sulfotransferases (SULTs), which catalyze the sulfonation of small endogenous molecules and xenobiotics. In humans, SULTs 2A1 and 2B1 have been identified as the relevant sulfotransferases for neutral hydroxysteroids. SULT2A1 exhibits a broad substrate spectrum. In
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B Zimmer, L Tenbusch, M C Klymiuk, Y Dezhkam, and G Schuler
Denis Delić, Nicole Gailus, Hans-Werner Vohr, Mohamed Dkhil, Saleh Al-Quraishy, and Frank Wunderlich
-prevalent enzymes such as CYP2B9, CYP2B13, CYP3A41, CYP3A44, FMO3, SULT2A2, and SULT3A1 as well as the female-prevalent transporter BC014805. Remarkably, 27 genes, i.e. 50% of the genes, which were deregulated by testosterone, belonged to the categories phase I and
P A Sinclair, W J Gilmore, Z Lin, Y Lou, and E J Squires
.01) with respect to hepatic SULT2A1 activity (Fig. 1B ). In terms of testicular SULT2A1 activity, animals with the highest sulfotransferase activity had the highest concentrations of sulfated 5α-androstenone in peripheral plasma, with concentrations as high
Robin Haring, Henri Wallaschofski, Alexander Teumer, Heyo Kroemer, Angela E Taylor, Cedric H L Shackleton, Matthias Nauck, Uwe Völker, Georg Homuth, and Wiebke Arlt
molecular action . Endocrine Reviews 23 703 – 732 . ( doi:10.1210/er.2001-0040 ). Utriainen P Laakso S Jaaskelainen J Voutilainen R 2012 Polymorphisms of POR, SULT2A1 and HSD11B1 in children with premature adrenarche . Metabolism 61
G Schuler, Y Dezhkam, L Tenbusch, MC Klymiuk, B Zimmer, and B Hoffmann
, the highly estrogen-specific sulfotransferase SULT1E1 and the phenol sulfotransferase SULT1A1 in defined segments of the epididymis in comparison to their expression in the testis; (b) to comprehensively characterize STS and SULT1E1 expression in
Douglas A Gibson, Paul A Foster, Ioannis Simitsidellis, Hilary O D Critchley, Olympia Kelepouri, Frances Collins, and Philippa T K Saunders
metabolism of steroids following conjugation of a sulphate moiety. Sulphotransferases are a diverse gene family and the isozymes SULT1A1, SULT1E1, SULT2A1 and SULT2B1 have been associated with sulphation of steroids ( Mueller et al . 2015 ). SULT1E1
Yiyan Wang, Xiaoheng Li, Fei Ge, Kaiming Yuan, Zhijian Su, Guimin Wang, Qingquan Lian, and Ren-Shan Ge
± 2 (−6)* Maob Monoamine oxidase B 74 ± 9 50 ± 6 (−1) 14 ± 1 (−5)* Enpp2 Ectonucleotide pyrophosphatase 1469 ± 485 466 ± 36 (−4) 356 ± 19 (−4) Sult1a1 Sulfotransferase family, cytosolic, 1A1 948 ± 76 561 ± 17
Jon Wolf Mueller and Paul A Foster
10.1016/S0039-128X(68)80142-4 Zimmer B Tenbusch L Klymiuk MC Dezhkam Y Schuler G 2018 Expression of SULT2A1, SULT2B1 and HSD3B1 in the porcine testis and epididymis . Journal of Molecular Endocrinology 61 M43 – M57 . ( https
Julika Lietzow, Janine Golchert, Georg Homuth, Uwe Völker, Wenke Jonas, and Josef Köhrle
profile in ND mice. However, 12 genes (Cyp1a2, Cyp39a1, Cyp46a1, Cyp51, Cyp2d9, Ces1(f,g) and 2a, Sult1b1, Slc13a3, Slc39a4, Gpx6) were exclusively differentially expressed in HFD mice ( Fig. 4 ). Figure 4 The influence of 3,5-T 2 treatment on the
Gerald Thiel, Isabelle Müller, and Oliver G Rössler
′-phosphosulfate to the substrate. The family of cytosolic sulfotransferases includes the enzymes SULT2A1 and SULT2B1. Differential splicing of the SULT2B1 gene generates two isoforms, SULTB2B1a and SULT2B1b ( Shimizu et al . 2003 ), where SULT2B1a actively
