[Binding capacity of aberrantly glycosylated serum IgA1 with human umbilical vein endothelial cells].
OBJECTIVE
To investigate the binding capacities of differently glycosylated IgA1 on human umbilical vein endothelial cells (HUVEC).


METHODS
Serum IgA1 was purified by jacalin affinity chromatography and then was desialylated and/or degalactosylated with neuraminidase and/or beta-galactosidase respectively. The efficacy of deglycosylations were assessed by peanut agglutinin (PNA) and vicia villosa lectin (VVL). Binding capacties of differently glycosylated IgA1 to HUVEC were evaluated by flow cytometry.


RESULTS
IgA1 could bind to HUVEC and the binding capacities of IgA1, DesIgA1 and Des/DeGalIgA1 were expressed by median fluorescence intensity (MFI) and they were 2.67+/-0.35, 4.62+/-1.09, 4.08+/-0.41 (IgA1 vs DesIgA1, P=0.015, IgA1 vs DesIgA1/DeGalIgA1, P=0.049, DesIgA1 vs DesIgA1/DeGalIgA1 , P>0.05), respectively.


CONCLUSIONS
IgA1 could bind to HUVEC directly, and the binding capacities of DesIgA1 and Des/DeGalIgA1 to HUVEC were significantly higher than that of normal IgA1. Serum IgA1, especially deglycosylated IgA1, might play some role in vascular lesions of IgAN.
Zhang
Jun-jun
JJ
Department of Nephrology, Peking University First Hospital, Peking University Institute of Nephrology; Beijing 100034, China.
Yu
Feng
F
Xu
Li-xia
LX
Zhang
Ying
Y
Zhao
Ming-hui
MH
D001665:Binding Sites; D042783:Endothelial Cells / Q000473:pathology*; D005922:Glomerulonephritis, IGA / Q000378:metabolism* / Q000473:pathology; D006031:Glycosylation; D006801:Humans; D007070:Immunoglobulin A / Q000097:blood*; D014471:Umbilical Veins / Q000473:pathology*
D007070:Immunoglobulin A; C042441:glycosylated IgA