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Last update 08 May 2025

SULT2B1

Last update 08 May 2025

Basic Info

Synonyms

Alcohol sulfotransferase, HSST2, Hydroxysteroid sulfotransferase 2

+ [5]

Introduction

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Responsible for the sulfation of cholesterol (PubMed:12145317, PubMed:19589875). Catalyzes sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA) (PubMed:12145317, PubMed:16855051, PubMed:21855633, PubMed:9799594). Preferentially sulfonates cholesterol, while it has also significant activity with pregnenolone and DHEA (PubMed:12145317, PubMed:21855633). Plays a role in epidermal cholesterol metabolism and in the regulation of epidermal proliferation and differentiation (PubMed:28575648). Sulfonates pregnenolone but not cholesterol.

Drugs associated with SULT2B1

US20240400606

Patent Mining

Target

SULT2B1

Mechanism-

Active Org.

The Board of Trustees of the University of Illinois

Originator Org.

The Board of Trustees of the University of Illinois

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with SULT2B1

100 Translational Medicine associated with SULT2B1

0 Patents (Medical) associated with SULT2B1

111

Literatures (Medical) associated with SULT2B1

01 Jul 2025·Critical Reviews in Oncology/Hematology

Pharmacogenomics in pediatric oncology patients with solid tumors related to chemotherapy-induced toxicity: A systematic review

Review

Author: Uvdal, Hanna ; Hansson, Paula ; Blacker, Christopher ; Wadelius, Mia ; Green, Henrik ; Ljungman, Gustaf

Chemotherapy-induced toxicities remain challenging in pediatric oncology, affecting patient outcomes, hospital stays, and quality of life. Genetic variation can partly explain these toxicities, and pharmacogenomics could potentially optimize treatment. This review provides an overview of pharmacogenomic studies in relation to chemotherapy-induced toxicity in children with solid tumors. A systematic literature search was performed in PubMed, Embase, and Web of Science following PRISMA guidelines. Two independent reviewers assessed eligibility, risk of bias using ROBINS-I, and extracted data. Out of 9000 articles screened, 279 were deemed relevant, and 59 met the inclusion criteria by focusing on children with solid tumors and pharmacogenomics in relation to chemotherapy-induced toxicity. Following risk of bias assessment, 24 articles with low to moderate risk of bias were summarized. Identifying specific SNPs associated with toxicities proved challenging due to variability across studies. For methotrexate, the genes ABCC2, MTHFR, and SXR were associated with myelosuppression and hepatotoxicity. The genes ABCC3, COMT, ERCC2, GSTP1, GSTT1, LRP2, SLC22A2, and TPMT showed associations with ototoxicity due to platinum-based drugs. Anthracycline-induced cardiotoxicity was associated with CBR2, CELF4, GSTM1, HAS3, RARG, and SLC28A3, and further with HNMT and SLC22A2 in younger children, with ABCB4 in females, and with SULT2B1 in males. A dose-dependent effect of CELF4 on cardiotoxicity was noted with anthracycline doses over 300 mg/m². This review highlights the complexity and variability of pharmacogenomic associations with chemotherapy-induced toxicities in pediatric oncology. While certain genetic variants show associations with specific toxicities, larger multinational/center studies are needed to strengthen the associations and improve clinical guidelines.

01 Apr 2025·Liver International

Exosomal ETV4 Derived From M2 Macrophages Induces Growth, Glycolysis and Stemness in Hepatocellular Carcinoma by UpRegulating SULT2B1 Expression

Article

Author: Gu, Songgang ; Zhong, Haibin ; Xu, Qiaodong ; Ma, Zhiyan ; Chen, Xinyue ; Feng, Gengren

ABSTRACTBackgroundM2 macrophage‐derived exosomes have been identified to modulate hepatocellular carcinoma (HCC) progression. E‐twenty‐six (ETS) variant transcription factor 4 (ETV4) shows protumoral effects in HCC. Here, we aimed to probe whether ETV4 performed oncogenic effects on HCC by macrophage‐derived exosomes and its associated mechanism.MethodsExosomes were isolated from macrophages and co‐cultured with HCC cells. qRT‐PCR and western blotting were utilised for the detection of mRNA and protein. Cell survival was evaluated using EdU assay and flow cytometry. Glycolysis was determined by measuring the glucose uptake, lactate production, and ATP levels. Cell stemness was assessed by sphere formation and flow cytometry. The interaction between ETV4 and SULT2B1 (sulfotransferase family 2B member 1) was determined by a dual‐luciferase reporter and chromatin immunoprecipitation assays. In vivo assay was performed by establishing mouse xenograft models.ResultsETV4 was highly expressed in the exosomes of M2 macrophages and could be internalised by HCC cells. ETV4 derived from M2 macrophage exosomes promoted HCC cell proliferation, glycolysis and stemness in vitro, and enhanced HCC growth in nude mice. Mechanistically, ETV4 interacted with SULT2B1 and promoted it transcription. SULT2B1 silencing suppressed HCC cell proliferation, glycolysis and stemness. In addition, exosomal ETV4 derived from M2 macrophage performed its effects by modulating SULT2B1.ConclusionETV4 derived from M2 macrophage exosomes promoted HCC cell proliferation, glycolysis and stemness by interacting with SULT2B1, suggesting a novel insight into developing exosome‐based therapy for HCC.

01 Mar 2025·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Steroid sulfatase suppresses keratinization by inducing proteasomal degradation of E-cadherin via Hakai regulation

Article

Author: Chun, Young-Jin ; Kwon, Yeo-Jung ; Park, Hyemin ; Kwon, Tae-Uk ; Kang, Keon Wook ; Lee, Hyein ; Kwak, Ji-Heung

X-linked ichthyosis (XLI) is a genetic disorder characterized by a steroid sulfatase (STS) deficiency inducing excessive cholesterol sulfate accumulation and keratinization. Our study utilizes STS knockout mice to reproduce the hyperkeratinization typical of XLI, providing a valuable model for investigating the underlying mechanisms. From the experiment of STS-deficient keratinocytes using the CRISPR/Cas9 system, we observed upregulation of E-cadherin, which is associated with keratinocyte differentiation and stratification. This was accompanied by elevated levels of keratinization markers, including involucrin and loricrin. We also found an increased expression of SULT2B1, which converts cholesterol to cholesterol sulfate, further accelerating cholesterol sulfate accumulation. As a result, STS deficiency and cholesterol sulfate accumulation lead to decreased expression of Hakai, the ubiquitin E3 ligase for E-cadherin. With reduced Hakai, endocytosis and ubiquitin-mediated degradation of E-cadherin are inhibited, resulting in its stabilization. This stabilization of E-cadherin is accompanied by increased expression of involucrin and loricrin, which is suppressed when the N-terminal extracellular domain of E-cadherin, responsible for cell-cell adhesion, is genetically modified. We propose that inhibition of E-cadherin, genetic modification of the N-terminal extracellular domain, and treatment with miR-6766 targeting E-cadherin significantly reduce the expression of keratinization markers, suggesting a potential therapeutic approach. We further suggest that the increased expression of E-cadherin observed in keratinocytes with STS deficiency is regulated by Hakai, underscoring the central role of E-cadherin in the pathogenesis of XLI.

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SULT2B1

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