Journal of Histochemistry and Cytochemistry Priciples for Free Access to Science
  Search:   
    >> Advanced Search

Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pelletier, G.
Right arrow Articles by Labrie, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pelletier, G.
Right arrow Articles by Labrie, F.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?
Journal of Histochemistry and Cytochemistry
Volume 51 (11): 1425-1436, 2003
Copyright ©The Histochemical Society, Inc.

Sex-related Expression of 20{alpha}-hydroxysteroid Dehydrogenase mRNA in the Adult Mouse

G. Pelletier, V. Luu–The, S. Li, L. Ren and F. Labrie

Oncology and Molecular Endocrinology Research Center, Laval University Medical Center (CHUL) and Laval University, Québec, (PQ) Canada

Correspondence to: Dr. Georges Pelletier, Oncology and Molecular Endocrinology Research Center and Québec Génome Center, Laval University Hospital (CHUL), 2705 Laurier Boulevard. Québec, PQ G1V 4G2, Canada. E-mail: georges.pelletier{at}crchul.ulaval.ca

The enzyme 20{alpha}-hydroxysteroid dehydrogenase (20{alpha}-HSD) catalyzes the conversion of progesterone into its inactive form, 20{alpha}-hydroxyprogesterone. To gain information about the exact sites of 20{alpha}-HSD mRNA expression, we performed in situ hybridization using a 35S-labeled cRNA probe in tissues of adult mice of both sexes. 20{alpha}-HSD mRNA was expressed in both male and female gonads. In the ovary, high expression was found in luteal cells of corpora lutea, while much lower expression could be detected in granulosa cells of growing follicles. In the testis, a specific hybridization signal was detected only in Leydig cells. In the female reproductive tract, 20{alpha}-HSD mRNA was found in the epithelial cells of the uterine cervix. In the adrenal cortex, only the zona reticularis exhibited specific radiolabeling, the expression being very high in the female and very low in the male. In the skin, specific labeling was restricted to sebaceous glands, the hybridization signal being much higher in the female than in the male. In the liver, 20{alpha}-HSD mRNA was found in hepatocytes, with a higher degree of expression in the female. In the kidney, specific labeling was observed in the epithelial cells of distal convoluted tubules, the signal being also much more striking in the female than in the male. In non-reproductive tissues, it clearly appears that the expression of 20{alpha}-HSD mRNA is higher in the female than in the male, suggesting that 20{alpha}-HSD may play an important role in reducing the intracellular concentration of progesterone originating from the circulation at a much higher level in the female. (J Histochem Cytochem 51:1425–1436, 2003)

Key Words: progesterone catabolism • 20{alpha}-hydroxysteroid • progesterone • 20{alpha}-hydroxysteroid • dehydrogenase • mRNA expression • in situ hybridization • mouse • autoradiography


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
EndocrinologyHome page
L. Hershkovitz, F. Beuschlein, S. Klammer, M. Krup, and Y. Weinstein
Adrenal 20{alpha}-Hydroxysteroid Dehydrogenase in the Mouse Catabolizes Progesterone and 11-Deoxycorticosterone and Is Restricted to the X-Zone
Endocrinology, March 1, 2007; 148(3): 976 - 988.
[Abstract] [Full Text] [PDF]


Home page
J Mol EndocrinolHome page
K A Brown, D Boerboom, N Bouchard, M Dore, J G Lussier, and J Sirois
Human chorionic gonadotropin-dependent induction of an equine aldo-keto reductase (AKR1C23) with 20{alpha}-hydroxysteroid dehydrogenase activity during follicular luteinization in vivo.
J. Mol. Endocrinol., June 1, 2006; 36(3): 449 - 461.
[Abstract] [Full Text] [PDF]




Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
The Journal of Histochemistry & Cytochemistry is owned, published, and licensed by The Histochemical Society © 2003