The adrenal cortex is the outer region and also the largest part of an adrenal gland. It is divided into three separate zones: zona glomerulosa, zona fasciculata and zona reticularis. Each zone is responsible for producing specific hormones. It is also a secondary site of androgen synthesis.
The zona reticularis is the innermost layer of the adrenal cortex, lying deep to the zona fasciculata and superficial to the adrenal medulla. The cells are arranged cords that project in different directions giving a net-like appearance.
Steroid sulfatase (STS), or steryl-sulfatase, formerly known as arylsulfatase C, is a sulfatase enzyme involved in the metabolism of steroids. It is encoded by the STS gene.
3β-Hydroxysteroid dehydrogenase/Δ5-4 isomerase (3β-HSD) is an enzyme that catalyzes the biosynthesis of the steroid progesterone from pregnenolone, 17α-hydroxyprogesterone from 17α-hydroxypregnenolone, and androstenedione from dehydroepiandrosterone (DHEA) in the adrenal gland. It is the only enzyme in the adrenal pathway of corticosteroid synthesis that is not a member of the cytochrome P450 family. It is also present in other steroid-producing tissues, including the ovary, testis and placenta. In humans, there are two 3β-HSD isozymes encoded by the HSD3B1 and HSD3B2 genes.
HSD3B2 is a human gene that encodes for 3beta-hydroxysteroid dehydrogenase/delta(5)-delta(4)isomerase type II or hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2. It is expressed principally in steroidogenic tissues and is essential for steroid hormone production. A notable exception is the placenta, where HSD3B1 is critical for progesterone production by this tissue.
In enzymology, a steroid sulfotransferase is an enzyme that catalyzes the chemical reaction
Sulfotransferase 1A1 is an enzyme that in humans is encoded by the SULT1A1 gene.
Sulfotransferase 1A3/1A4 is an enzyme that in humans is encoded by the SULT1A3 gene.
Estrogen sulfotransferase is an enzyme that in humans is encoded by the SULT1E1 gene.
Sulfotransferase family cytosolic 2B member 1 is an enzyme that in humans is encoded by the SULT2B1 gene.
Sulfotransferase 1A2 is an enzyme that in humans is encoded by the SULT1A2 gene.
Sulfotransferase 1C2 is an enzyme that in humans is encoded by the SULT1C2 gene.
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 is an enzyme that in humans is encoded by the PAPSS1 gene.
Sulfotransferase 4A1 is an enzyme that in humans is encoded by the SULT4A1 gene.
3-keto-steroid reductase is an enzyme that in humans is encoded by the HSD17B7 gene.
Sulfotransferase family cytosolic 1B member 1 is an enzyme that in humans is encoded by the SULT1B1 gene.
Estradiol 17 beta-dehydrogenase 8 is an enzyme that in humans is encoded by the HSD17B8 gene.
Sulfotransferase 1C4 is an enzyme that in humans is encoded by the SULT1C4 gene.
Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2 is an enzyme that in humans is encoded by the NDST2 gene.
Phenol sulfur transferase deficiency, in short PST deficiency, is the lack or the reduced activity of the functional enzyme phenol sulfur transferase, which is crucial in the detoxification of mainly phenolic compounds by catalysing the sulfate conjugation of the hydroxyl groups in the toxic phenolic compounds to result in more hydrophilic forms for more efficient excretion. This metabolic disorder was first discovered in the late 1990s by Dr. Rosemary Waring during her researches with autistic children, which also made this deficiency commonly associated to the topics of autism. Mutations in the PST genes account for the genetic causes of the deficiency, of which single nucleotide polymorphism and methylation of promoters are two examples of mutations that respectively cause conformational abnormalities and diminished expressions to the enzyme, resulting in the reduced detoxification of phenolic compounds and regulation of phenolic neurotransmitter. The deficiency may cause symptoms like flushing, tachycardia, and depression, and be a risk factor for disorders like autism, migraine, and cancer, while it also limits the use of phenolic drugs in PST deficient patients. There is currently no drug available for treating PST deficiency.
