Localization of 17 beta-hydroxysteroid dehydrogenase throughout gestation in human placentaE Dupont, F Labrie, V Luu-The and G Pelletier Medical Research Council Group in Molecular Endocrinology, CHUL Research Center, Quebec, Canada. 17 beta-Hydroxysteroid dehydrogenase (17 beta-HSD) is the enzyme responsible for the formation of all sex steroids in gonadal as well as extragonadal tissues. To obtain more information about the age-specific expression of 17 beta-HSD in the human placenta, we have localized this enzyme by immunocytochemistry at the light microscopic level at different periods of gestation. In the 7- and 9-week-old placenta, immunostaining was detected exclusively in the cytoplasm of the syncytiotrophoblast. Between the tenth and thirteenth weeks of gestation, immunolabeling was also observed in the cytoplasm of the cytotrophoblastic cells, suggesting that these cells could be transiently involved in the biosynthesis of sex steroids. Interestingly, between the fourteenth and twenty-fifth weeks of gestation, 17 beta-HSD was observed in both the cytoplasm and nucleus of the syncytiotrophoblast. The reaction product was much more intense in nuclei than in cytoplasm. During the last trimester of gestation, strong immunocytochemical staining was observed in all the nuclei of the syncytiotrophoblast, the cytoplasm being unstained. The meaning of this nuclear staining for 17 beta-HSD is still unclear and remains to be extensively investigated.
Volume 39,
Issue 10,
pp. 1403-1407,
10/01/1991
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Y. Takase, M.-H. Levesque, V. Luu-The, M. El-Alfy, F. Labrie, and G. Pelletier Expression of Enzymes Involved in Estrogen Metabolism in Human Prostate J. Histochem. Cytochem., August 1, 2006; 54(8): 911 - 921. [Abstract] [Full Text] [PDF] |
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M. Bonenfant, C. H. Blomquist, P. R. Provost, R. Drolet, P. DAscoli, and Y. Tremblay Tissue- and Site-Specific Gene Expression of Type 2 17{beta}-Hydroxysteroid Dehydrogenase: In Situ Hybridization and Specific Enzymatic Activity Studies in Human Placental Endothelial Cells of the Arterial System J. Clin. Endocrinol. Metab., December 1, 2000; 85(12): 4841 - 4850. [Abstract] [Full Text] |
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S. Leivonen, Y.-s. Piao, H. Peltoketo, P. Numchaisrika, R. Vihko, and P. Vihko Identification of Essential Subelements in the hHSD17B1 Enhancer: Difference in Function of the Enhancer and That of the hHSD17BP1 Analog Is due to -480C and -486G Endocrinology, August 1, 1999; 140(8): 3478 - 3487. [Abstract] [Full Text] |
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M. W. Sawicki, M. Erman, T. Puranen, P. Vihko, and D. Ghosh Structure of the ternary complex of human 17beta -hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP+ PNAS, February 2, 1999; 96(3): 840 - 845. [Abstract] [Full Text] [PDF] |
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M. V. J. Mustonen, V. V. Isomaa, T. Vaskivuo, J. Tapanainen, M. H. Poutanen, F. Stenbäck, R. K. Vihko, and P. T. Vihko Human 17{beta}-Hydroxysteroid Dehydrogenase Type 2 Messenger Ribonucleic Acid Expression and Localization in Term Placenta and in Endometrium during the Menstrual Cycle J. Clin. Endocrinol. Metab., April 1, 1998; 83(4): 1319 - 1324. [Abstract] [Full Text] |
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