Altered Cell Surface Glycosphingolipids of Murine Lymphocytes Belonging to Different Differentiation Pathways

Author(s):  
P. F. Mühlradt ◽  
B. Kniep ◽  
R. G. Gruner
1976 ◽  
Vol 21 (3) ◽  
pp. 563-578
Author(s):  
J.H. Temmink ◽  
J.G. Collard ◽  
J. Roosien ◽  
J.F. Van den Bosch

Two human lymphoblasts (Raji and EB3) and normal human peripheral lymphocytes were exposed to different concentrations of Concanavalin A and wheat germ agglutinin. The lectin-induced agglutination was determined and correlated with lectin-induced changes in the surface morphology of these cells as studied in a scanning electron microscope. Whenever the lectin induced high agglutinability in a cell type, it also invariably had a smoothing effect on the cell surface. In contrast, when cells did not agglutinate well with a certain lectin, their cell surface remained essentially rough (villous) after addition of the lectin. The correlation found between increased agglutinability and altered cell surface morphology upon treatment with certain lectins suggests that both phenomena result from one and the same process. Additional evidence for this postulate is presented.


2019 ◽  
Vol 20 (18) ◽  
pp. 4455 ◽  
Author(s):  
Enikő Szabó ◽  
Ákos Hornung ◽  
Éva Monostori ◽  
Márta Bocskai ◽  
Ágnes Czibula ◽  
...  

Altered cell surface glycosylation in congenital and acquired diseases has been shown to affect cell differentiation and cellular responses to external signals. Hence, it may have an important role in immune regulation; however, T cell surface glycosylation has not been studied in systemic lupus erythematosus (SLE), a prototype of autoimmune diseases. Analysis of the glycosylation of T cells from patients suffering from SLE was performed by lectin-binding assay, flow cytometry, and quantitative real-time PCR. The results showed that resting SLE T cells presented an activated-like phenotype in terms of their glycosylation pattern. Additionally, activated SLE T cells bound significantly less galectin-1 (Gal-1), an important immunoregulatory lectin, while other lectins bound similarly to the controls. Differential lectin binding, specifically Gal-1, to SLE T cells was explained by the increased gene expression ratio of sialyltransferases and neuraminidase 1 (NEU1), particularly by elevated ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 (ST6GAL1)/NEU1 and ST3 beta-galactoside alpha-2,3-sialyltransferase 6 (ST3GAL6)/NEU1 ratios. These findings indicated an increased terminal sialylation. Indeed, neuraminidase treatment of cells resulted in the increase of Gal-1 binding. Altered T cell surface glycosylation may predispose the cells to resistance to the immunoregulatory effects of Gal-1, and may thus contribute to the pathomechanism of SLE.


2002 ◽  
Vol 277 (32) ◽  
pp. 28749-28756 ◽  
Author(s):  
Manuel Ramos ◽  
Alberto Paradela ◽  
Miriam Vázquez ◽  
Anabel Marina ◽  
Jesús Vázquez ◽  
...  

2004 ◽  
Vol 190 (5) ◽  
pp. 957-966 ◽  
Author(s):  
Barbara‐Ann D. Conway ◽  
Karen K. Chu ◽  
Johan Bylund ◽  
Eleonora Altman ◽  
David P. Speert

1987 ◽  
Vol 23 (11) ◽  
pp. 1748-1749
Author(s):  
J. Finne ◽  
H. Haidvogl ◽  
S. Castori ◽  
T. Feizi ◽  
M.M. Burger

1987 ◽  
Vol 84 (5) ◽  
pp. 1361-1363 ◽  
Author(s):  
L. Jacob ◽  
M. A. Lety ◽  
R. C. Monteiro ◽  
F. Jacob ◽  
J. F. Bach ◽  
...  

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