Mainz, Germany. spessert@mail.uni-mainz.de

Journal of Neuroendocrinology
|July 10, 2001
PubMed
Summary

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Serine/threonine phosphatases regulate arylalkylamine N-acetyltransferase (AA-NAT) activity in rat pineal glands. Inhibitors of these phosphatases reduced AA-NAT expression, suggesting their crucial role in melatonin production regulation.

Area of Science:

  • Neuroendocrinology
  • Molecular Biology
  • Chronobiology

Background:

  • Circadian rhythms in melatonin production are controlled by adrenergic regulation of the pineal enzyme serotonin N-acetyltransferase (AA-NAT).
  • Protein phosphatases are implicated in cellular signaling pathways, but their role in AA-NAT regulation remains unclear.

Purpose of the Study:

  • To investigate the role of protein phosphatases in the adrenergic regulation of rat pineal AA-NAT activity.
  • To determine if specific phosphatase inhibitors affect AA-NAT activity and gene expression.

Main Methods:

  • Cultured rat pineal glands were treated with specific inhibitors of serine/threonine phosphatases (okadaic acid, calyculin A, cypermethrin) and tyrosine phosphatases (dephostatin).
  • AA-NAT activity was measured following adrenergic or cAMP stimulation.

Related Experiment Videos

  • Reverse transcriptase-polymerase chain reaction (RT-PCR) was used to analyze AA-NAT transcript levels and the expression of ICER and Fra-2 mRNA.

    • Main Results:

    • Okadaic acid and calyculin A significantly decreased adrenergically or cAMP-induced AA-NAT activity.
    • These inhibitors also downregulated the amount of AA-NAT transcript, indicating transcriptional regulation.
    • Cypermethrin and dephostatin had no significant effect on AA-NAT activity.
    • Okadaic acid did not alter the cAMP responsiveness of ICER or Fra-2 mRNA.

    Conclusions:

    • Pineal serine/threonine phosphatases, specifically types 1 and 2A, play a significant role in the adrenergic regulation of AA-NAT activity.
    • This regulation appears to occur at the transcriptional level.
    • The mechanism does not seem to involve the previously identified negative regulators ICER and Fra-2.