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In recent years, the enzymes which are involved in the formation of DHT in steroid target tissues have been well investigated, however, enzymes responsible for the catabolism and elimination of steroids in these tissues, in particular the uridine diphospho-glucuronosyltransferase (UGT) family of enzymes, have received much less attention. We have recently(More)
Genetic polymorphisms occur in many of the drug metabolizing enzymes. However, the effect of polymorphisms in the genes encoding phase II drug metabolizing UDP-glucuronosyltransferases is still undescribed, despite the many reported cases of variations in glucuronidation activities. Characterization of the UGT2B15(Y85) cDNA, which was isolated from human(More)
Uridine diphosphate glucuronosyltransferases (UGTs) are important phase II detoxification enzymes. Despite the expression of UGT proteins in many species, previous results have suggested that simians represent the most appropriate animal model to study the glucuronidation of steroids in extrahepatic steroid target tissues. Northern blot analysis using a(More)
UGT2B17 is a UDP-glucuronosyltransferase enzyme expressed in several extrahepatic steroid target tissues, including the human prostate, where it glucuronidates C19 steroids such as dihydrotestosterone (DHT), androsterone (ADT), and androstane-3alpha, 17beta-diol (3alpha-diol). To determine if UGT2B17 is regulated by physiological effectors of the human(More)
Evidence supporting the validity of the 'two dopamine receptor' hypothesis is presented. The availability of the 'first generation' of selective agonists and antagonists of the D-1 and the D-2 dopamine receptors provides pharmacological support for the hypothesis. The demonstration that stimulation of the D-2 receptor either inhibits or has no effect upon(More)
UDP-glucuronosyltransferase (UGT) enzymes belonging to the UGT2B subfamily catalyze the transfer of glucuronic acid to a large number of endogenous compounds, particularly steroids, to facilitate their elimination from target cells. A novel human UGT2B cDNA of 1666 bp was isolated and encodes a 529-amino acid protein named UGT2B28 type I. Glucuronidation(More)
Since the introduction of mediastinoscopy, there has been a great deal of discussion regarding indications for this technique and the significance of positive findings. We undertook this study to determine the role of clinical staging and the value of routine mediastinoscopy in the treatment selection of patients with primary lung cancer. From 1975 to 1983,(More)
The glucuronidation of steroid hormones is catalyzed by a family of UDP-glucuronosyltransferase (UGT) enzymes. Previously, two cDNA clones, UGT2B15 and UGT2B17, which encode UGT enzymes capable of glucuronidating C19steroids, were isolated and characterized. These proteins are 95% identical in primary structure; however, UGT2B17 is capable of conjugating(More)
A monkey cDNA, UGT2B18, encoding a UDP-glucuronosyltransferase (UGT) active on 3-hydroxyandrogens, has been isolated and characterized. Previous results suggested that the monkey represents the most appropriate animal model for studying the physiologic relevance of steroid UGTs. UGT2B18 was isolated from a cynomolgus monkey prostate cDNA library using human(More)
Variations in glucuronidation activities among different individuals have been reported; however, genetic polymorphisms in the genes encoding phase II drug metabolizing UDP-glucuronosyltransferases have not been studied extensively. A novel UGT2B cDNA clone UGT2B4(E458) was isolated from human prostate and LNCaP cell cDNA libraries. The cDNA encoding(More)