Expression of 17beta-hydroxysteroid dehydrogenase type 1 and type 2, P450 aromatase, and 20alpha-hydroxysteroid dehydrogenase enzymes in immature, mature, and pregnant rats.
In the present study, we evaluated the expression and regulation of 17beta-hydroxysteroid dehydrogenase (17HSD) type 1 and type 2, cytochrome P450 aromatase (P450arom), and 20alpha-hydroxysteroid dehydrogenase (20HSD) in mature and pregnant rats. Immunohistochemical analysis of rat 17HSD type 1 showed that the enzyme is exclusively expressed in the granulosa cells of developing, healthy, primary, secondary, and tertiary follicles at all stages of the estrous cycle and pregnancy, and is not detected in the corpora lutea. The data showed that the amount of the enzyme expressed in the follicle increases as follicular maturation progresses and is highest in tertiary and Graafian follicles. However, Northern blot analysis of total RNA from whole ovaries showed a rather constitutive expression of the 17HSD type 1 enzyme. It is evident that compared with P450arom, 17HSD type 1 is more widely expressed in the follicles during the various maturational stages of folliculogenesis. Hence, the data indicate distinct localization, expression, and regulation patterns for 17HSD type 1 and P450arom during the rat estrous cycle and pregnancy. Furthermore, compared with the two estradiol biosynthetic enzymes, a different expression pattern was detected for 20HSD messenger RNA. During the estrous cycle the enzyme was detected in the ovaries throughout the cycle, and in the ovaries of pregnant animals the enzyme showed an expression pattern the opposite of that observed for P450arom. Rat 17HSD type 2, not detected in the ovaries, was constitutively expressed in both female and male liver and small intestine in 21-day-old fetuses up to 6-week-old mature animals. Similarly, in these tissues the enzyme was constitutively expressed in normal cycling and pregnant animals, but it showed increasing expression in the placenta as pregnancy advanced. The relatively constitutive expression of the enzyme at all physiological stages of the animals suggests a general role for the enzyme in the inactivation of circulating sex steroids.
Akinola
L A
LA
Biocenter Oulu and the Department of Clinical Chemistry, University of Oulu, Finland.
Poutanen
M
M
Vihko
R
R
Vihko
P
P
D015067:17-Hydroxysteroid Dehydrogenases / Q000235:genetics / Q000378:metabolism*; D015089:20-Hydroxysteroid Dehydrogenases / Q000235:genetics / Q000378:metabolism*; D043607:20-alpha-Hydroxysteroid Dehydrogenase; D000375:Aging / Q000378:metabolism*; D000818:Animals; D001141:Aromatase / Q000235:genetics / Q000378:metabolism*; D004958:Estradiol / Q000378:metabolism; D004970:Estrone / Q000378:metabolism; D005260:Female; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism*; D008297:Male; D010053:Ovary / Q000201:enzymology; D010920:Placenta / Q000201:enzymology; D011247:Pregnancy; D012333:RNA, Messenger / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley
D007527:Isoenzymes; D012333:RNA, Messenger; D004970:Estrone; D004958:Estradiol; D015067:17-Hydroxysteroid Dehydrogenases; D015089:20-Hydroxysteroid Dehydrogenases; D043607:20-alpha-Hydroxysteroid Dehydrogenase; C044256:3 (or 17)-beta-hydroxysteroid dehydrogenase; D001141:Aromatase