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Abstract
The SULT2b gene family consists of a single gene capable of generating two functional transcripts utilizing different transcriptional start sites in the first exon. This results in the translation of two separate proteins, SULT2B1a and SULT2B1b, with different amino-terminal peptides and approximately 95% identical sequences. The second distinguishing feature of the SULT2B isoforms is the proline/serine-rich carboxy-terminal sequence. To date, presence of the SULT2B gene appears limited to mammals and there is also only limited conservation of structure or sequence of the carboxy-terminal peptide. Although both SULT2B1 messages are present in human tissues, to date, only the SULT2B1b protein has been detected in the tissues investigated. In contrast, selective expression of SULT2B1a has been detected in rodent brain, whereas SULT2B1b was expressed in skin and intestine. Characterization of the SULT2B1 isoforms has been limited by the inability to isolate reliably active SULT2B1b from tissues or cells. SULT2B1 cDNAs can be expressed in Escherichia coli and the expressed active enzymes show selectivity for sulfation of 3β-hydroxysteroids. SULT2B1b due to the binding properties of the amino-terminal peptides also shows high cholesterol sulfation activity. Although human SULT2B1b displays significant substrate cross-reactivity with SULT2A1, the isoforms have different tissue expression patterns. Human SULT2B1b also shows nuclear localization in selected tissues that appears related to serine phosphorylation of the carboxy-terminal peptide. Overall, the understanding of the properties and function of the SULT2B1 isoforms is limited and the structural variability of the unique amino- and carboxy-sequences suggests significant species differences that need to be investigated.