Expression levels of the major human sulfotransferases (SULTs) involved in xenobiotic detoxification in a range of human tissues (i.e., SULT “pies”) are not available in a form allowing comparison between tissues and individuals. Here we have determined, by quantitative immunoblotting, expression levels for the five principal human SULTs—SULT1A1, SULT1A3/4, SULT1B1, SULT1E1, and SULT2A1—and determined the kinetic properties toward probe substrates, where available, for these enzymes in cytosol samples from a bank of adult human liver, small intestine, kidney, and lung. We produced new isoform-selective antibodies against SULT1B1 and SULT2A1, which were used alongside antibodies against SULT1A3 and SULT1A1 previously produced in our laboratory or available commercially (SULT1E1). Expression levels were derived using purified recombinant enzymes to construct standard curves for each individual isoform and immunoblot. Substantial intertissue and interindividual differences in expression were observed. SULT1A1 was the major enzyme (>50% of total, range 420-4900 ng/mg cytosol protein) in the liver, followed by SULT2A1, SULT1B1, and SULT1E1. SULT1A3 was completely absent from this tissue. In contrast, the small intestine contained the largest overall amount of SULT of any of the tissues, with SULT1B1 the major enzyme (36%), closely followed by SULT1A3 (31%), and SULT1A1, SULT1E1, and SULT2A1 more minor forms (19, 8, and 6% of total, respectively). The kidney and lung contained low levels of SULT. We provide a unique data set that will add value to the study of the role and contribution of sulfation to drug and xenobiotic metabolism in humans.

A nomenclature system for the cytosolic sulfotransferase (SULT) superfamily has been developed. The nomenclature guidelines were applied to 65 SULT cDNAs and 18 SULT genes that were characterized from eukaryotic organisms. SULT cDNA and gene sequences were identified by querying the GenBank databases and from published reports of their identification and characterization. These sequences were evaluated and named on the basis of encoded amino acid sequence identity and, in a few cases, a necessity to maintain historical naming convention. Family members share at least 45% amino acid sequence identity whereas subfamily members are at least 60% identical. cDNAs which encode amino acid sequences of at least 97% identity to each other were assigned identical isoform names. We also attempted to categorize orthologous enzymes between various species, where these have been identified, and the nomenclature includes a species descriptor. We present recommendations for the naming of allelic variants of SULT genes and their derived allozymes arising from single nucleotide polymorphisms and other genetic variation. The superfamily currently comprises 47 mammalian SULT isoforms, one insect isoform and eight plant enzymes, and collectively these sequences represent nine separate SULT families and 14 subfamilies. It is hoped that this nomenclature system will be widely adopted and that, as novel SULTs are identified and characterized, investigators will name their discoveries according to these guidelines.