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This version published online on November 14, 2003
Endocrinology, doi:10.1210/en.2003-1170
A more recent version of this article appeared on March 1, 2004
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Submitted on September 5, 2003
Accepted on November 4, 2003

Inhibition of p38 Mitogen-Activated Protein Kinase Enhances Adrenergic-Stimulated Arylalkylamine N-Acetyltransferase Activity in Rat Pinealocytes

J. R. Man1, S. Rustaeus1, D. M. Price1, C. L. Chik1, and A. K. Ho1*

1 Department of Physiology and Department of Medicine; Faculty of Medicine, University of Alberta; 7-26 Medical Sciences Building; Edmonton, Alberta T6G 2H7, CANADA

* To whom correspondence should be addressed. E-mail: anho{at}ualberta.ca.

We have previously shown that inhibition of p38MAPK increases adrenergic-stimulated p42/44MAPK activation in rat pinealocytes. In this study, we investigated whether p38MAPK played a role in the adrenergic regulation of arylalkylamine-N-acetyltransferase (AA-NAT) induction and melatonin (MT) synthesis. Treatment of pinealocytes with norepinephrine (NE) caused a time-dependent increase in the levels of AA-NAT mRNA, AA-NAT protein and enzymatic activity as well as MT production. Co-treatment with SB202190, a selective p38MAPK inhibitor, while having no effect on AA-NAT activity or protein level 3 h after NE treatment, caused a sustained increase in AA-NAT activity and protein level after 6 h of NE treatment. The increase in NE-stimulated AA-NAT activity and protein level by SB202190 occurred in the absence of an increase in AA-NAT mRNA level. Similar results were obtained when AA-NAT was induced by (Bu)2cAMP or when SB203580 was used to inhibit p38MAPK. In comparison, SB202474, the inactive analog, had no effect on NE or (Bu)2cAMP-stimulated AA-NAT activity or protein level. SB202190 also increased cumulative NE-stimulated MT production, provided that the medium was supplemented with 5-methoxytryptamine. p38MAPK inhibitors had no effect on hydroxyindole-O-methyltransferase (HIOMT) activity. These results show that inhibition of p38MAPK, while having no effect on cAMP-mediated AA-NAT transcription, appears to increase AA-NAT activity either by increasing translation or by reducing degradation of the AA-NAT protein. The lack of effect on NE-stimulated MT accumulation by p38MAPK inhibitors in the absence of 5-methoxytryptamine could be secondary to either a lack of substrate or alternatively HIOMT may become limiting.
Key words: p38MAPK • AA-NAT • melatonin • pineal




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