Regulation of phenol sulfotransferase expression in cultured bovine bronchial epithelial cells by hydrocortisone

Beckmann, Joe D.; Illig, Mary; Bartzatt, Ronald

doi:10.1002/jcp.1041600324

Cited by 15 publications

(22 citation statements)

References 42 publications

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“…The first such demonstrations were performed in cultured bovine adrenocortical cells, where it was shown that glucocorticoid treatment produced substantial increases in SULT1A1 enzyme activity and mRNA content [21,22]. Subsequent studies in vivo and in primary cultured rat hepatocytes indicated that glucocorticoids regulate the expression of rat hepatic SULT1A1 [23].…”

Section: Sult Regulation By Steroid Hormone Receptorsmentioning

confidence: 99%

Regulation of Sulfotransferases by Xenobiotic Receptors

Runge‐Morris¹,

Ta²

2005

CDM

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The transcription factor networks that regulate basal and xenobiotic-modulated expression of the hepatic sulfotransferases affect the dynamics of xenobiotic detoxication, carcinogen bioactivation and metabolic homeostasis. Emerging evidence suggests that liver-enriched transcription factors, the aryl hydrocarbon (Ah) receptor and members of the nuclear receptor transcription factor superfamily all play integrated roles in the control of sulfotransferase gene transcription. Unlike the well known up-regulation of CYP1A1, expression of rat hepatic aryl (SULT1A1) and hydroxysteroid (SULT2A) sulfotransferase is suppressed in response to treatment with the prototypic Ah receptor ligand, 2, 3, 7, 8-tetrachlorodibenzo-p-dioxin. Glucocorticoid-inducible rat hepatic SULT1A1 gene transcription occurs through a glucocorticoid receptor (GR)-mediated mechanism, while human hepatic SULT1A1 does not display GR-inducible expression. By comparison, liver-enriched transcription factors, such as CCAAT/enhancer binding protein, are essential for the maintenance of basal and GR-inducible rat hepatic SULT2A expression. The transcriptional control of rodent and human hepatic SULT2A expression is subject to trans-activation by the environmental sensor, pregnane X receptor (PXR). IR0 (inverted repeat with zero intervening bases) motifs located in the 5'-flanking regions of rodent SULT2A genes are required for transcriptional activation by PXR and other nuclear receptors, including constitutive androstane receptor, farnesoid X receptor and vitamin D receptor. Peroxisome proliferator activated receptor alpha (PPARalpha) mediates the induction of human, but not rat, hepatic SULT2A gene transcription, thus implicating a role for fatty acids as endogenous regulators of hepatic sulfonation in humans. This review focuses on the xenobiotic sensors and transcription factor systems that regulate sulfotransferase gene expression.

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Section: Sult Regulation By Steroid Hormone Receptorsmentioning

confidence: 99%

Regulation of Sulfotransferases by Xenobiotic Receptors

Runge‐Morris¹,

Ta²

2005

CDM

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“…This tissue has a low basal level of phenol sulfotransferase expression as demonstrated both enzymologically and immunohistologically (Beckmann et al, 1993). Hydrocortisone and other corticosteroids, however, can stimulate the expression of this enzyme in cultured bovine bronchial epithelial cells by 3-5-fold (Beckmann et al, 1994). Here we report that the stimulatory effects of hydrocortisone can be attenuated with retinoic acid, which may have important implications for the dietary control of xenobiotic metabolism in the lung.…”

mentioning

confidence: 62%

“…Cell extracts were prepared by NP-40 detergent lysis method number two as previously described (Beckmann et al, 1994). TotaI protein concentrations were determined by a Coomassie Blue G-250 binding assay (Bio-Rad, Richmond, CA) using bovine serum albumin as the standard.…”

Section: Enzyme Extraction and Analysesmentioning

confidence: 99%

Retinoic acid inhibits hydrocortisone-stimulated expression of phenol sulfotransferase in bovine bronchial epithelial cells

Beckmann¹,

Palmatier²,

Kliewer³

1996

J. Cell. Physiol.

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The airway epithelium, which is commonly exposed to xenobiotics, contains the conjugative enzyme phenol sulfotransferase (PST). We have previously reported that hydrocortisone (HC) stimulates the expression of PST severalfold in cultured bovine bronchial epithelial cells (Beckmann et al., 1994, J. Cell. Physiol. 160:603-610). Here we report that this stimulation is attenuated by retinoic acid (RA). Dose-response measurements of both enzyme activities and mRNA levels indicated a 50% inhibition of HC-stimulated PST expression with 0.05 nM RA. Varied concentrations of RA had a general repressive effect on HC-stimulated PST expression, with no change in the half-maximal HC stimulatory concentration of 12.5 nM. Steady state kinetic measurements indicated no significant changes in apparent Km values of 3-5 microM for the acceptor substrate, 2-naphthol; only HC- and RA-dependent changes in Vmax were observed. These changes were likely due to altered enzyme expression, as evidenced by immunoblot and Northern blot hybridization analyses. Thus, the expression of PST within bronchial epithelial cells is not merely constitutive, but is subject to both positive and negative controls.

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“…SULT1A1 expression was previously observed to be induced by glucocorticoids in cultured bovine tracheobronchial epithelial cells (Beckmann et al, 1994;Schauss et al, 1995). These foundation studies implied a role for steroid receptors in the trans-species regulation of SULT1A1 transcription.…”

Section: Fang Et Almentioning

confidence: 78%

Transactivation of Glucocorticoid-Inducible Rat Aryl Sulfotransferase (Sult1a1) Gene Transcription

et al. 2003

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This article is available online at http://dmd.aspetjournals.org ABSTRACT:The purpose of the current study was to establish the role of the glucocorticoid receptor (GR) and androgen receptor (AR) transcription factors in the transactivation of rat aryl sulfotransferase (SULT1A1) gene transcription and to identify the functional hormone-responsive element(s) in the SULT1A1 gene. A cis-acting inverted repeat with three intervening bases (IR3) was identified in the 5-flanking of the SULT1A1 gene that mediates the transactivation of SULT1A1 gene transcription by both the GR and AR. CV-1 cells were cotransfected with SULT1A1-luciferase reporter plasmids and either wild-type or mutant GR or AR expression constructs. In cotransfectants expressing the wild-type GR, treatment with triamcinolone acetonide produced an ϳ4-to 6-fold induction of luciferase activity in IR3-containing SULT1A1 reporter plasmids. IR3-containing SULT1A1 reporter constructs were also activated by treatment with the synthetic androgen R1881 in cells cotransfected with wild-type but not mutant AR. In primary cultured rat hepatocytes, androgen-inducible expression of IR3-containing SULT1A1 reporter plasmids required cotransfection with AR expression plasmid. Targeted disruption of the SULT1A1 IR3 by mutation of a conserved GT sequence in the 3 half-site of the element ablated GR and AR responsiveness. These results indicate that a proximal IR3 element in the 5-flanking region of the rat SULT1A1 gene is sufficient for the transactivation of SULT1A1 gene transcription by the GR and AR, and that relative to the GR, functional AR activity is reduced in primary cultured rat hepatocytes.

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Regulation of phenol sulfotransferase expression in cultured bovine bronchial epithelial cells by hydrocortisone

Cited by 15 publications

References 42 publications

Regulation of Sulfotransferases by Xenobiotic Receptors

Regulation of Sulfotransferases by Xenobiotic Receptors

Retinoic acid inhibits hydrocortisone-stimulated expression of phenol sulfotransferase in bovine bronchial epithelial cells

Transactivation of Glucocorticoid-Inducible Rat Aryl Sulfotransferase (Sult1a1) Gene Transcription

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