Open AccessPhenylethanolamine‐N‐methyl transferase and catechol‐O‐methyl transferase activity in rat uterus
Author(s) -
Casimiri Viviane,
Cohen Wayne R.,
Parvez Simone,
Hobel Calvin,
Parvez Hasan
Publication year - 1993
Publication title -
acta obstetricia et gynecologica scandinavica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.401
H-Index - 102
eISSN - 1600-0412
pISSN - 0001-6349
DOI - 10.3109/00016349309021151
Subject(s) - transferase , phenylethanolamine , uterus , steroid , methyltransferase , catechol , medicine , endocrinology , catechol o methyl transferase , enzyme , biochemistry , chemistry , immunohistochemistry , hormone , tyrosine hydroxylase , allele , methylation , gene
Purpose. The activity of phenylethanolamine‐N‐melhyl‐transferase (PNMT) and catechol‐O‐methyl‐transferasc (COMT) was studied in uterine homogenates from adult female Wistar rats with normal cycles and that had been ovariectomized. adrenalectomized. and steroid‐treated. Results. Activities of the two enzymes changed significantly during the normal estrus cycle. Both peaked during metestrus. with COMT showing a secondary peak of activity at proestrus. Progesterone treatment significantly increased and estradiol decreased PNMT activity in comparison to untreated controls. Hydrocortisone administration had no effect on uterine PNMT activity. COMT activity was not affected significantly by any of the steroid treatments. Conclusion. The data confirm that uterine tissues possess the enzymatic machinery to synthesize epinephrine from norepincphrine. and suggest the activity of this pathway may be mediated by variations in the sex hormone environment of the uterus.