Identification of diabetic nephropathy-selective proteins in human plasma by multi-lectin affinity chromatography and LC-MS/MS

2010 ◽  
Vol 4 (6-7) ◽  
pp. 644-653 ◽  
Author(s):  
Jung-Mo Ahn ◽  
Byung-Gyu Kim ◽  
Myong-Hee Yu ◽  
In-Kyu Lee ◽  
Je-Yoel Cho
1989 ◽  
Vol 22 (2) ◽  
pp. 115-119 ◽  
Author(s):  
Joris R. Delanghe ◽  
Marc L. De Buyzere ◽  
Ivan K. de Scheerder ◽  
Uwe Faust ◽  
Roger J. Wieme

1991 ◽  
Vol 69 (4) ◽  
pp. 239-244 ◽  
Author(s):  
Erwin Regoeczi ◽  
J. Michael Kay ◽  
Paul A. Chindemi ◽  
Ouahida Zaimi ◽  
Kaye L. Suyama

The aim of this study was to examine the effect of reduced O2 tension on the glycosylation of transferrin. Rats were placed in a hypobaric chamber (380 mmHg) that corresponded to an altitude of 5486 m above sea level for 21 days. The animals responded with marked increases in hematocrit (from 44 to 76%) and cardiac weight, and with reductions in the concentration of plasma transferrin averaging 15%. Analyses of their plasma transferrin by serial anion-exchange and lectin affinity chromatography revealed no changes in the extent of glycan branching. However, there was a moderate rise in the proportion of fucosylated transferrin molecules (fucosylation index) and a slight decrease in the transferrin fraction bearing a tetrasialylated biantennary glycan. The fucosylation index correlated positively with plasma transferrin concentrations in the test animals, but not in the controls. In contradistinction to the situation with transferrin, hypoxic rats exhibited a reduced fucosylation index of immunoglobulin G.Key words: fucosylation index, hypoxia, immunoglobulin G, lectin affinity chromatography, transferrin.


Sign in / Sign up

Export Citation Format

Share Document