Document Detail


N-linked oligosaccharides affect the enzymatic activity of CD39: diverse interactions between seven N-linked glycosylation sites.
MedLine Citation:
PMID:  15673609     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Rat CD39, a membrane-bound ectonucleoside triphosphate diphosphohydrolase that hydrolyzes extracellular nucleoside tri- and diphosphates, has seven potential N-glycosylation sites at asparagine residues 73, 226, 291, 333, 375, 429, and 458. To determine their roles in the structure and function of CD39, we mutated these sites individually or in combination by replacing asparagine with serine or glutamine and analyzed the surface expression and the enzymatic activity of the mutants. The results indicate that rat CD39 can be glycosylated at all seven sites when expressed in COS7 cells. Glycosylation sites 73 at the N terminus, 333 in the middle, and 429 and 458 at the C terminus were principally required for cell surface appearance of enzymatically active CD39. Whereas deletion of these sites individually had modest effects on surface ATPase activity, some double deletions of these sites had major effects on both surface activity and expression. The importance of these N-glycosylation sites is recognizable in other members of the ectonucleoside triphosphate diphosphohydrolase family.
Authors:
James J Wu; Lisa E Choi; Guido Guidotti
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.     Date:  2005-01-26
Journal Detail:
Title:  Molecular biology of the cell     Volume:  16     ISSN:  1059-1524     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2005 Apr 
Date Detail:
Created Date:  2005-03-31     Completed Date:  2005-08-24     Revised Date:  2013-06-09    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1661-72     Citation Subset:  IM    
Affiliation:
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Antigens, CD / genetics,  metabolism*
Apyrase / genetics,  metabolism*
COS Cells
Calcium / pharmacology
Cercopithecus aethiops
Enzyme Stability
Gene Expression Regulation, Enzymologic
Glycosylation
Mutation / genetics
Oligosaccharides / chemistry,  metabolism*
Rats
Grant Support
ID/Acronym/Agency:
HL-08893/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Antigens, CD; 0/Oligosaccharides; 7440-70-2/Calcium; EC 3.6.1.5/Apyrase; EC 3.6.1.5/CD39 antigen
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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