UDP-glucuronosyltransferase activity, expression and cellular localization in human placenta at term

Collier, A.C., Ganley, N.A., Tingle, M.D., Blumenstein, M., Marvin, K.W., Paxton, J.W., Mitchell, M.D. and Keelan, J.A. (2002) UDP-glucuronosyltransferase activity, expression and cellular localization in human placenta at term. Biochemical Pharmacology, 63 3: 409-419. doi:10.1016/S0006-2952(01)00890-5


Author Collier, A.C.
Ganley, N.A.
Tingle, M.D.
Blumenstein, M.
Marvin, K.W.
Paxton, J.W.
Mitchell, M.D.
Keelan, J.A.
Title UDP-glucuronosyltransferase activity, expression and cellular localization in human placenta at term
Journal name Biochemical Pharmacology   Check publisher's open access policy
ISSN 0006-2952
Publication date 2002-02
Sub-type Article (original research)
DOI 10.1016/S0006-2952(01)00890-5
Volume 63
Issue 3
Start page 409
End page 419
Total pages 11
Place of publication New York, N.Y. U.S.A.
Publisher Elsevier
Language eng
Subject 1103 Clinical Sciences
1114 Paediatrics and Reproductive Medicine
Formatted abstract
The activity, expression and localization of the UDP-glucuronosyltransferases (UGTs) were investigated in human placenta at term. UGT activity (measured with the substrate 4-methylumbelliferone (4-MU)) was observed in all 25 placentas sampled and maximum velocity (Vmax) ranged 13-fold from 5.1±0.9 to 66.9±17.5 nmol/min/mg protein (mean±SD). Substrate affinity (Km) ranged 5-fold from 246±24 to 1124±422 μM. Using reverse transcriptase-polymerase chain reaction (RT-PCR), expression of the isoforms UGT2B4, 2B7, 2B10, 2B11 and 2B15 was observed in all (12/12) placentas sampled and expression of UGT2B17 was noted in 8/12 placentas. Northern analysis of the UGT2B7 isoform in 12 placentas revealed a 10-fold difference in expression with RT-PCR variability and the 13-fold variation observed in UGT activity. The presence of UGT2B4 and 2B7 proteins (52 and 56kDa, respectively) was demonstrated by Western blotting. The sites of placental UGT2B transcription (in situ hybridization) and protein expression (immunohistochemistry) were located in the syncytium of the placental trophoblasts bordering the placental villi. UGT1A proteins could not be observed with immunohistochemistry or Western blotting and expression could not be observed with RT-PCR. Our discovery of UGT expression and activity at the site of maternal-fetal exchange is consistent with a role for UGTs in detoxification of exogenous and endogenous ligands and the maintenance of placental function through clearance and regulation of steroid hormones. © 2002 Elsevier Science Inc. All rights reserved.
Keyword UDP-glucuronosyltransferase
Placenta
Placental metabolism
UGT gene expression
UGT2B
Immunohistochemistry
Human-liver
Glucuronyitransferase Activity
Postnatal-development
Rat-liver
Glucuronidation
Bilirubin
Identification
Metabolism
Cloning
UGT2B15
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: UQ Centre for Clinical Research Publications
 
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Created: Thu, 26 Aug 2010, 12:49:37 EST