Sulfotransferase family 1C member 2 (SULT1C2)

Sulfotransferase family 1C member 2 (SULT1C2) is a cytosolic enzyme involved in phase II detoxification, primarily catalyzing the sulfate conjugation of phenolic compounds using 3'-phospho-5'-adenylyl sulfate (PAPS) as a donor. This reaction increases the water solubility of various drugs, hormones, neurotransmitters, and environmental toxins, facilitating their excretion via urine or bile. SULT1C2 is expressed in tissues such as stomach, kidney, thyroid, and fetal liver. It does not conjugate steroids or dopamine, but uniquely sulfates carcinogens such as N-hydroxy-2-acetylaminofluorene, producing reactive DNA-adduct forming intermediates that are implicated in mutagenesis and cancer development. In mitochondria, SULT1C2 can sulfate cholesterol, producing cholesterol sulfate, which alters mitochondrial membrane organization and increases respiratory capacity, conferring protection against ischemia/reperfusion injury. Expression of this enzyme may be upregulated by environmental factors such as cigarette smoke and possibly regulated by vitamin D3. Two splice variants are known, but clinical drugs directly targeting SULT1C2 are not established. Substrate inhibition and excessive activation of pro-carcinogens are important safety considerations for its therapeutic targeting.

Other names

Sulfotransferase 1C2SULT1C2SULT1C1ST1C2SULT1C#1ST1C1humSULTC2sulfotransferase family, cytosolic, 1C, member 1sulfotransferase family, cytosolic, 1C, member 2

Drug/metabolite is conjugated by addition of sulfonate group via PAPS, increasing water solubility, facilitating excretion. Sulfonation of carcinogens produces reactive intermediates that may form DNA adducts. Modifies cholesterol in mitochondria, influencing respiration and membrane properties.