Four cypermethrin isomers induced stereoselective metabolism in H295R cells

Chirality ◽  
2020 ◽  
Vol 32 (8) ◽  
pp. 1107-1118
Author(s):  
Chenyang Ji ◽  
Chang Yu ◽  
Jianqiang Zhu ◽  
Yafei Cheng ◽  
Tian Tian ◽  
...  
Keyword(s):  
Stereoselective Metabolism ◽  
H295r Cells

Estrogenic effects of fluorinated diiodine alkanes in MCF‐7 cells, H295R cells and zebrafish embryo assays

2019 ◽  
Vol 39 (7) ◽  
pp. 945-954 ◽  
Author(s):  
Liang Lu ◽  
Jia Chang ◽  
Yunliang Qiu ◽  
Yan Chang ◽  
Jing Ma
Keyword(s):  
Zebrafish Embryo ◽  
Estrogenic Effects ◽  
H295r Cells ◽  
Mcf 7

scholarly journals Differential regulation of aldosterone synthase and 11beta-hydroxylase transcription by steroidogenic factor-1

2002 ◽  
Vol 28 (2) ◽  
pp. 125-135 ◽  
Author(s):  
MH Bassett ◽  
Y Zhang ◽  
C Clyne ◽  
PC White ◽  
WE Rainey
Keyword(s):  
Electrophoretic Mobility ◽  
Cell Model ◽  
Orphan Receptor ◽  
Luciferase Reporter ◽  
Zona Fasciculata ◽  
Genetic Linkage Analysis ◽  
Mobility Shift ◽  
Steroidogenic Factor 1 ◽  
Aldosterone Synthase ◽  
H295r Cells

11beta-Hydroxylase (hCYP11B1) and aldosterone synthase (hCYP11B2) are closely related isozymes with distinct roles in cortisol and aldosterone production respectively. Aldosterone synthase catalyzes the final step in aldosterone biosynthesis and is expressed only in the zona glomerulosa of the normal adrenal. 11beta-Hydroxylase catalyzes the final reaction in the production of cortisol and is expressed at higher levels in the zona fasciculata. The mechanisms causing differential expression of these genes are not well defined. Herein, we demonstrate contrasting roles for the orphan receptor steroidogenic factor-1 (SF-1) in the regulation of human (h) CYP11B1 and hCYP11B2. Human NCI-H295R (H295R) or mouse Y-1 cells were transiently transfected with luciferase reporter constructs containing 5'-flanking regions of hCYP11B1, hCYP11B2, human 17alpha-hydroxylase (hCYP17), human cholesterol side-chain cleavage (hCYP11A1) or mouse (m) cyp11b2 (mcyp11b2). Co-transfection of vectors encoding SF-1 increased expression of hCYP11B1, hCYP11A1 and hCYP17 constructs, but inhibited hCYP11B2 reporter activity. Murine, bovine and human SF-1 were unable to increase transcription of hCYP11B2 in H295R cells. Both hCYP11B2 and mcyp11b2 promoter constructs were inhibited similarly by human SF-1. In mouse Y-1 cells, reporter expression of hCYP11B2 and mcyp11b2 was very low compared with hCYP11B1 constructs, suggesting that this adrenal cell model may not be appropriate for studies of CYP11B2. Electrophoretic mobility shift assay demonstrated that SF-1 interacted with an element from both hCYP11B1 and hCYP11B2. However, mutation of this element, termed Ad4, did not prevent agonist stimulation of hCYP11B2 by angiotensin II or forskolin but blocked activity of hCYP11B1. In some, but not all, reports of genetic linkage analysis, a naturally occurring single nucleotide polymorphism within the Ad4 element of hCYP11B2 (-344C/T) has been associated with cardiovascular disease. Herein, we have demonstrated that this polymorphism influenced binding of SF-1 in electrophoretic mobility shift assays, with the C allele binding SF-1 more strongly than the T allele. However, when hCYP11B2 constructs containing these alleles were transfected into H295R cells, there was no difference in agonist-stimulated expression or the response of either reporter construct to co-expression with human SF-1. Taken together, these data suggest that SF-1 and the Ad4 element are not major regulators of adrenal hCYP11B2 gene expression. Thus far, hCYP11B2 is the first steroid hydroxylase gene which is not positively regulated by SF-1.

Species differences for stereoselective metabolism of ethofumesate and its enantiomersin vitro

Xenobiotica ◽  
2009 ◽  
Vol 39 (9) ◽  
pp. 649-655 ◽  
Author(s):  
W. Zhu ◽  
Z. Dang ◽  
J. Qiu ◽  
Y. Liu ◽  
C. Lv ◽  
...  
Keyword(s):  
Species Differences ◽  
Stereoselective Metabolism

scholarly journals Interleukin-8 Synthesis, Regulation, and Steroidogenic Role in H295R Human Adrenocortical Cells

Endocrinology ◽  
2006 ◽  
Vol 147 (2) ◽  
pp. 891-898 ◽  
Author(s):  
Damian G. Romero ◽  
Gaston R. Vergara ◽  
Zheng Zhu ◽  
Gina S. Covington ◽  
Maria W. Plonczynski ◽  
...  
Keyword(s):  
Immune System ◽  
Angiotensin Ii ◽  
Adrenal Gland ◽  
Interferon Γ ◽  
Cell Culture Supernatant ◽  
Adrenocortical Cells ◽  
Adrenal Cells ◽  
Endothelin 1 ◽  
H295r Cells ◽  
First Time

The adrenal gland secretes several cytokines, and cytokines modulate steroid secretion by this gland. In this study, a survey of cytokine production by H295R human adrenocortical cells demonstrated that these cells secreted IL-2, IL-4, IL-8, IL-10, IL-13, and TNFα but not IL-5, IL-12, or interferon-γ. IL-8 was the IL secreted at higher concentration. IL-8 secretion, its regulation, and role in steroidogenesis were further studied. Secreted ILs and steroids were measured by ELISA in cell culture supernatant. IL-8 mRNA was quantified by real-time RT-PCR. H295R cells and human adrenal gland expressed IL-8 mRNA. Angiotensin II, potassium, endothelin-1, IL-1α, IL-1β, TNFα, and Escherichia coli lipopolysaccharide dose-dependently increase IL-8 secretion by H295R cells after 24 h incubation. IL-6 had no effect on IL-8 secretion. Angiotensin II time-dependently increased IL-8 secretion by H295R cells up to 48 h. Angiotensin II caused a biphasic increase in IL-8 mRNA expression with a peak 6 h after stimulation. TNFα synergized angiotensin II, potassium, and IL-1α-mediated IL-8 secretion. IL-8 did not modify aldosterone or cortisol secretion by H295R cells under basal or stimulated (angiotensin II or potassium) conditions. In conclusion, it is demonstrated for the first time that human adrenal cells expressed and secreted IL-8 under the regulation of angiotensin II, potassium, endothelin-1, and immune peptides. Adrenal-secreted IL-8 is one point of convergence between the adrenal gland and the immune system and may have relevance in physiological and pathophysiological conditions associated with increased levels of aldosterone secretagogues and the immune system.

scholarly journals More than just hormones: H295R cells as predictors of reproductive toxicity

2014 ◽  
Vol 45 ◽  
pp. 77-86 ◽  
Author(s):  
Jodi M. Maglich ◽  
Max Kuhn ◽  
Robert E. Chapin ◽  
Mathew T. Pletcher
Keyword(s):  
Reproductive Toxicity ◽  
H295r Cells

scholarly journals CREM confers cAMP responsiveness in human steroidogenic acute regulatory protein expression in NCI-H295R cells rather than SF-1/Ad4BP

2006 ◽  
Vol 191 (1) ◽  
pp. 327-337 ◽  
Author(s):  
Teruo Sugawara ◽  
Noriaki Sakuragi ◽  
Hisanori Minakami
Keyword(s):  
Promoter Activity ◽  
Activity Level ◽  
Expression Vectors ◽  
Camp Response Element ◽  
Star Protein ◽  
Protein Levels ◽  
Sirna Treatment ◽  
H295r Cells ◽  
Steroidogenic Acute Regulatory ◽  
Camp Induction

Steroidogenic acute regulatory (StAR) protein plays a critical role in steroid hormone synthesis. Tropic hormones induce human StAR gene expression by a cAMP-dependent pathway. Steroidogenic factor-1/adrenal-4-binding protein (SF-1/Ad4BP) plays an important role in the expression of human StAR gene. We investigated the mechanism of cAMP responsiveness in human StAR gene expression in NCI-H295R cells. The StAR promoter activity and protein levels in cells subjected to various treatments were examined. Anti-SF-1/Ad4BP IgG transfection treatment resulted in decreases in the basal StAR promoter activity and StAR protein levels, but did not affect cAMP-stimulated promoter activity and protein levels. The basal and cAMP-stimulated StAR promoter activity levels were reduced in SF-1/Ad4BP mutant (G35E)-transfected cells, but the cAMP induction of StAR promoter activity in response to 1 mM 8-Br-cAMP was not inhibited when G35E SF-1/Ad4BP mutant expression vectors were co-transfected with cAMP-response element-binding (CREB) expression vectors. Although the basal StAR mRNA expression and protein levels were decreased by SF-1/Ad4BP-siRNA treatment, the cAMP-stimulated StAR mRNA expression and protein levels did not change. The basal StAR promoter activity level was not decreased by cAMP-response element modulator (CREM)-siRNA treatment, but the cAMP-stimulated StAR promoter activity level, the magnitude of cAMP induction of StAR promoter, and the cAMP-stimulated StAR protein level were decreased. The cAMP induction of StAR promoter activity in cells was inhibited when S117ACREM mutant expressionvectors were transfected. We conclude that inhibition of the function of SF-1/Ad4BP does not reduce the cAMP induction of StAR promoter activity and protein level. CREM is needed to confer cAMP responsiveness in human StAR protein expression.

scholarly journals Stereoselective Metabolism of Carvedilol by the β-Naphthoflavone-Inducible Enzyme in Human Intestinal Epithelial Caco-2 Cells

2007 ◽  
Vol 30 (10) ◽  
pp. 1930-1933 ◽  
Author(s):  
Kazuya Ishida ◽  
Mutsuko Honda ◽  
Takako Shimizu ◽  
Masato Taguchi ◽  
Yukiya Hashimoto
Keyword(s):  
Intestinal Epithelial ◽  
Stereoselective Metabolism ◽  
Inducible Enzyme
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