Melandrium firmum Extract Promotes Hair Growth by Modulating 5α-Reductase Activity and Gene Expression in C57BL/6J Mice

Chorion is the most abundant site of 11β-hydroxysteroid dehydrogenase type 1 (11β-HSD1) expression within intrauterine tissues. It is important to study the regulation of 11β-HSD1 expression in the chorion in terms of local cortisol production during pregnancy. Using real-time PCR and enzyme activity assay, we found that cortisol (1 μm) and IL-1β (10 ng/ml) for 24 h significantly increased 11β-HSD1 mRNA expression and reductase activity in cultured human chorionic trophoblasts. A further significant increase of 11β-HSD1 mRNA expression and reductase activity was observed with cotreatment of cortisol and IL-1β. To explore the mechanism of induction, 11β-HSD1 promoter was cloned into pGL3 plasmid expressing a luciferase reporter gene. By transfecting the constructed vector into WISH cells, an amnion-derived cell line, we found that cortisol (1 μm) or IL-1β (10 ng/ml) significantly increased reporter gene expression. Likewise, an additional increase in reporter gene expression was observed with cotreatment of cortisol and IL-β. To explore the physiological significance of 11β-HSD1 induction in the chorion, we studied the effect of cortisol on cytosolic phospholipase A2 and cyclooxygenase 2 expression. We found that treatment of chorionic trophoblast cells with cortisol (1 μm) induced both cytosolic phospholipase A2 and cyclooxygenase 2 mRNA expression. We conclude that cortisol up-regulates 11β-HSD1 expression through induction of promoter activity, and the effect was enhanced by IL-1β, suggesting that more biologically active glucocorticoids could be generated in the fetal membranes in the presence of infection, which may consequently feed forward in up-regulation of prostaglandin synthesis.

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Control of dimethylsulfoxide reductase expression in Rhodobacter capsulatus: the role of carbon metabolites and the response regulators DorR and RegA

Microbiology ◽

10.1099/00221287-148-2-605 ◽

2002 ◽

Vol 148 (2) ◽

pp. 605-614 ◽

Cited By ~ 25

Author(s):

Ulrike Kappler ◽

Wilhelmina M Huston ◽

Alastair G McEwan

Keyword(s):

Gene Expression ◽

Carbon Source ◽

Rhodobacter Capsulatus ◽

Response Regulator ◽

Reductase Activity ◽

Negative Regulator ◽

Wild Type ◽

Dmso Reductase ◽

Dimethylsulfoxide Reductase ◽

Operon Expression

Regulation of the expression of dimethylsulfoxide (DMSO) reductase was investigated in the purple phototrophic bacterium Rhodobacter capsulatus. Under phototrophic, anaerobic conditions with malate as carbon source, DMSO caused an approximately 150-fold induction of DMSO reductase activity. The response regulator DorR was required for DMSO-dependent induction and also appeared to slightly repress DMSO reductase expression in the absence of substrate. Likewise, when pyruvate replaced malate as carbon source there was an induction of DMSO reductase activity in cells grown at low light intensity (16 W m−2) and again this induction was dependent on DorR. The level of DMSO reductase activity in aerobically grown cells was elevated when pyruvate replaced malate as carbon source. One possible explanation for this is that acetyl phosphate, produced from pyruvate, may activate expression of DMSO reductase by direct phosphorylation of DorR, leading to low levels of induction of dor gene expression in the absence of DMSO. A mutant lacking the global response regulator of photosynthesis gene expression, RegA, exhibited high levels of DMSO reductase in the absence of DMSO, when grown phototrophically with malate as carbon source. This suggests that phosphorylated RegA acts as a repressor of dor operon expression under these conditions. It has been proposed elsewhere that RegA-dependent expression is negatively regulated by the cytochrome cbb 3 oxidase. A cco mutant lacking cytochrome cbb 3 exhibited significantly higher levels of Φ[dorA::lacZ] activity in the presence of DMSO compared to wild-type cells and this is consistent with the above model. Pyruvate restored DMSO reductase expression in the regA mutant to the same pattern as found in wild-type cells. These data suggest that R. capsulatus contains a regulator of DMSO respiration that is distinct from DorR and RegA, is activated in the presence of pyruvate, and acts as a negative regulator of DMSO reductase expression.

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Syringic Acid Extracted fromHerba dendrobiiPrevents Diabetic Cataract Pathogenesis by Inhibiting Aldose Reductase Activity

Evidence-based Complementary and Alternative Medicine ◽

10.1155/2012/426537 ◽

2012 ◽

Vol 2012 ◽

pp. 1-13 ◽

Cited By ~ 11

Author(s):

Xiaoyong Wei ◽

Dan Chen ◽

Yanchun Yi ◽

Hui Qi ◽

Xinxin Gao ◽

...

Keyword(s):

Gene Expression ◽

Dynamic Models ◽

Hydrophobic Interactions ◽

Reductase Activity ◽

Syringic Acid ◽

Stoichiometric Ratio ◽

Diabetic Cataract ◽

Interaction Sites ◽

Qrt Pcr ◽

Lens Transparency

Objective. Effects of Syringic acid (SA) extracted from dendrobii on diabetic cataract (DC) pathogenesis were explored.Methods. Bothin vitroandin vivoDC lens models were established using D-gal, and proliferation of HLEC exposed to SA was determined by MMT assay. After 60-day treatment with SA, rat lens transparency was observed by anatomical microscopy using a slit lamp. SA protein targets were extracted and isolated using 2-DE and MALDI TOF/TOF. AR gene expression was investigated using qRT-PCR. Interaction sites and binding characteristics were determined by molecule-docking techniques and dynamic models.Results. Targeting AR, SA provided protection from D-gal-induced damage by consistently maintaining lens transparency and delaying lens turbidity development. Inhibition of AR gene expression by SA was confirmed by qRT-PCR. IC50of SA for inhibition of AR activity was 213.17 μg/mL. AR-SA binding sites were Trp111, His110, Tyr48, Trp20, Trp79, Leu300, and Phe122. The main binding modes involved hydrophobic interactions and hydrogen bonding. The stoichiometric ratio of non-covalent bonding between SA and AR was 1.0 to 13.3.Conclusion. SA acts to prevent DC in rat lenses by inhibiting AR activity and gene expression, which has potential to be developed into a novel drug for therapeutic management of DC.

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In vivo cytokine and receptor gene expression during the rat hair growth cycle. Analysis by semi-quantitative RT-PCR

Experimental Dermatology ◽

10.1111/j.1600-0625.1996.tb00118.x ◽

1996 ◽

Vol 5 (4) ◽

pp. 202-212 ◽

Cited By ~ 19

Author(s):

Julic C. Little ◽

Katherine L. Redwood ◽

Stewart P. Granger ◽

Gail Jenkins

Keyword(s):

Gene Expression ◽

Hair Growth ◽

Receptor Gene ◽

Growth Cycle ◽

Rt Pcr ◽

Receptor Gene Expression

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Cultured dermal papilla cells induce follicle formation and hair growth by transdifferentiation of an adult epidermis

Development ◽

10.1242/dev.115.2.587 ◽

1992 ◽

Vol 115 (2) ◽

pp. 587-593 ◽

Cited By ~ 3

Author(s):

A.J. Reynolds ◽

C.A. Jahoda

Keyword(s):

Gene Expression ◽

Hair Follicle ◽

Hair Growth ◽

De Novo ◽

Dermal Papilla ◽

Dermal Papilla Cells ◽

Local Skin ◽

Structural Arrangement ◽

Adult Rat ◽

Skin Epidermis

Adult rat pelage follicle dermal papilla cells induced follicle neogenesis and external hair growth when associated with adult footpad skin epidermis. They thus demonstrated a capacity to completely change the structural arrangement and gene expression of adult epidermis—an ability previously undocumented for cultured adult cells. Isolation chambers ensured that de novo follicle formation must have occurred by eliminating the possibility of cellular contributions, and/or inductive influences, from local skin follicles. These findings argue against previous suggestions of vibrissa follicle specificity, and imply that the potential for hair follicle induction may be common to all adult papilla cells.

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