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In the porcine testis, in addition to estrogen sulfates, the formation of numerous sulfonated neutral hydroxysteroids has been observed. However, their functions and the underlying synthetic pathways are still widely unclear. To obtain further information on their formation in postpubertal boars, the expression of sulfotransferases considered relevant for neutral hydroxysteroids ( SULT2A1, SULT2B1 ) was investigated in the testis and defined segments of the epididymis applying real-time RT-qPCR, Western blot and immunohistochemistry (IHC). Sulfotransferase activities were assessed in tissue homogenates or cytosolic preparations applying dehydroepiandrosterone and pregnenolone as substrates. A high  SULT2A1  expression was confirmed in the testis and localized in Leydig cells by IHC. In the epididymis,  SULT2A1  expression was virtually confined to the body.  SULT2B1  expression was absent or low in the testis but increased significantly along the epididymis. Immunohistochemical observations indicate that both enzymes are secreted into the ductal lumen via an apocrine mechanism. The results from the characterization of expression patterns and activity measurements suggest that SULT2A1 is the prevailing enzyme for the sulfonation of hydroxysteroids in the testis, whereas SULT2B1 may catalyze the formation of sterol sulfates in the epididymis. In order to obtain information on the overall steroidogenic capacity of the porcine epididymis, the expression of important steroidogenic enzymes ( CYP11A1, CYP17A1, CYP19, HSD3B1, HSD17B3, SRD5A2 ) was monitored in the defined epididymal segments applying real-time RT-qPCR. Surprisingly, in addition to a high expression of  SRD5A2  in the epididymal head, a substantial expression of  HSD3B1  was detected, which increased along the organ.

SULFATION PATHWAYS: Expression of SULT2A1, SULT2B1 and HSD3B1 in the porcine testis and epididymis