3-Epi-25-hydroxyvitamin D3 is a poor substrate for SULT2A1: Analysis of its 3-sulfate in cord plasma and recombinant human SULT2A1 incubate

Yusuke Yoshimura, Moeka Togashi, Shoujiro Ogawa, Tatsuya Higashi

Research output: Contribution to journalArticle

Abstract

A variety of metabolites derived from 25-hydroxyvitamin D3 [25(OH)D3], including its 3-epimer [Epi-25(OH)D3] and 3-O-sulfate [25(OH)D3-3S], is found in human plasma/serum. We hypothesized that the 3-O-sulfate of Epi-25(OH)D3 [Epi-25(OH)D3-3S] might be present in plasma/serum. Clarifying this point could improve our understanding of the metabolism of vitamin D3. In this study, we first carefully analyzed the cord plasma samples by derivatization-assisted liquid chromatography/electrospray ionization-tandem mass spectrometry and demonstrated the occurrence of Epi-25(OH)D3-3S in the plasma. However, the concentration ratio of Epi-25(OH)D3-3S to 25(OH)D3-3S (sulfated form) was infinitely lower than the ratio of Epi-25(OH)D3 to 25(OH)D3 (unconjugated form). To determine what caused this result, we next performed an in vitro experiment of the 3-O-sulfation for 25(OH)D3 and Epi-25(OH)D3 using the recombinant human sulfotransferase (SULT) 2A1. This in vitro experiment revealed that Epi-25(OH)D3 is a poor substrate for the 3-O-sulfation catalyzed by SULT2A1 as compared to 25(OH)D3. This substrate specificity of SULT2A1 would be the main cause for the result obtained from the analysis of the cord plasma samples.

Original languageEnglish
Article number108695
JournalSteroids
Volume162
DOIs
Publication statusPublished - Oct 2020

Keywords

  • 3-Epi-25-hydroxyvitamin D
  • Cord plasma
  • SULT2A1
  • Substrate specificity
  • Sulfation

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