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Sulfation of vitamin D 3 ‐related compounds—identification and characterization of the responsible human cytosolic sulfotransferases
Author(s) -
Kurogi Katsuhisa,
Sakakibara Yoichi,
Suiko Masahito,
Liu MingCheh
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12767
Subject(s) - sulfation , cytosol , chemistry , sulfotransferase , biochemistry , calcitriol , sulfate , vitamin d and neurology , enzyme , biology , endocrinology , calcium , organic chemistry
While 25‐hydroxyvitamin D 3 3‐ O ‐sulfate is known to be present in circulation, how it is generated in the body remains unclear. This study aimed to investigate its sulfation in major human organs and to unveil the responsible cytosolic sulfotransferases ( SULT s). Of the vitamin D 3 ‐related compounds tested, 25‐hydroxyvitamin D 3 and 7‐dehydrocholesterol are preferentially sulfated by human organ cytosols. Among the 13 human SULT s, SULT 2A1 shows sulfating activity toward all vitamin D 3 ‐related compounds, whereas SULT 1A1 and SULT 2B1a/ SULT 2B1b show sulfating activity exclusively for, respectively, calcitriol and 7‐dehydrocholesterol. These findings suggest that the metabolic pathway leading to the formation of 25‐hydroxyvitamin D 3 3‐ O ‐sulfate may be mediated by the sulfation of 25‐hydroxyvitamin D 3 or by the conversion of 7‐dehydrocholesterol‐3‐ O ‐sulfate in the skin.