Molecular biology of the human phenol sulfotransferase gene family

Dooley, Thomas P.

doi:10.1002/(sici)1097-010x(199809/10)282:1/2<223::aid-jez23>3.0.co;2-t

Cited by 11 publications

(1 citation statement)

References 50 publications

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“…A solitary SULT1A1 isoform has been characterized in all the above-mentioned species, but in humans, four SULT1A subfamily members have been identified (SULT1-A1, A2, A3, and A4; Blanchard et al, 2004;Hildebrandt et al, 2004). Their genes are all clustered on the short arm of chromosome 16 and are thought to have arisen following gene duplication or gene duplication plus recombination events (Aksoy et al, 1994;Dooley, 1998a;Rikke and Roy, 1996). The gene sequences of SULT1A1 and SULT1A2 are 93% similar, whereas SULT1A3 shares approximately 60% identity with the other two genes.…”

Section: Sult1a1mentioning

confidence: 99%

Human Sulfotransferases and Their Role in Chemical Metabolism

Gamage¹,

Barnett²,

Hempel³

et al. 2005

Toxicological Sciences

605

484

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Sulfonation is an important reaction in the metabolism of numerous xenobiotics, drugs, and endogenous compounds. A supergene family of enzymes called sulfotransferases (SULTs) catalyze this reaction. In most cases, the addition of a sulfonate moiety to a compound increases its water solubility and decreases its biological activity. However, many of these enzymes are also capable of bioactivating procarcinogens to reactive electrophiles. In humans three SULT families, SULT1, SULT2, and SULT4, have been identified that contain at least thirteen distinct members. SULTs have a wide tissue distribution and act as a major detoxification enzyme system in adult and the developing human fetus. Nine crystal structures of human cytosolic SULTs have now been determined, and together with site-directed mutagenesis experiments and molecular modeling, we are now beginning to understand the factors that govern distinct but overlapping substrate specificities. These studies have also provided insight into the enzyme kinetics and inhibition characteristics of these enzymes. The regulation of human SULTs remains as one of the least explored areas of research in the field, though there have been some recent advances on the molecular transcription mechanism controlling the individual SULT promoters. Interindividual variation in sulfonation capacity may be important in determining an individual's response to xenobiotics, and recent studies have begun to suggest roles for SULT polymorphism in disease susceptibility. This review aims to provide a summary of our present understanding of the function of human cytosolic sulfotransferases.

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Section: Sult1a1mentioning

confidence: 99%

Human Sulfotransferases and Their Role in Chemical Metabolism

Gamage¹,

Barnett²,

Hempel³

et al. 2005

Toxicological Sciences

605

484

View full text Add to dashboard Cite

show abstract

Expression Profiling of Human Sulfotransferase and Sulfatase Gene Superfamilies in Epithelial Tissues and Cultured Cells

Dooley

Haldeman-Cahill

Joiner

et al. 2000

Biochemical and Biophysical Research Communications

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134

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Molecular cloning and functional analysis of porcine SULT1A1 gene and its variant: a single mutation SULT1A1 causes a significant decrease in sulfation activity

2004

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The characterization of the SULT1A1 gene and its variants should have an important impact on the efforts to develop genetic markers to select for low skatole in pigs. Raising intact male pigs would have a significant economic impact on the pork industry; however, the presence of skatole (a major cause of boar taint) in meat from male pigs would be highly objectionable to consumers. It has been shown that the phase II metabolism of skatole metabolites by phenol sulfotransferase is related to the clearance of skatole in the liver. The aim of this study was to isolate and characterize the SULT1A1 gene from pig liver, examine its expression, identify genetic polymorphisms, and study how a genetic variation in this enzyme translates into interindividual variation in skatole levels. We show here that a substitution of A-->G at base 546 of SULT1A1 causes a significant decrease in its sulfation activity and thus may be at least partially responsible for a higher level of skatole in pigs. Our findings provide an important basis toward the goal of making it possible to predict the sulfation status in pigs and the development of genetic markers for low skatole.

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Molecular biology of the human phenol sulfotransferase gene family

Cited by 11 publications

References 50 publications

Human Sulfotransferases and Their Role in Chemical Metabolism

Human Sulfotransferases and Their Role in Chemical Metabolism

Expression Profiling of Human Sulfotransferase and Sulfatase Gene Superfamilies in Epithelial Tissues and Cultured Cells

Molecular cloning and functional analysis of porcine SULT1A1 gene and its variant: a single mutation SULT1A1 causes a significant decrease in sulfation activity

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