Distribution of 2-naphthol sulphotransferase and its endogenous substrate adenosine 3?-phosphate 5?-phosphosulphate in human tissues

Abstract

The activity of sulphotransferase towards 2-naphthol and the concentration of its endogenous substrate, adenosine 3'-phosphate 5'-phosphosulphate (PAPS), have been measured in five specimens of human liver, lung, and kidney, and the mucosa from the ileum and the ascending, descending and sigmoid colon. The activity of 2-naphthol sulphotransferase (mean nmol.min-1.mg-1 protein) was 1.82 (liver); 0.034 (kidney); 0.19 (lung); 0.64 (ileum); 0.47 (ascending colon); 0.50 (descending colon); 0.40 (sigmoid colon). The concentration of PAPS (mean nmol.g-1 wet tissue) was 22.6 (liver); 4.8 (kidney); 4.3 (lung); 12.8 (ileum); 8.1 (ascending colon); 7.5 (descending colon); 6.2 (sigmoid colon). The concentration of PAPS and the activity of 2-naphthol sulphotransferase were higher in the liver than in the extrahepatic tissues. There was significant difference between ileum and ascending colon, both the activity of sulphotransferase and the concentration of PAPS being higher in the former. 2-Naphthol sulphotransferase activity and the concentration of PAPS have consistent distribution patterns. Differences between the tissues studied were more marked for sulphotransferase than for its endogenous substrate.

Interindividual variability in the N‐sulphation of desipramine in human liver and platelets.

“…The Km value for PAPS was 0.04 mm which compares with its endogenous concentration of 0.02 mmol per kg liver (Cappiello et al, 1990a).…”

Detoxication of Benzo[a]pyrene-7,8-dione by Sulfotransferases (SULTs) in Human Lung Cells

“…It is possible that inhibition to SULT1E1 by B[a]P-7,8-catechol and other PAH catechols may increase the risk factor for estrogen-dependent genotoxicity. (34,44) and suggests that is reasonable to infer from our cell-based study that both enzymes will play a significant role in the detoxication of B[a]P-7,8-dione.…”

“…Estrogen o-quinones are structurally related to the PAH o-quinones, and multiple SULTs catalyze the sulfonation of estrogen catechols such as 2-hydroxyestradiol, 4-hydroxyestradiol, 2-hydroxyestrone, and 4-hydroxyestrone (31)(32)(33). SULT enzymes are also widely expressed and found in human lung (34). Therefore, it is imperative to investigate whether sulfonation of B[a]P-7,8-catechol by SULTs is a detoxication pathway for B[a]P-7,8-dione that will limit its ability to redox cycle.…”

Tamoxifen Induction of Aryl Sulfotransferase and Hydroxysteroid Sulfotransferase in Male and Female Rat Liver and Intestine

“…Intestinal epithelial cells, the main part of the gastrointestinal tract, represent the first barrier to exogenous compounds of foods or orally administered drugs that are metabolized before occurring in the circulation throughout the whole body. The presence of phenol-catalyzing sulfotransferases (PSTs) in human gastrointestinal tract has been reported (Pacifici et al, 1988;Cappiello et al, 1989;Chen et al, 2003). Polyphenolic flavonoids have been reported to induce phase II enzymes and interact with type II estrogen binding sites in the intestinal cells, thus implying their antineoplastic effects (Gee and Johnson, 2001).…”