Localization of type 5 17β-hydroxysteroid dehydrogenase mRNA in mouse tissues as studied by in situ hybridization

2005 ◽  
Vol 320 (3) ◽  
pp. 393-398 ◽  
Author(s):  
G. Pelletier ◽  
V. Luu-The ◽  
S. Li ◽  
F. Labrie
Keyword(s):  
In Situ Hybridization ◽  
Hydroxysteroid Dehydrogenase ◽  
Mouse Tissues

scholarly journals Localization of Type 8 17β-hydroxysteroid Dehydrogenase mRNA in Mouse Tissues as Studied by In Situ Hybridization

2005 ◽  
Vol 53 (10) ◽  
pp. 1257-1271 ◽  
Author(s):  
Georges Pelletier ◽  
Van Luu-The ◽  
Songyun Li ◽  
Fernand Labrie
Keyword(s):  
In Situ Hybridization ◽  
Epithelial Cells ◽  
Stromal Cells ◽  
Cellular Localization ◽  
Pulmonary Arteries ◽  
Hydroxysteroid Dehydrogenase ◽  
Hybridization Signal ◽  
Mouse Tissues ◽  
Sites Of Action

The enzyme type 8 17β-hydroxysteroid dehydrogenase (17β-HSD) selectively catalyzes the conversion of estradiol (E2) to estrone (E1). To obtain detailed information on the sites of action of type 8 17β-HSD, we have studied the cellular localization of type 8 17β-HSD mRNA in mouse tissues using in situ hybridization. In the ovary, hybridization signal was detected in granulosa cells of growing follicles and luteal cells. In the uterus, type 8 17β-HSD mRNA was found in the epithelial (luminal and glandular) and stromal cells. In the female mammary gland, the enzyme mRNA was seen in ductal epithelial cells and stromal cells. In the testis, hybridization signal was observed in the seminiferous tubule. In the prostate, type 8 17β-HSD was detected in the epithelial cells of the acini and stromal cells. In the clitoral and preputial glands, labeling was detected in the epithelial cells of acini and small ducts. The three lobes of the pituitary gland were labeled. In the adrenal gland, hybridization signal was observed in the three zones of the cortex, the medulla being unlabeled. In the kidney, the enzyme mRNA was found to be expressed in the epithelial cells of proximal convoluted tubules. In the liver, all the hepatocytes exhibited a positive signal. In the lung, type 8 17β-HSD mRNA was detected in bronchial epithelial cells and walls of pulmonary arteries. The present data suggest that type 8 17β-HSD can exert its action to downregulate E2 levels in a large variety of tissues.

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

2000 ◽  
Vol 165 (2) ◽  
pp. 217-222 ◽  
Author(s):  
M Bonenfant ◽  
PR Provost ◽  
R Drolet ◽  
Y Tremblay
Keyword(s):  
In Situ Hybridization ◽  
Hydroxysteroid Dehydrogenase ◽  
Binding Activity ◽  
Placental Lactogen ◽  
Specific Expression ◽  
P450 Aromatase ◽  
Chain Cleavage ◽  
Extravillous Cytotrophoblasts

The 17beta-hydroxysteroid dehydrogenases (17beta-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 17beta-hydroxy-steroids. Because this reaction essentially transforms steroids having low binding activity for the steroid receptor to their more potent 17beta-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 17beta-HSD enzyme (E17beta-HSD) catalyzes the reduction of the low activity estrogen, estrone, into the potent estrogen, estradiol. We studied the cell-specific expression of type 1 17beta-HSD in human term placental villous tissue by combining in situ hybridization to localize type 1 17beta-HSD mRNA with immunohistochemistry using an antibody against human placental lactogen, a trophoblast marker. Immunolocalization of E17beta-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 3beta-hydroxysteroid dehydrogenase (3beta-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 17beta-HSD mRNA and protein, as well as P450scc, P450 aromatase, and 3beta-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 17beta-HSD gene. However, CTBs lying beneath the syncytial layer, e.g. those from which syncytiotrophoblasts develop, contained barely detectable amounts of type 1 17beta-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 17beta-HSD mRNA.

scholarly journals Ontogenesis of 3β-Hydroxysteroid Dehydrogenase Δ5-Δ4 Isomerase in the Rat Ovary as Studied by Immunocytochemistry and in Situ Hybridization

1993 ◽  
Vol 48 (2) ◽  
pp. 226-234 ◽  
Author(s):  
Christian Juneau ◽  
Eric Dupont ◽  
Van Luu-The ◽  
Fernand Labrie ◽  
Georges Pelletier
Keyword(s):  
In Situ Hybridization ◽  
Hydroxysteroid Dehydrogenase ◽  
Rat Ovary

Localization of 20α-hydroxysteroid dehydrogenase mRNA in mouse brain by in situ hybridization

2004 ◽  
Vol 125 (1-2) ◽  
pp. 143-146 ◽  
Author(s):  
G. Pelletier ◽  
V. Luu-The ◽  
S. Li ◽  
F. Labrie
Keyword(s):  
In Situ Hybridization ◽  
Mouse Brain ◽  
Hydroxysteroid Dehydrogenase

scholarly journals Localization of Type 5 17β-Hydroxysteroid Dehydrogenase, 3β-Hydroxysteroid Dehydrogenase, and Androgen Receptor in the Human Prostate by in Situ Hybridization and Immunocytochemistry

Endocrinology ◽  
1999 ◽  
Vol 140 (3) ◽  
pp. 1481-1491 ◽  
Author(s):  
Mohamed El-Alfy ◽  
Van Luu-The ◽  
Xiao-Fang Huang ◽  
Louise Berger ◽  
Fernand Labrie ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Androgen Receptor ◽  
Hydroxysteroid Dehydrogenase ◽  
Human Prostate

11 beta-Hydroxysteroid dehydrogenase mRNA expression in rat kidney

1991 ◽  
Vol 260 (5) ◽  
pp. F764-F767
Author(s):  
J. L. Yau ◽  
A. D. Van Haarst ◽  
M. P. Moisan ◽  
S. Fleming ◽  
C. R. Edwards ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Binding Sites ◽  
Mineralocorticoid Receptor ◽  
Rat Kidney ◽  
Hydroxysteroid Dehydrogenase ◽  
Mineralocorticoid Receptors ◽  
Tubular Cells ◽  
Renal Tubular

11 beta-Hydroxysteroid dehydrogenase (11 beta-OHSD) protects nonspecific renal mineralocorticoid receptors from exposure to circulating glucocorticoid in vivo by catalyzing the conversion of corticosterone to inactive 11-dehydrocorticosterone. Although 11 beta-OHSD bioactivity and aldosterone binding sites are found in distal tubular cells, mineralocorticoid receptor and 11 beta-OHSD immunoreactivities are not colocalized. However, there are several kidney isoforms of 11 beta-OHSD, not all of which may be immunoreactive, whereas only a single mRNA species has been described. Using in situ hybridization we found 11 beta-OHSD mRNA is highly expressed in all renal tubular epithelia in the rat. It is therefore likely that 11 beta-OHSD is colocalized with mineralocorticoid receptors in distal tubular cells.

Expression of laminin isoforms in mouse myogenic cells in vitro and in vivo

1995 ◽  
Vol 108 (12) ◽  
pp. 3795-3805 ◽  
Author(s):  
F. Schuler ◽  
L.M. Sorokin
Keyword(s):  
In Situ Hybridization ◽  
Basement Membranes ◽  
Chain Gene ◽  
Muscle Fibres ◽  
Myogenic Cells ◽  
Mouse Tissues ◽  
Laminin 1

The expression of laminin-1 (previously EHS laminin) and laminin-2 (previously merosin) isoforms by myogenic cells was examined in vitro and in vivo. No laminin alpha 2 chainspecific antibodies react with mouse tissues, 50 rat monoclonal antibodies were raised against the mouse laminin alpha 2 chain: their characterization is described here. Myoblasts and myotubes from myogenic cell lines and primary myogenic cultures express laminin beta 1 and gamma 1 chains and form a complex with a 380 kDa alpha chain identified as laminin alpha 2 by immunofluorescence, immunoprecipitation and PCR. PCR from C2C12 myoblasts and myotubes for the laminin alpha 2 chain gene (LamA2) provided cDNA sequences which were used to investigate the in vivo expression of mouse LamA2 mRNA in embryonic tissues by in situ hybridization. Comparisons were made with specific probes for the laminin alpha 1 chain gene (LamA1). LamA2 but not LamA1 mRNA was expressed in myogenic tissues of 14- and 17-day-old mouse embryos, while the laminin alpha 2 polypeptide was localized in adjacent basement membranes in the muscle fibres. In situ hybridization also revealed strong expression of the LamA2 mRNA in the dermis, indicating that laminin alpha 2 is expressed other than by myogenic cells in vivo. Immunofluorescence studies localized laminin alpha 2 in basement membranes of basal keratinocytes and the epithelial cells of hair follicles, providing new insight into basement membrane assembly during embryogenesis. In vitro cell attachment assays revealed that C2C12 and primary myoblasts adhere to laminin-1 and -2 isoforms in a similar manner except that myoblast spreading was significantly faster on laminin-2. Taken together, the data suggest that laminins 1 and 2 play distinct roles in myogenesis.

scholarly journals Expression of Human Group II Phospholipase A2 in Transgenic Mice

1997 ◽  
Vol 45 (8) ◽  
pp. 1109-1119 ◽  
Author(s):  
Timo J. Nevalainen ◽  
V. Jukka O. Laine ◽  
David S. Grass
Keyword(s):  
In Situ Hybridization ◽  
Epithelial Cells ◽  
Urinary Bladder ◽  
Connective Tissue ◽  
Transgenic Mice ◽  
Phospholipase A ◽  
Human Group ◽  
Mouse Tissues ◽  
Group Ii

Group II phospholipase A2 (PLA2) has been proposed to play an important role in inflammation and defense against bacterial infection. We investigated tissues of transgenic mice expressing the human group II PLA2 gene by immunohistochemistry using rabbit anti-human group II PLA2 antibodies, and by in situ hybridization by probing with human group II PLA2 mRNA anti-sense (test) and sense (control) riboprobes. By immunohis-tochemistry, human group II PLA2 was found in various mouse tissues and cell types including hepatocytes, proximal tubule cells of the kidney, epithelial cells of the renal pelvis, urinary bladder and ureter, granulosa cells of Graafian follicles, aortic intima and media, cartilage, epiphyseal bone, bronchial epithelial cells, and connective tissue cells in the dermis. By in situ hybridization, group II PLA2 mRNA was localized in hepatocytes, epidermal cells, dermal cells, connective tissue fibroblasts, epithelial and smooth muscle cells of the urinary bladder, and cells of Bowman's capsule. These results show that human group II PLA2 is expressed in large amounts in hepatocytes and many extrahepatic tissues of the transgenic mice. These animals provide a useful new tool for studies on the metabolism, in vivo effects, and physiological and pathological roles of phospholipase A2. (J Histochem Cytochem 45:1109–1119, 1997)

Differential expression of type 2 and type 3 inositol 1,4,5-trisphosphate receptor mRNAs in various mouse tissues: in situ hybridization study

1995 ◽  
Vol 280 (2) ◽  
pp. 201-210 ◽  
Author(s):  
Ichiroh Fujino ◽  
Norihiko Yamada ◽  
Atsushi Miyawaki ◽  
Mamoru Hasegawa ◽  
Teiichi Furuichi ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Differential Expression ◽  
Hybridization Study ◽  
Mouse Tissues ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Type 3 ◽  
Receptor Mrnas
Sign in / Sign up

Export Citation Format

Share Document