Estradiol induces class I alcohol dehydrogenase activity and mRNA in kidney of female rats

Qulali, Mona; Ross, Ruth Ann; Crabb, David W.

doi:10.1016/0003-9861(91)90213-3

Cited by 36 publications

(12 citation statements)

References 41 publications

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“…Furthermore, the male-dominant incidence of urolithiasis may be related to the activity/expression of rate-limiting enzymes that contribute to oxalate synthesis in the respective organs, e.g., alcohol dehydrogenase 1 (ADH-1/Adh-1; EC 1.1.1.1), which catalyzes the conversion of EG to glycoaldehyde, and hydroxyacid oxidase (HAO-1/Hao-1, EC 1.1.3.15), which converts glycolate to glyoxylate. Thus, in both rat kidneys (168,169) and liver (170-172) the Adh-1 activity and its mRNA expression were found to be female-dominant due to stimulation by estrogens, whereas Hao-1 activity and its mRNA expression in rat liver and kidneys were found to be maledominant due to stimulation by androgens and inhibition by estrogens (167,173,174). Although the enzymatic level suggests that oxalate metabolism is largely controlled by androgens, ovariectomized and EG-treated female rats showed significantly higher urinary oxalate excretion, Ca 2+ content and crystal deposition, and a higher expression of osteopontin mRNA in the kidneys, suggesting that female sex hormones may also affect the deposition of renal crystals on several levels (175).…”

Section: +mentioning

confidence: 94%

Oxalate: From the Environment to Kidney Stones

Brzica

Breljak

Burckhardt

et al. 2013

Archives of Industrial Hygiene and Toxicology

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Oxalate urolithiasis (nephrolithiasis) is the most frequent type of kidney stone disease. Epidemiological research has shown that urolithiasis is approximately twice as common in men as in women, but the underlying mechanism of this sex-related prevalence is unclear. Oxalate in the organism partially originate from food (exogenous oxalate) and largely as a metabolic end-product from numerous precursors generated mainly in the liver (endogenous oxalate). Oxalate concentrations in plasma and urine can be modifi ed by various foodstuffs, which can interact in positively or negatively by affecting oxalate absorption, excretion, and/or its metabolic pathways. Oxalate is mostly removed from blood by kidneys and partially via bile and intestinal excretion. In the kidneys, after reaching certain conditions, such as high tubular concentration and damaged integrity of the tubule epithelium, oxalate can precipitate and initiate the formation of stones. Recent studies have indicated the importance of the SoLute Carrier 26 (SLC26) family of membrane transporters for handling oxalate. Two members of this family [Sulfate Anion Transporter 1 (SAT-1; SLC26A1) and Chloride/Formate EXchanger (CFEX; SLC26A6)] may contribute to oxalate transport in the intestine, liver, and kidneys. Malfunction or absence of SAT-1 or CFEX has been associated with hyperoxaluria and urolithiasis. However, numerous questions regarding their roles in oxalate transport in the respective organs and male-prevalent urolithiasis, as well as the role of sex hormones in the expression of these transporters at the level of mRNA and protein, still remain to be answered.

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Section: +mentioning

confidence: 94%

Oxalate: From the Environment to Kidney Stones

Brzica

Breljak

Burckhardt

et al. 2013

Archives of Industrial Hygiene and Toxicology

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“…In our experiments, it is evident that the cycle of ADH expression is mediated on a pretranslational level, by control of gene transcription. ADH gene expression has been reported to be regulated by several hormones, such as: androgens (28); estrogens (29); glucocorticoids (10); growth hormone (12); and insulin-like growth factor I (30). The class I ADH gene regulatory region contains response elements for glucocorticoids (10), retinoic acids (12) and C/EBP (31).…”

Section: Figmentioning

confidence: 99%

Cyclic Expression of Class I Alcohol Dehydrogenase in Male Rats Treated with Ethanol

Badger

Höög²,

Svensson³

et al. 2000

Biochemical and Biophysical Research Communications

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“…It was reported that ADH class I transcript in mouse kidney was stimulated by testosterone treatment, whereas ADH class I transcript in mouse adrenal gland was reduced to less than 5% [41]. Estrogen treatment induced the expression of ADH class I mRNA in rat kidney [12,13] and rat liver [42]. Harada et al demonstrated that the administration of estrogen and progesterone increased ADH activities in rat liver, while that of testosterone decreased ADH activities [43].…”

Section: Discussionmentioning

confidence: 99%

“…Detection of ADH activity was performed essentially as described previously [12,13]. Briefly, tissues were homogenized in a double volume of 50 mM Hepes, pH 8.4 containing 0.5 mM dithiothreitol, using glassteflon homogenizer.…”

Section: Detection Of Alcohol Dehydrogenase Activitymentioning

confidence: 99%

Evidence for the Expression of Alcohol Dehydrogenase Class I Gene in Rat Uterus and Its Up-regulation by Progesterone

et al. 2008

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Abstract. The endometrium is one of the target tissues of the ovarian steroid hormones, estrogen and progesterone. In order to elucidate the mechanism of gene regulation in the endometrium, suppressive subtraction hybridization was performed to isolate the candidate genes controlled by progesterone in rat uterus. Alcohol dehydrogenase (ADH) class I gene was one of the candidate genes. Here we investigated the expression and regulation of ADH class I gene in rat uterus. The mRNA of ADH class I was detected in uterus by RT-PCR using specific primers. Using specific probe for ADH class I, in situ hybridization was performed to investigate localization in rat uterus. Positive signals were detected in the endometrial stromal cells of rat uterus by in situ hybridization and were not detected in endometrial epithelial cells and myometrium in rat uterus. Ovariectomized rats were treated with 17-β estradiol and progesterone and the uteri of these rats were used for Northern blot analysis and assay of the ADH activity. Northern blot analysis revealed that the expression of ADH class I mRNA in rat uteri was up-regulated approximately two-fold after progesterone treatment, but not estrogen. Likewise, ADH activity was approximately two-fold higher in progesterone-treated rat uteri compared with controls. This study demonstrated that ADH class I gene is progesterone-responsive in the uterus. This implies that progesterone might be involved with retinoic acid synthesis in the uterus, since ADH is the key enzyme for retinoic acid synthesis.

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Estradiol induces class I alcohol dehydrogenase activity and mRNA in kidney of female rats

Cited by 36 publications

References 41 publications

Oxalate: From the Environment to Kidney Stones

Oxalate: From the Environment to Kidney Stones

Cyclic Expression of Class I Alcohol Dehydrogenase in Male Rats Treated with Ethanol

Evidence for the Expression of Alcohol Dehydrogenase Class I Gene in Rat Uterus and Its Up-regulation by Progesterone

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