Disease relevance of SULT2B1

• This fluorometric assay was used to determine the activities of AST as purified form and in crude extracts of pig liver, rat liver, and Escherichia coli [1].

High impact information on SULT2B1

• The gene for human hydroxysteroid sulfotransferase (SULT2B1) encodes two peptides, SULT2B1a and SULT2B1b, that differ only at their amino termini [2].
• In addition, the amino-terminal helix comprising residues Asp19 to Lys26, which determines the specificity difference between the SULT2B1 isoforms, becomes ordered upon pregnenolone binding, covering the substrate binding pocket [2].
• Thus, if the gene for SULT2B1 employs exon 1B, cholesterol sulfotransferase is synthesized, whereas if exon 1A is used, pregnenolone sulfotransferase is produced [3].
• cDNAs for rat SULT2B1 steroid/sterol sulfotransferase isoforms were cloned, and the encoded proteins overexpressed, purified and characterized [4].
• Cloning, characterization and tissue expression of rat SULT2B1a and SULT2B1b steroid/sterol sulfotransferase isoforms: divergence of the rat SULT2B1 gene structure from orthologous human and mouse genes [4].

Biological context of SULT2B1

• The divergence in 5'-terminal sequences of the two SULT2B1 cDNAs resulted from alternative transcription initiation prior to different 5' exons, combined with alternative splicing [5].
• The substrate specificity of the expressed SULT2B1 isoforms suggests that these enzymes are capable of regulating the activity of adrenal androgens in human tissues via their inactivation by sulfation [6].
• Biochemical characterization and tissue distribution of human SULT2B1 [7].
• Analysis of the deduced amino acid sequences revealed that one represents a novel member of the phenol sulfotransferase family and the other is highly homologous to human SULT2B1 hydroxysteroid sulfotransferases [8].

Anatomical context of SULT2B1

• Northern blot analysis demonstrated the presence of SULT2B1 mRNA species approximately 1.4 kb in length in human placenta, prostate, and trachea and-faintly-in small intestine and lung [5].
• Expression of the two human SULT2B1 cDNAs in COS-1 cells showed that both of the encoded proteins catalyzed sulfation of the prototypic hydroxysteroid SULT substrate, dehydroepiandrosterone, but both failed to catalyze the sulfate conjugation of 4-nitrophenol or 17beta-estradiol, prototypic substrates for the phenol and estrogen SULT subfamilies [5].
• No SULT2B1 message was observed in RNA isolated from human liver, colon, lung, kidney, brain, or testis tissue [6].
• In contrast to the limited tissue distribution of SULT2A1, SULT2B1 was detected in a variety of hormone-responsive tissues including placenta, ovary, uterus, and prostate [7].
• Immunoblot analysis of human lung tissue with a specific rabbit anti-SULT2B1 polyclonal antibody detected only SULT2B1b immunoreactive protein in human lung cytosol [9].

Associations of SULT2B1 with chemical compounds

• Both SULT2B1 enzymes also sulfonated dihydrotestosterone [7].
• The catalytic activity toward dehydroepiandrosterone and dihydrotestosterone, biologically important androgens, coupled with expression in prostate suggests that SULT2B1 may play a novel regulatory role that protects against the mitogenic effects of androgens [7].
• The change of fluorescence intensity of 4-methylumbelliferone corresponded directly to the amount of active AST and was sensitive enough to measure nanogram or picomole amounts of the enzyme activity [1].
• Human cytosolic sulfotransferase 2B1: Isoform expression, tissue specificity and subcellular localization [10].

Other interactions of SULT2B1

• The outstanding structural feature that distinguishes the SULT2B1 isoforms from the prototypical SULT2A1 isozyme is the presence of extended amino- and carboxyl-terminal ends in the former [3].
• The recombinant PST did not use the alcohol substrate under the designed condition, and the sensitivity for AST activity was found to be comparable to that of radioactive assay as reported in the literature [1].
• SULT1C2 expression was abundant in all cell types, whereas that of SULT1E1, SULTIBI or SULT2B1 was restricted to a specific cell type [11].

Analytical, diagnostic and therapeutic context of SULT2B1

• Northern blot analysis and SULT2B1 isoform specific RT-PCR detected only SULT2B1b message in human lung tissue [9].

References