Email: fmorrel@nccu.edu
The UDP-glucuronosyltransferase (UGT) enzymes are endoplasmic reticulum membrane bound proteins that catalyze the transfer of glucuronyl group from uridine 5’-diphosphogulucoronic acid to insoluble molecules (endogenous/exogenous) including steroids there by facilitating their excretion. These enzymes are highly expressed in liver, which is the major site for detoxification, and extrahepatic tissues where endogenous steroids need to be glucuronidated. Deregulation of UGT2B genes expression has been proposed as one of the contributors of abnormal cell proliferation in cancer cells. UGT2B28, 17, and 15 are expressed in prostate cancer cells. In our lab, I study 1) the effect of EGF on regulation of these genes in androgen dependent (LNCaP) and androgen independent (PC-3) cells 2) unraveling the EGF signaling pathway(s) that lead to these effects.
Shafiee-Kermani F, Han SO, Miller WL. 2007 Chronic gonadotropin-releasing hormone inhibits activin induction of the ovine follicle-stimulating hormone beta-subunit: involvement of 3', 5'-cyclic adenosine monophosphate response element binding protein and nitric oxide synthase type I. Endocrinology 148: 3346-55
Su P, Shafiee-Kermani F, Gore AJ, Jia J, Wu JC, Miller WL. 2007 Expression and regulation of the beta-subunit of ovine follicle-stimulating hormone relies heavily on a promoter sequence likely to bind Smad-associated proteins. Endocrinology 148: 4500-8
Miller WL, Shafiee-Kermani F, Strahl BD, Huang HJ. 2002 The nature of FSH induction by GnRH. Trends Endocrinol Metab 13:257-63