Abstract:
:The metabolism of progesterone (PROG) by cytochrome P450 17α-hydroxylase/17,20-lyase (CYP17A1) results in the formation of both 17α-hydroxyprogesterone (17-OHPROG) and 16α-hydroxyprogesterone (16-OHPROG) in humans. Unlike 17-OHPROG, 16-OHPROG is not metabolised further in steroidogenic tissue. While this metabolite can be readily detected in serum and urine, its physiological role remains unclear. This paper reviews the production of 16-OHPROG by human CYP17A1 by providing insight into the catalysis of PROG by CYP17A1 and highlights the role of Ala105 in the 16α-hydroxylation reaction. As 16-OHPROG has been putatively linked to reproductive function, we investigated the interaction of this steroid metabolite with both isoforms of the human progesterone receptor (hPR). We show for the first time that 16-OHPROG can bind to both hPR-A and hPR-B and act as an agonist for both receptors.
journal_name
Mol Cell Endocrinoljournal_title
Molecular and cellular endocrinologyauthors
Storbeck KH,Swart P,Africander D,Conradie R,Louw R,Swart ACdoi
10.1016/j.mce.2010.11.016subject
Has Abstractpub_date
2011-04-10 00:00:00pages
92-101issue
1-2eissn
0303-7207issn
1872-8057pii
S0303-7207(10)00544-7journal_volume
336pub_type
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