Linked Life Data

19951703

Source:http://linkedlifedata.com/resource/pubmed/id/19951703

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2010-2-17
pubmed:abstractText
UDP-glucuronosyltransferases (UGTs) catalyze the glucuronidation of a variety of xeno/endobiotics. UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain. In the present study, we investigated the role of N-glycosylation in the function of human UGT1A9. Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed. In comparison with the wild-type, these mutants showed decreased enzyme activities in parallel with the extent of the band shift in Western blot analysis. To evaluate the role of glycosylation in the enzyme activity, we produced unglycosylated UGT1A9 by treating HEK293 cells transiently transfected with expression plasmid with tunicamycin. The unglycosylated UGT1A9 was almost inactive, which was not an indirect effect of ER stress. To the contrary, the deglycosylated UGT1A9, which was produced by the treatment with Endo H under the non-denaturing condition, showed the same enzyme kinetics as the control. These results suggest that the glycosylation that occurs during translation is important for the folding of UGT1A9. The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins supported the findings. In conclusion, we found that the N-glycosylation has an important role in the folding of UGT1A9.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1873-2968
pubmed:author
pubmed:copyrightInfo
2009 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
79
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1165-72
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
N-Glycosylation plays a role in protein folding of human UGT1A9.
pubmed:affiliation
Kanazawa University, Kakuma-machi, Japan. nmiki@kenroku.kanazawa-u.ac.jp
pubmed:publicationType
Journal Article