Expression and Functional Characterization of a Rat Sulfotransferase (ST1A1) cDNA for Sulfations of Phenolic Substrates in COS-1 Cells

Ozawa, Shogo; Nagata, Kiyoshi; Gong, Da-Wei; Yamazoe, Yasushi; Kato, Ryuichi

doi:10.1254/jjp.61.153

Cited by 19 publications

(3 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In humans, there were no gender differences in platelet SULT activity toward 4-nitrophenol, which is attributed to various SULT1 members, including SULT1A1 (Marazziti et al, 1998). In contrast to humans and similar to mice, Sult1a1 expression and 4-nitrophenolsulfonation are male-predominant in several rat tissues such as liver and kidney (Singer et al, 1982; Ozawa et al, 1993; Liu and Klaassen, 1996b; Klaassen et al, 1998). This difference among rodents and between rodents and humans may be because 4-nitrophenol is not a selective substrate for Sult1a1 or may result from species differences in the hormonal regulation of Sult1a1 expression.…”

Section: Discussionmentioning

confidence: 97%

Mechanisms of gender-specific regulation of mouse sulfotransferases (Sults)

Alnouti

Klaassen

2010

Xenobiotica

View full text Add to dashboard Cite

Marked gender differences in the expression of sulfotransferases (Sults) are known to exist in several species including rats, mice and hamsters. However, the mechanism for this gender difference is not known. Therefore, in the present study, it was determined whether sex and/or growth hormone (GH) are responsible for the gender difference in the expression of Sults using gonadectomized (GNX), hypophysectomized (HX) and GH-releasing hormone receptor-deficient little (lit/lit) mouse models.Sult1a1 and Papss2 in liver and kidney, and Sult1d1 in liver are female-predominant in mice because of suppressive effects of both androgens and male-pattern GH secretion. Sult2a1/a2 is the most markedly female-predominant Sult in mouse liver due to suppressive effects of androgens and male-pattern GH secretion, as well as stimulatory effects by estrogens and female-pattern GH secretion. Sult3a1 is female-predominant in mouse liver due to suppressive effects of androgens as well as stimulatory effects of estrogens and female-pattern GH secretion. Sult1c1 expression is male-predominant in mouse liver and kidney because of stimulatory effects of androgens in males. Sult4a1 expression is female-predominant in mouse brain due to stimulatory effects of estrogens.In conclusion, gender-divergent Sults are mostly female-predominant and Sult1c1 is the only male-dominant Sult. The gender differences in expression of various mouse Sults are influenced by various mechanisms involving sex and/or GHs.

show abstract

Section: Discussionmentioning

confidence: 97%

Mechanisms of gender-specific regulation of mouse sulfotransferases (Sults)

Alnouti

Klaassen

2010

Xenobiotica

View full text Add to dashboard Cite

show abstract

“…Cultured normal human breast epithelial cells, as well as cultured mammary carcinoma cell lines, exhibit EST activity (128). A note of caution: it should be born in mind that the sulfonation of phenolic steroids can also be carried out by phenol sulfotransferases (88,129). Thus, detection of estrogen sulfonation does not necessarily indicate the presence of a specific EST, as distinct from a phenol sulfotransferase; difficulty in making this distinction is aptly illustrated in a recent study of EST activity in human fetal lung tissue (130).…”

Section: Tissue Distribution and Expressionmentioning

confidence: 99%

Steroid sulfotransferases

Strott¹

1996

Endocrine Reviews

View full text Add to dashboard Cite

“…Sulphotransferases, however, can convert some xenobiotics into ultimate carcinogens [8,9]. Regulation of either the activities or the expression of these enzymes is therefore under current investigation [10][11][12][13], and most recently this is being extended by molecular biological methods [14,15]. Although the liver is the organ generally accepted as the major site for sulphate conjugation [16,17], sulphotransferases are also present in several other locations [18][19][20] including lung [21].…”

Section: Introductionmentioning

confidence: 99%

Characterization of bovine tracheobronchial phenol sulphotransferase cDNA and detection of mRNA regulation by cortisol

Schauss

Henry

Palmatier

et al. 1995

Biochemical Journal

View full text Add to dashboard Cite

Phenol sulphotransferases esterify both endogenous and foreign hydroxylated aromatic compounds with sulphate. Since these enzymes participate in both hormone and drug metabolism, elucidating their regulation at both the enzymic and molecular levels may provide new understanding in several metabolic pathways. The primary structure of a bovine phenol sulphotransferase has been determined by isolation of the corresponding cDNA. Two partial bovine cDNAs were first isolated by probing a tracheal epithelial cell lambda gt11 cDNA library with a rat phenol sulphotransferase cDNA. These clones provided the sequences of the 5' and 3' ends of the predicted coding region. A contiguous cDNA was subsequently isolated by PCR using 5' and 3' oligonucleotide primers and the cDNA library as the template. The sequence of the resulting approx. 1 kbp cDNA predicted an amino acid sequence that included sequences determined for several tryptic peptides of the purified protein. Antiserum directed to a synthetic N-terminal peptide predicted by the cDNA sequence showed reactivity with the purified enzyme. High-level Trc-promoter-driven expression of the recombinant bovine enzyme was achieved in Escherichia coli. The bovine cDNA was used to determine relative steady-state levels of phenol sulphotransferase transcripts in bovine lung tissues; distal lung parenchymal RNA levels were 6-10-fold greater than those in tracheobronchial epithelium. Using a bronchial epithelial cell culture model, however, cortisol was observed to increase mRNA levels by 5-fold in both a dose- and time-dependent manner; this corresponds to previously reported glucocorticoid stimulation of phenol sulphotransferase activity in this system [Beckmann, Illig and Bartzatt (1994) J. Cell Physiol. 160, 603-610].

show abstract

Expression and Functional Characterization of a Rat Sulfotransferase (ST1A1) cDNA for Sulfations of Phenolic Substrates in COS-1 Cells

Cited by 19 publications

References 12 publications

Mechanisms of gender-specific regulation of mouse sulfotransferases (Sults)

Mechanisms of gender-specific regulation of mouse sulfotransferases (Sults)

Steroid sulfotransferases

Characterization of bovine tracheobronchial phenol sulphotransferase cDNA and detection of mRNA regulation by cortisol

Contact Info

Product

Resources

About