Sulfotransferase family 2B member 1 (SULT2B1)

Sulfotransferase family 2B member 1 (SULT2B1) is a cytosolic enzyme responsible for the sulfonation of hydroxysteroids including cholesterol, oxysterols, and DHEA, thereby playing a crucial role in modulating steroid hormone and lipid metabolism[4]. The protein exists as two isoforms (SULT2B1a and SULT2B1b), with SULT2B1b being the predominant form with functional significance in cancer biology[1]. SULT2B1b is frequently upregulated in colorectal and colon cancers, where it promotes tumor growth, invasion, and metastasis, in part by regulating lipid metabolism through direct interaction with stearoyl-CoA desaturase 1 (SCD1)[1][2]. High SULT2B1b expression is a poor prognostic marker, particularly for metastasis and reduced survival in colorectal cancer[1][2]. Conversely, in some tissues, SULT2B1 may suppress proliferation—for example, in esophageal squamous cell carcinoma, promoter hypermethylation causes downregulation, and forced expression can inhibit tumorigenesis[3]. In cardiovascular disease, elevated SULT2B1 expression in macrophages is associated with heightened inflammation and atherosclerosis via modulation of specific metabolites and signaling pathways[4]. The enzyme represents a promising target for anticancer therapy, with drugs such as lovastatin shown to inhibit its pro-metastatic effects in preclinical models[2].

Other names

Sulfotransferase 2B1HSST2ST2B1Alcohol sulfotransferaseHydroxysteroid sulfotransferase 2Sulfotransferase family cytosolic 2B member 1ARCI14sulfotransferase 2B1hydroxysteroid sulfotransferase SULT2B1a

Inhibition of SULT2B1 impedes cancer cell proliferation and invasion. Inhibition disrupts lipid metabolism and metastatic activity by modulating SCD1. Lovastatin suppresses SULT2B1-induced lipid metabolism and metastasis.