Immunohistochemical Localization of Aromatase Cytochrome P-450 and Estradiol Dehydrogenase in the Syncytiotrophoblast of the Human Placenta*

Fournet-Dulguerov, Nicole; MacLusky, Neil J.; Leranth, Csaba; Todd, Roberta B.; Mendelson, Carole R.; Simpson, Evan R.; Naftolin, Frederick

doi:10.1210/jcem-65-4-757

Cited by 142 publications

(54 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Immunohistochemical localization of P-450AROM *n *ne ovary has not been published except for one report showing the presence of P-450AROM in the theca interna (Matsuda et al, 1984). In addition, immunohistochemical localization of P-450AROM was reported in syncytiotrophoblast ofthe human placenta (Fournet-Dulguerov et al, 1987), and confirmed in the present study. In our current investigation, the distribution of P-450,la and P-450scc was essentially similar to that in cow follicles (Rodgers et al, 1986b).…”

Section: Discussionsupporting

confidence: 85%

Immunolocalization of aromatase, 17 -hydroxylase and side-chain-cleavage cytochromes P-450 in the human ovary

et al. 1989

View full text Add to dashboard Cite

Summary. Immunohistochemical localization of cholesterol side-chain-cleavage, 17\ g=a\ \ x=r eq-\ hydroxylase and aromatase cytochromes P-450 was performed in 35 morphologically normal human premenopausal ovaries by using specific antibodies against the enzymes. In well-developed ovarian follicles in the late stages of follicular growth, immunoreactivity of P-450arom was only seen in granulosa cells while P-45017\g=a\ and P-450scc activity was confined to theca interna cells, confirming that follicular oestrogen is produced in granulosa cells by the aromatization of androgens derived from the theca interna cells. In the corpus luteum, this functional differentiation is maintained, since immunoreactivity of P-450arom was exclusively present in luteinized granulosa cells while that of P-45017\g=a\ was present in luteinized theca cells. Immunoreactivity of P-450scc was present in both types of cells in the corpus luteum.

show abstract

Section: Discussionsupporting

confidence: 85%

Immunolocalization of aromatase, 17 -hydroxylase and side-chain-cleavage cytochromes P-450 in the human ovary

et al. 1989

View full text Add to dashboard Cite

show abstract

“…It is widely expressed in a number of tissues throughout the body, such as ovary (31,(35)(36)(37)(38), placenta (31,32,(38)(39)(40)(41)(42), testis (36,(43)(44)(45)(46)(47)(48)(49)(50)(51)(52)(53)(54), adipose tissue (31,(55)(56)(57)(58)(59)(60)(61)(62), muscle (55), liver (63), various sites in the brain including the hypothalamus (64)(65)(66)(67)(68), hair follicles (69), genital skin fibroblasts (70,71), fetal tissues (31,60,(72)(73)(74) (75) and in many human tumours including endometrial cancer …”

Section: Aromatasementioning

confidence: 99%

Oestrogen deficiency in men: where are we today?

Faustini‐Fustini

Rochira

Carani

1999

European Journal of Endocrinology

123

105

View full text Add to dashboard Cite

show abstract

“…The other antibodies were also raised in rabbits against either a synthetic peptide for P450 aromatase (Fournet-Dulguerov et al 1987) or purified proteins for P450scc (Black et al 1993), 3 -HSD-1 (Luu- The et al 1989b), and E17 -HSD (Luu-The et al 1989a). Each antiserum was previously described and used in immunohistochemical or Western blots and no cross-reactivity with other known steroidconverting enzymes has been reported.…”

Section: Antisera and Nucleotidesmentioning

confidence: 99%

“…In a study with placental tissues from the first trimester of pregnancy, Fournet-Dulguerov et al (1987) observed immunoreactive E17 -HSD only in the syncytiotrophoblasts. In that study, they reported an absence of immunoreactivity in CTBs.…”

Section: Introductionmentioning

confidence: 95%

Localization of type 1 17beta-hydroxysteroid dehydrogenase mRNA and protein in syncytiotrophoblasts and invasive cytotrophoblasts in the human term villi

Bonenfant

Pr²,

Drolet³

et al. 2000

Journal of Endocrinology

View full text Add to dashboard Cite

The 17 -hydroxysteroid dehydrogenases (17 -HSDs) play a key role in the synthesis of sex steroids. The hallmark of this family of enzymes is the interconversion, through their oxydoreductive reactivity at position C17, of 17-keto-and 17 -hydroxy-steroids. Because this reaction essentially transforms steroids having low binding activity for the steroid receptor to their more potent 17 -hydroxysteroids isoforms, it is crucial to the control of the physiological activities of both estrogens and androgens. The human placenta produces large amounts of progesterone and estrogens throughout pregnancy. The placental type 1 17 -HSD enzyme (E17 -HSD) catalyzes the reduction of the low activity estrogen, estrone, into the potent estrogen, estradiol. We studied the cell-specific expression of type 1 17 -HSD in human term placental villous tissue by combining in situ hybridization to localize type 1 17 -HSD mRNA with immunohistochemistry using an antibody against human placental lactogen, a trophoblast marker. Immunolocalization of E17 -HSD was also performed. To ascertain whether other steroidogenic enzymes are present in the same cell type, cytochrome P450 cholesterol side-chain cleavage (P450scc), P450 aromatase, and type 1 3 -hydroxysteroid dehydrogenase (3 -HSD) were also localized by immunostaining. Our results showed that the syncytium is the major steroidogenic unit of the fetal term villi. In fact, type 1 17 -HSD mRNA and protein, as well as P450scc, P450 aromatase, and 3 -HSD immunoreactivities were found in these cells. In addition, our results revealed undoubtedly that extravillous cytotrophoblasts (CTBs), e.g. those from which cell columns of anchoring villous originate, also express the type 1 17 -HSD gene. However, CTBs lying beneath the syncytial layer, e.g. those from which syncytiotrophoblasts develop, contained barely detectable amounts of type 1 17 -HSD mRNA as determined by in situ hybridization. These findings, along with those from other laboratories confirm the primordial role of the syncytium in the synthesis of steroids during pregnancy. In addition, our results indicate for the first time that CTBs differentiating along the invasive pathway contain type 1 17 -HSD mRNA.

show abstract

Immunohistochemical Localization of Aromatase Cytochrome P-450 and Estradiol Dehydrogenase in the Syncytiotrophoblast of the Human Placenta*

Cited by 142 publications

References 0 publications

Immunolocalization of aromatase, 17 -hydroxylase and side-chain-cleavage cytochromes P-450 in the human ovary

Immunolocalization of aromatase, 17 -hydroxylase and side-chain-cleavage cytochromes P-450 in the human ovary

Oestrogen deficiency in men: where are we today?

Localization of type 1 17beta-hydroxysteroid dehydrogenase mRNA and protein in syncytiotrophoblasts and invasive cytotrophoblasts in the human term villi

Contact Info

Product

Resources

About