Document Detail


Human alpha galactosidase and alpha 1,2 fucosyltransferase concordantly inhibit xenoreactivity of NIH 3T3 cells with human serum.
MedLine Citation:
PMID:  12956935     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
AIM: To study the influence of the expression of human alpha galactosidase and alpha1,2 fucosyltransferase on Gal alpha 1,3 Gal and consequent xenoreactivity in NIH3T3 cells. METHODS: The expression levels of G antigen and H antigen and binding of human natural antibodies (IgG and IgM) and complement (C3c) to NIH3T3 cells were analyzed by flow cytometry. Western blot was employed to further determine the expression of glycoproteins of G antigen. Cytolysis assay with normal human serum was performed by MTT assay. RESULTS: Western blot showed that glycoproteins with molecular weight of 107 kDa, 98 kDa, 88 kDa, 56 kDa, 40 kDa, and 37 kDa were inhibited and even abrogated totally in alpha galactosidase transfectants and alpha 1,2 fucosyltransferase transfectants. The combined transfection of the two enzymes led to a much stronger inhibition of the glycoproteins. The binding of GS-IB4 was decreased by 57.4 % in alpha galactosidase transfectants, 28.8 % in alpha 1,2 fucosyltransferase transfectants, and 72.1 % in combined transfectants, respectively. In contrast, UEA-1 binding was increased about 6.7-fold, 6.0-fold, and 8.0-fold respectively. The xenoreactivity with human IgG was also reduced by 61.4 %, 67.0 %, and 73.4 %, respectively in the three kinds of transfectants. The resistance to cytolysis mediated by human serum was enhanced by 42.4 % in alpha galactosidase transfectants, 51.9 % in alpha 1,2 fucosyltranferase, and even 65.5 % in the combined transfectants. CONCLUSION: Although alpha galactosidase and alpha 1,2 fucosyltransferase had different biochemical properties, they could inhibit the expression of Gal alpha 1,3 Gal synergistically, leading to stronger resistance of xenograft against cytolysis.
Authors:
Jing-Lian Yan; Lu-Yang Yu; Li-He Guo
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Acta pharmacologica Sinica     Volume:  24     ISSN:  1671-4083     ISO Abbreviation:  Acta Pharmacol. Sin.     Publication Date:  2003 Sep 
Date Detail:
Created Date:  2003-09-05     Completed Date:  2004-02-10     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  100956087     Medline TA:  Acta Pharmacol Sin     Country:  China    
Other Details:
Languages:  eng     Pagination:  878-84     Citation Subset:  IM    
Affiliation:
Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China. lhguo@sunm.shcnc.ac.cn
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MeSH Terms
Descriptor/Qualifier:
3T3 Cells
Animals
Complement C3c / metabolism
Disaccharides / metabolism*
Fucosyltransferases / biosynthesis,  genetics*
Immunoglobulin G / metabolism
Immunoglobulin M / metabolism
Mice
Transfection
Transplantation, Heterologous
alpha-Galactosidase / biosynthesis,  genetics*
Chemical
Reg. No./Substance:
0/Disaccharides; 0/Immunoglobulin G; 0/Immunoglobulin M; 13168-24-6/galactosyl-(1-3)galactose; 80295-44-9/Complement C3c; EC 2.4.1.-/Fucosyltransferases; EC 2.4.1.69/galactoside 2-alpha-L-fucosyltransferase; EC 3.2.1.22/alpha-Galactosidase

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