Enzymatic sulphation of bile salts in man.

Scand J Gastroenterol

Published: December 1979

An investigation of the occurrence of glycolithocholate sulphotransferase in the human gastrointestinal tract and kidney is described. In addition to in the liver, glycolithocholate sulphotransferase was found in the small intestine, but no activity could be detected in the gastric mucosa, colonic mucosa, or kidney.

Download full-text PDF

Source
http://dx.doi.org/10.3109/00365527909181383DOI Listing

Publication Analysis

Top Keywords

glycolithocholate sulphotransferase
8
enzymatic sulphation
4
sulphation bile
4
bile salts
4
salts man
4
man investigation
4
investigation occurrence
4
occurrence glycolithocholate
4
sulphotransferase human
4
human gastrointestinal
4

Similar Publications

Inhibition of Human Sulfotransferase 2A1-Catalyzed Sulfonation of Lithocholic Acid, Glycolithocholic Acid, and Taurolithocholic Acid by Selective Estrogen Receptor Modulators and Various Analogs and Metabolites.

J Pharmacol Exp Ther

June 2019

Department of Pharmacy, Faculty of Science (S.B., A.J.L.) and Department of Pharmacology, Yong Loo Lin School of Medicine (A.J.L.), National University of Singapore, Singapore, Singapore

Lithocholic acid (LCA) is a bile acid associated with adverse effects, including cholestasis, and it exists in vivo mainly as conjugates known as glyco-LCA (GLCA) and tauro-LCA (TLCA). Tamoxifen has been linked to the development of cholestasis, and it inhibits sulfotransferase 2A1 (SULT2A1)-catalyzed dehydroepiandrosterone (DHEA) sulfonation. The present study was done to characterize the sulfonation of LCA, GLCA, and TLCA and to investigate whether triphenylethylene (clomifene, tamoxifen, toremifene, ospemifene, droloxifene), benzothiophene (raloxifene, arzoxifene), tetrahydronaphthalene (lasofoxifene, nafoxidine), indole (bazedoxifene), and benzopyran (acolbifene) classes of selective estrogen receptor modulator (SERM) inhibit LCA, GLCA, and TLCA sulfonation.

View Article and Find Full Text PDF

Bile salt sulphotransferase activity in the liver of cholestatic infants.

Scand J Clin Lab Invest

July 1994

Department of Paediatrics, Karolinska Institutet, Huddinge, Hospital, Stockholm, Sweden.

A simple assay of bile salt sulphotransferase activity in human liver was developed. The system used glycolithocholate and PAPS as substrates. Km values for glycolithocholate and PAPs were 2.

View Article and Find Full Text PDF

Sulfation of hepatotoxic monohydroxy bile salts is viewed as an important detoxification mechanism. Bile salts are bound by fatty acid binding protein (FABP) with decreasing affinity as the extent of their hydroxylation increases. This binding has the potential to interfere with sulfation of monohydroxy bile salts and to augment their toxicity.

View Article and Find Full Text PDF

Bile salt sulfotransferase (BSS) activity for the fetal bile acid, 3 beta-hydroxy-5-cholenoate, was first detected in the fetus at 18-19 days of gestation and was twofold greater than for glycolithocholate. The near-term (20-21 days of gestation) and newborn pup BSS activity was only 5-10% of that in maternal liver. The 3 beta-hydroxy-5-cholenoate sulfotransferase activity rose by the second day of life to levels observed in the mature male, and to activities greater than the mature female by the time of weaning at 3 weeks of age.

View Article and Find Full Text PDF

The effect of aging on hepatic drug conjugation in 5- to 6-, 12- to 13- and 22- to 23-month-old female Fischer 344 rats was examined. The overall disposition of acetaminophen including the formation and elimination kinetics of its sulfate and glucuronide metabolites were used as in vivo probes. The effects of aging on selected in vitro drug metabolizing enzyme activities and on the pattern of phenol and bile salt sulfotransferase isoenzymes were also determined.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!