scholarly journals Specific label-free and real-time detection of oxidized low density lipoprotein (oxLDL) using an immunosensor with three monoclonal antibodies

2014 ◽  
Vol 2 (5) ◽  
pp. 477-484 ◽  
Author(s):  
Gustavo Cabral-Miranda ◽  
E. H. G. Yamashiro-Kanashiro ◽  
Magnus Gidlund ◽  
M. Goreti F. Sales
1995 ◽  
Vol 73 (03) ◽  
pp. 543-545 ◽  
Author(s):  
Laurent Daviet ◽  
Marie-Christine Morel-Kopp ◽  
Cécile Kaplan ◽  
John L McGregor

SummaryThe human CD36 antigen is an integral membrane glycoprotein expressed by platelets, monocytes, endothelial cells and various tumor cell lines. CD36 acts as a receptor for thrombospondin, collagen, Plasmodium falciparum-infected erythrocytes and oxidized low- density lipoprotein. Individuals possessing the Naka-negative phenotype do not express CD36 and risk developing anti-CD36 isoantibodies upon blood transfusion or during pregnancy. In the present study, we have examined the interaction of an anti-Naka serum with recombinantly expressed CD36. Results obtained show that five functional CD36 monoclonal antibodies (OKM5, FA6-152, L103, ESIV-C7 and 10/5) prevent the binding of the anti-Naka serum whereas a single monoclonal antibody (13/10) has no effect. Consistent with this result, an epitope map of CD36 generated using cross-blocking experiments, indicates that the inhibitory monoclonal antibodies recognize closely- related epitopes whereas 13/10 reacts with a distinct CD36 determinant. Furthermore, we have demonstrated, in a recent study, that OKM5, FA6-152, L103 and 10/5 bind to the same CD36 domain defined by amino acids 155 to 183. Taken together, our results indicate that the 155-183 sequence is important for the binding of the anti-Naka serum to CD36 and may represent a surface-exposed, immunogenic and presumably functional region on human CD36.


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