Isolation and characterization of a human orphan UDP-glucuronosyltransferase, UGT2B11.

Glucuronidation is an important metabolic pathway for both endogenous and exogenous compounds. To isolate novel UGT2B cDNA clones, human prostate and LNCaP cell cDNA libraries were screened using a pool of steroid-specific UGT2B cDNA as probes. We have isolated a novel human cDNA of 1.7 kb in length containing an open reading frame of 1587 pb which encodes a deduced protein of 529 residues named UGT2B11. UGT2B11 share 91% identity in amino acids with UGT2B10, a UDP-glucuronosyltransferase (UGT) protein with unknown function. In agreement with other characterized UGT2B proteins, a Western blot analysis showed high levels of a 52-kDa protein present in a microsome preparation from HK293 cells stably transfected with the UGT2B11 cDNA. Despite the screening of 100 potential substrates, glucuronidation activity was not detected for the stably expressed UGT2B11 protein. However, UGT2B11 specific RT-PCR analysis revealed expression of the transcripts in a wide range of human tissues including the liver, kidney, mammary gland, prostate, skin, adipose, adrenal, and lung. The biological function of the UGT2B11 protein is unknown but its wide expression in human tissues raises the possibility that UGT2B11 may constitute an orphan UGT enzyme whose substrates specificity remain to be identified.