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Regulation of Tyrosine Hydroxylase and Dopamine β‐Hydroxylase mRNA Levels in Rat Adrenals by a Single and Repeated Immobilization Stress
Author(s) -
McMahon Anne,
Kvetňansk Richard,
Fukuhara Koki,
Weise Virginia K.,
Kopin Irwin J.,
Sabban Esther L.
Publication year - 1992
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1992.tb10954.x
Subject(s) - tyrosine hydroxylase , endocrinology , medicine , dopamine , catecholamine , tyrosine 3 monooxygenase , chemistry , biology
Adrenal catecholamines are known to mediate many of the physiological consequences of the “fight or flight” response to stress. However, the mechanisms by which the long‐term responses to repeated stress are mediated are less well understood and possibly involve alterations in gene expression. In this study the effects of a single and repeated immobilization stress on mRNA levels of the adrenal catecholamine biosynthetic enzymes, tyrosine hydroxylase and dopamine β ‐hydroxylase, were examined. A repeated 2‐hr daily immobilization for 7 consecutive days markedly elevated both tyrosine hydroxylase and dopamine β ‐hydroxylase mRNA levels (about six‐ and fourfold, respectively). In contrast, tyrosine hydroxylase but not dopamine β ‐hydroxylase mRNA levels were elevated immediately following a single immobilization. The elevation in tyrosine hydroxylase mRNA with a single immobilization was as high as with seven daily repeated immobilizations. This elevation was not sustained and returned toward control values 24 hr later. Both tyrosine hydroxylase and dopamine β ‐hydroxylase mRNA levels were elevated immediately following two daily immobilizations to levels similar to those observed after seven immobilizations and were maintained 24 hr later. The results indicate that both tyrosine hydroxylase and dopamine β ‐hydroxylase mRNA levels are elevated by stress; however, the mechanism and/or timing of their regulation are not identical.