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 Synthesis of transthyretin (pre-albumin) mRNA in choroid plexus epithelial cells, localized by in situ hybridization in rat brain.

1986 ◽  
Vol 34 (7) ◽  
pp. 949-952 ◽  
Author(s):  
A J Stauder ◽  
P W Dickson ◽  
A R Aldred ◽  
G Schreiber ◽  
F A Mendelsohn ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Epithelial Cells ◽  
Rat Brain ◽  
Choroid Plexus ◽  
Cellular Localization ◽  
Lateral Ventricles ◽  
The Brain ◽  
Albumin Mrna ◽  
Choroid Plexus Epithelial

The sites of synthesis of transthyretin in the brain were investigated using in situ hybridization with [35S]-labeled recombinant cDNA probes specific for transthyretin mRNA. Autoradiography of hybridized coronal sections of rat brain revealed specific cellular localization of transthyretin mRNA in choroid plexus epithelial cells of the lateral, third, and fourth ventricles. Transferrin mRNA was also investigated and, in contrast to transthyretin mRNA, was localized mainly in the lateral ventricles. Our results indicate that substantial synthesis of transthyretin and transferrin mRNA may occur in the choroid plexus.

scholarly journals Localization of Cytochrome P450 CYP2S1 Expression in Human Tissues by In Situ Hybridization and Immunohistochemistry

2005 ◽  
Vol 53 (5) ◽  
pp. 549-556 ◽  
Author(s):  
Sirkku T. Saarikoski ◽  
Harriet A.-L. Wikman ◽  
Gillian Smith ◽  
C. Henrik J. Wolff ◽  
Kirsti Husgafvel-Pursiainen
Keyword(s):  
Cytochrome P450 ◽  
In Situ Hybridization ◽  
Epithelial Cells ◽  
Cellular Localization ◽  
Tumor Development ◽  
Tissue Microarrays ◽  
Cell Types ◽  
Human Tissues ◽  
Expression Levels

CYP2S1 is a recently discovered dioxin-inducible member of the cytochrome P450 superfamily. It has been shown to be involved in the metabolism of some aromatic hydrocarbons as well as retinoic acid, suggesting a role in biotransformation of both exogenous and endogenous compounds. In this study, we used mRNA in situ hybridization and immunohistochemistry to investigate the cellular localization of CYP2S1 in various human tissues using tissue microarrays. High expression levels were observed mainly in epithelial cell types, especially in the epithelia frequently exposed to xenobiotics. In the respiratory tract, the expression was strong in nasal cavity, bronchi, and bronchioli, whereas it was low in the alveolar lining cells. Similarly, CYP2S1 was highly expressed in the epithelial cells throughout the gastrointestinal tract. Strong epithelial expression was also observed in uterine cervix, urinary bladder, and skin. In many exocrine glands (e.g., adrenal gland and pancreas), secretory epithelial cells showed moderate to strong expression levels. In the liver, the expression was low. CYP2S1 was highly expressed in epithelial cells that are major targets for carcinogen exposure and common progenitor cells to tumor development. Indeed, we found strong CYP2S1 expression in many tumors of epithelial origin.

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)

scholarly journals Localization of 17β-hydroxysteroid dehydrogenase type 1 mRNA in mouse tissues

2004 ◽  
Vol 33 (2) ◽  
pp. 459-465 ◽  
Author(s):  
G Pelletier ◽  
V Luu-The ◽  
S Li ◽  
L Ren ◽  
F Labrie
Keyword(s):  
Cellular Localization ◽  
Hydroxysteroid Dehydrogenase ◽  
Hair Follicles ◽  
Hybridization Signal ◽  
Sweat Glands ◽  
Seminiferous Tubules ◽  
Intermediate Lobe ◽  
Peripheral Tissues ◽  
Mouse Tissues

The enzyme 17β-hydroxysteroid dehydrogenase (17β-HSD) type 1 catalyzes the conversion of estrone (E1) into 17β estradiol (E2). To gain information about the cellular localization of 17β-HSD mRNA type 1 expression, we performed in situ hybridization using a 35S-labeled cRNA probe in several tissues of adult mice of both sexes. In the ovary, high expression was found in granulosa cells of growing follicles. No specific labeling could be observed in corpora lutea or interstitial cells. In the pituitary gland of animals of both sexes, 17β-HSD type 1 mRNA was expressed in the intermediate lobe melanotrophs while no specific signal could be detected in the anterior or posterior lobes of the pituitary. In the prostate, 17β-HSD type 1 mRNA was exclusively found in the epithelial cells. In both male and female mouse dorsal skin, a specific hybridization signal was seen in the sebaceous glands while the epidermis, stroma, hair follicles and sweat glands were unlabeled. In the testis, a hybridization signal was detected in germ cells of the seminiferous tubules, Leydig cells being unlabeled. The present data indicate that E2 can be formed through the action of 17β-HSD type 1 in specific cells of the gonads and peripheral tissues. In the testes and peripheral tissues, the action of E2 is probably limited to the cells involved in its formation in an intracrine fashion.

scholarly journals Localization of oestrogen receptor alpha, oestrogen receptor beta and androgen receptors in the rat reproductive organs

2000 ◽  
Vol 165 (2) ◽  
pp. 359-370 ◽  
Author(s):  
G Pelletier ◽  
C Labrie ◽  
F Labrie
Keyword(s):  
In Situ Hybridization ◽  
Epithelial Cells ◽  
Leydig Cells ◽  
Oestrogen Receptor ◽  
Muscle Cells ◽  
Seminal Vesicles ◽  
Secretory Cells ◽  
Cell Nuclei ◽  
Sites Of Action

There is now evidence that oestrogens and androgens can influence male and female reproductive systems. In order to accurately identify the sites of action of oestrogens and androgens, we have proceeded to the histological localization of the two oestrogen receptor (ER) subtypes, ERalpha and ERbeta, and the androgen receptor (AR) in the reproductive tissues of adult rats of both sexes. AR was detected by immunocytochemistry, while ERalpha and ERbeta were localized by both immunocytochemistry and in situ hybridization. In the pituitary gland of animals of both sexes, ERalpha was found in the majority of nuclei of secretory cells in the anterior pituitary. The intermediate and posterior lobes did not show any staining. ERbeta was not found to be expressed in any of the pituitary lobes. Using AR antibodies, nuclear staining was detected in about 50% of secretory cells of the anterior lobe, the intermediate and posterior lobes being completely unstained. In the testis, ERalpha was localized in nuclei of Leydig cells as well as in round spermatocytes and spermatids, while ERbeta could only be detected in Sertoli cell nuclei. AR immunoreactivity was found in nuclei of Sertoli, peritubular myoid and Leydig cells. In the prostate, ERbeta was observed in epithelial cells of tubulo-alveoli, while the stroma was unlabelled. ERalpha was not found to be expressed in any prostate cells. In the prostate, AR was detected in nuclei of epithelial, stromal and endothelial cells. In seminal vesicles, staining of ERalpha was found in nuclei of epithelial and stromal cells. Similar findings were observed using AR antibodies. While ERbeta mRNA could not be detected by in situ hybridization, weak staining for ERbeta was localized in epithelial cells of seminal vesicles. In the ovary, both ERalpha and ERbeta were found to be expressed. ERbeta mRNA was found in granulosa cells of growing follicles, while ERalpha was present in theca cells, interstitial gland cells and germinal epithelium. AR immunoreactivity was detected in granulosa cell nuclei in growing follicles and also in scattered interstitial cells. In the oviduct and uterus, ERalpha was observed in nuclei of epithelial cells as well as of stromal and muscle cells. Similarly, AR immunoreactivity was present in nuclei of epithelial cells, stromal and muscle cells in both the oviduct and uterus. ERbeta was not detected in the oviduct and uterus. The present findings indicate a cell-specific localization of ERalpha, ERbeta and AR in reproductive tissues in rats of both sexes. By establishing the precise sites of action of oestrogens and androgens they contribute to a better understanding of the respective role of these steroids in reproduction function.

scholarly journals Expression of Adiponectin Receptors and Its Possible Implication in the Human Endometrium

Endocrinology ◽  
2006 ◽  
Vol 147 (7) ◽  
pp. 3203-3210 ◽  
Author(s):  
Yuri Takemura ◽  
Yutaka Osuga ◽  
Toshimasa Yamauchi ◽  
Masaki Kobayashi ◽  
Miyuki Harada ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Stromal Cells ◽  
Adiponectin Receptors ◽  
Monocyte Chemoattractant Protein 1 ◽  
Monocyte Chemoattractant ◽  
Monocyte Chemoattractant Protein ◽  
Amp Activated Protein Kinase

Adiponectin, a pleiotropic cytokine, exerts its effects via the specific receptors AdipoR1 and AdipoR2. Whereas circulating adiponectin concentrations decrease in women with endometriosis and endometrial cancer, possible effects of adiponectin and the presence of the receptors in the endometrium have not been determined. In this study, we examined the expression of adiponectin receptors AdipoR1 and AdipoR2 in the human endometrium and assessed effects of adiponectin in endometrial cells. Expression of AdipoR1 and AdipoR2 in endometrial tissues was evaluated by real-time quantitative PCR, in situ hybridization, and Western blotting. The effects of adiponectin on phosphorylation of AMP-activated protein kinase, a regulator of energy homeostasis, in cultured endometrial stromal cells (ESCs) and epithelial cells (EECs) were studied by Western blotting. The effects of adiponectin on IL-1β-induced secretion of IL-6, IL-8, and monocyte chemoattractant protein 1 from cultured ESCs were determined using specific ELISAs. The expression of AdipoR1 and AdipoR2 was detected in the endometrium. The expression of both genes was increased in the midluteal phase, the period of embryo implantation. In situ hybridization revealed that both AdipoR1 and AdipoR2 appeared to be equally expressed in the epithelial cells and in the stromal cells. Adiponectin increased phosphorylation of AMP-activated protein kinase in ESCs and EECs. Adiponectin decreased IL-1β-induced secretion of IL-6, IL-8, and monocyte chemoattractant protein 1 from ESCs. These findings suggest that adiponectin exerts energy-homeostatic and antiinflammatory effects in the endometrium, and these effects might be relevant to pathological and physiological endometrium-related events such as implantation and endometriosis.

Expression and localization of aquaporins in rat gastrointestinal tract

1999 ◽  
Vol 276 (3) ◽  
pp. C621-C627 ◽  
Author(s):  
Yu Koyama ◽  
Tadashi Yamamoto ◽  
Tatsuo Tani ◽  
Kouei Nihei ◽  
Daisuke Kondo ◽  
...  
Keyword(s):  
Small Intestine ◽  
In Situ Hybridization ◽  
Gastrointestinal Tract ◽  
Epithelial Cells ◽  
Cellular Localization ◽  
Basolateral Membrane ◽  
Rnase Protection Assay ◽  
Rnase Protection ◽  
Basolateral Membranes

A family of water-selective channels, aquaporins (AQP), has been demonstrated in various organs and tissues. However, the localization and expression of the AQP family members in the gastrointestinal tract have not been entirely elucidated. This study aimed to demonstrate the expression and distribution of several types of the AQP family and to speculate on their role in water transport in the rat gastrointestinal tract. By RNase protection assay, expression of AQP1–5 and AQP8 was examined in various portions through the gastrointestinal tract. AQP1 and AQP3 mRNAs were diffusely expressed from esophagus to colon, and their expression was relatively intense in the small intestine and colon. In contrast, AQP4 mRNA was selectively expressed in the stomach and small intestine and AQP8 mRNA in the jejunum and colon. Immunohistochemistry and in situ hybridization demonstrated cellular localization of these AQP in these portions. AQP1 was localized on endothelial cells of lymphatic vessels in the submucosa and lamina propria throughout the gastrointestinal tract. AQP3 was detected on the circumferential plasma membranes of stratified squamous epithelial cells in the esophagus and basolateral membranes of cardiac gland epithelia in the lower stomach and of surface columnar epithelia in the colon. However, AQP3 was not apparently detected in the small intestine. AQP4 was present on the basolateral membrane of the parietal cells in the lower stomach and selectively in the basolateral membranes of deep intestinal gland cells in the small intestine. AQP8 mRNA expression was demonstrated in the absorptive columnar epithelial cells of the jejunum and colon by in situ hybridization. These findings may indicate that water crosses the epithelial layer through these water channels, suggesting a possible role of the transcellular route for water intake or outlet in the gastrointestinal tract.

scholarly journals Chronologic Localization of Mycoplasma hyopneumoniae in Experimentally Infected Pigs

2002 ◽  
Vol 39 (5) ◽  
pp. 584-587 ◽  
Author(s):  
D. Kwon ◽  
C. Choi ◽  
C. Chae
Keyword(s):  
In Situ Hybridization ◽  
Epithelial Cells ◽  
Mycoplasma Hyopneumoniae ◽  
Hybridization Signal ◽  
Type I ◽  
Luminal Surface ◽  
Strong Hybridization ◽  
Different Tissues

The chronologic localization of Mycoplasma hyopneumoniae was examined by in situ hybridization in experimentally infected pigs for a period of 35 days after intratracheal inoculation. M. hyopneumoniae DNA was detected in bronchial and bronchiolar epithelial cells from infected pigs at 7, 14, 21, and 28 days postinoculation (DPI) and in alveolar and interstitial macrophages and type I pneumocytes from infected pigs at 14, 21, 28, and 35 DPI. Strong hybridization signals for M. hyopneumoniae were detected mainly at the luminal surface of bronchial and bronchiolar lining epithelial cells. When a hybridization signal was detected at the luminal surface of bronchial and bronchiolar lining epithelial cells, a given bronchus or bronchiole also exhibited peribronchiolar lymphoid cuffing. These observations suggested that the presence of M. hyopneumoniae in different tissues could be due to a difference in the duration of the infection.

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