Steroid sulfatase function

As a mitochondrial P450 system, P450c11 is dependent on two electron transfer proteins, adrenodoxin reductase and adrenodoxin that transfer 2 electrons from NADPH to the P450 for each monooxygenase reaction catalyzed by the enzyme. In most respects this process of electron transfer appears similar to that of P450scc system that catalyzes cholesterol side chain cleavage. [9] Similar to P450scc the process of electrons transfer is leaky leading to superoxide production. The rate of electron leakage during metabolism depends on the functional groups of the steroid substrate. [10]

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The StAR protein was first identified, characterized and named by Dr. Douglas Stocco at Texas Tech University Health Sciences Center in 1994. [19] The role of this protein in lipoid CAH was confirmed the following year in collaboration with Dr. Walter Miller at the University of California, San Francisco . [20] All of this work follows the initial observations of the appearance of this protein and its phosphorylated form coincident with factors that caused steroid production by Dr. Nanette Orme-Johnson while at Tufts University . [21]

Gonadotropin-releasing hormone is encoded from a single gene on the short arm of chromosome 8p21-p11. The human gene contains 4 exons; exon 2 encodes pro-GnRH, exon 3 and part of exon 2 and 4 encode the GAP protein, and exon 4 encodes a long 3′ untranslated region. Molecular processing occurs primarily in the nucleus of the cell body (soma). After transcription, the mRNA is transported to the cytoplasm where translation takes place and it is converted into the decapeptide. GnRH and its cleavage products, GAP and pro-GnRH, are then transported to the nerve terminals where they are secreted in tandem into the portal circulation. 187, 189, 190

The mineralocorticoid pathway starts with 21-hydroxylation of progesterone to form deoxycorticosterone (DOC). The enzyme in this reaction, 21-hydroxylase, is encoded by the CYP21 gene. 11 , 12 Deoxycorticosterone is then converted to corticosterone through the action of 11β-hydroxylase. There are two distinct 11β-hydroxylase isoenzymes, both of which are encoded by two genes, CYP11B1 and CYP11B2 . 13 Corticosterone is hydroxylated at carbon 18 to form 18-hydroxycorticosterone, which is transformed to aldosterone by removal of two hydrogens (oxidation) at carbon 18. These two reactions are catalyzed by 18-hydroxylase and 18-hydroxysteroid dehydrogenase, respectively, which are encoded by the same gene, CYP11B2 . Transcription of CYP11B1 is regulated primarily by ACTH, whereas angiotensin II regulates CYP11B2 transcription. 14 , 15 Similarly, the glucocorticoid pathway begins with 17α-hydroxyprogesterone, which is converted to deoxycortisol and subsequently to cortisol by 21-hydroxylase and 11β-hydroxylase, respectively, in the same manner as the conversion of progesterone to corticosterone. A deficiency of 21-hydroxylase, 11β-hydroxylase, or 3β-HSD in the adrenals may result in congenital adrenal hyperplasia and female pseudohermaphroditism, manifested as a masculinized female fetus.

Steroid sulfatase function

steroid sulfatase function

Gonadotropin-releasing hormone is encoded from a single gene on the short arm of chromosome 8p21-p11. The human gene contains 4 exons; exon 2 encodes pro-GnRH, exon 3 and part of exon 2 and 4 encode the GAP protein, and exon 4 encodes a long 3′ untranslated region. Molecular processing occurs primarily in the nucleus of the cell body (soma). After transcription, the mRNA is transported to the cytoplasm where translation takes place and it is converted into the decapeptide. GnRH and its cleavage products, GAP and pro-GnRH, are then transported to the nerve terminals where they are secreted in tandem into the portal circulation. 187, 189, 190

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