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Investigation of the Effects of SULT2A1 Genetic Polymorphisms on the Sulfation of Dehydroepiandrosterone by Human Cytosolic Sulfotransferase SULT2A1
Author(s) -
Abunnaja Maryam,
Liu MingCheh
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.lb163
Subject(s) - sulfotransferase , sulfation , dehydroepiandrosterone , single nucleotide polymorphism , biology , dehydroepiandrosterone sulfate , gene , microbiology and biotechnology , biochemistry , genotype , androgen , hormone
The cytosolic sulfotransferase (SULT) SULT2A1 is known to mediate the sulfation of dehydroepiandrosterone (DHEA) as well as many other sterols and steroids. The present study was designed to investigate how genetic polymorphisms of the human SULT2A1 gene may affect the sulfation of DHEA. Online databases were comprehensively searched to identify human SULT2A1 single nucleotide polymorphisms (SNPs). Of the 98 SULT2A1 non‐synonymous coding SNPs identified, seven were selected for further investigation. Site‐directed mutagenesis was used to generate cDNAs encoding these seven SULT2A1 allozymes, which were expressed in BL21 E . coli cells and purified by glutathione‐Sepharose affinity chromatography. Enzymatic assays revealed that purified SULT2A1 allozymes displayed differential sulfating activity toward DHEA. Kinetic analyses showed further differential catalytic efficiency and substrate affinity of the SULT2A1 allozymes, in comparison with wild‐type SULT2A1. These findings provided useful information concerning the effects of genetic polymorphisms on the sulfating activity of SULT2A1 allozymes. Support or Funding Information This work was supported in part by a grant from National Institutes of Health (Grant # R03HD071146). This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .