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- W2016114570 abstract "The 5-ene-steroid-3β-monosulfates (SMS) are accepted as potential intermediates in androgen biosynthesis in vivo. Evidence from this laboratory and others are reviewed to support the premise that despite low conversions, the physiological significance of the regulation of SMS cleavage is important for androgen biosynthesis primarily at the target site of responsive tissue. Steroid sulfatase enzyme, regardless of tissue source in mammals, appears to be a monomeric unit having a steroid sulfate binding-site and a second regulatory steroid binding-site. Monomer or its aggregates intimately associated with particulate cell membrane implicate both transport and metabolism of steroid hormones. A model is presented in which SMS (substrates) contribute to androgen biosynthesis through hormonally (steroid allosteric modifiers and inhibitors) regulated cleavages at the cell membrane by steroid sulfatase enzyme at the site of hormone (steroid product) utilization. This is suggested to occur at the blood-organ barrier in target tissues sensitive to androgens, and in particular as a means of regulating the level of androgens within the seminiferous tubule." @default.
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- W2016114570 title "Regulatory interactions for the control of steroid sulfate metabolism" @default.
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- W2016114570 doi "https://doi.org/10.1016/0022-4731(75)90148-x" @default.
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