High impact information on SULT1A1

• A computer search of the protein data banks revealed significant homology with several sulfotransferases: 71% with bovine placental estrogen sulfotransferase, 52% with rat liver phenol sulfotransferase, 35% with rat liver hydroxysteroid sulfotransferase, and 36% with rat liver senescence marker protein 2 [1].
• Thus, the expression of PST within bronchial epithelial cells is not merely constitutive, but is subject to both positive and negative controls [2].
• Retinoic acid inhibits hydrocortisone-stimulated expression of phenol sulfotransferase in bovine bronchial epithelial cells [2].
• The airway epithelium, which is commonly exposed to xenobiotics, contains the conjugative enzyme phenol sulfotransferase (PST) [2].
• The activities of monoamine oxidase (MAO), catechol-O-methyltransferase (COMT), phenol sulfotransferase (PST), alkaline phosphatase (AP), gamma-glutamyl transpeptidase (GT), and angiotensin converting enzyme (ACE) were quantitated in primary cultures of bovine brain microvessel endothelial cell monolayers and cerebral gray matter [3].

Biological context of SULT1A1

• Substrate specificity of phenol sulfotransferase from primary cultures of bovine brain microvessel endothelium [4].
• A Ms1I PCR/RFLP in the bovine phenol sulfotransferase gene [5].

Anatomical context of SULT1A1

• Therefore, results from this study suggest a potential role for PST as part of the "enzymatic" blood-brain barrier in regulating transendothelial passage of endogeneous catecholamines between the blood and the brain [4].
• Selected catecholamines, catecholamine metabolites, and p-nitrophenol at 5, 50, and 500 microM were used as substrates in PST assays of cytosol extracts [4].

Associations of SULT1A1 with chemical compounds

• Previous work with the bovine SULT1A1 has utilized the highly fluorescent substrate 7-hydroxycoumarin (7-HC, umbelliferone) as an acceptor substrate [Biochem. Biophys. Res. Commun. 261 (1999) 815] [6].
• Here, we report that inhibition of bovine SULT1A1 by CoA is time-dependent at neutral pH under non-reducing conditions [7].
• 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) [2].
• Inhibition of phenol sulfotransferase by pyridoxal phosphate [8].
• Inhibition and binding studies of coenzyme A and bovine phenol sulfotransferase [9].

References