Cycloastragenol mediates activation and proliferation suppression in concanavalin A-induced mouse lymphocyte pan-activation model

2017 ◽  
Vol 39 (3) ◽  
pp. 131-139 ◽  
Author(s):  
Chenghong Sun ◽  
Mingmin Jiang ◽  
Li Zhang ◽  
Jian Yang ◽  
Guimin Zhang ◽  
...  
2012 ◽  
Vol 61 (6) ◽  
pp. 623-634 ◽  
Author(s):  
Xiangfeng Zeng ◽  
Tong Wang ◽  
Cairong Zhu ◽  
Yanxia Ye ◽  
Bing Song ◽  
...  

Author(s):  
B. Monis ◽  
D. Lis ◽  
I. Parlanti ◽  
A. R. Eynard ◽  
M. A. Valentich ◽  
...  

We are gathering evidences which indicate ultrastructural variations and chemical heterogeneity of certain glycocalyces as well as hormone dependence of some of them. Thus, in the lumenal glycocalyx of renal collecting tubules of the guinea-pig granular and filamentous structures were seen (1, fig. 1). By isolation, chemical analysis and cellulose acetate electrophoresis in various buffers of tubular membrane material, glycopeptides and glycosaminoglycans were identified (fig. 2).Guinea-pig and rat transitional epithelium of urinary tract showed a filamentous lumenal glycocalyx demonstrable with ruthenium red (fig. 3) but which only in part stained with concanavalin A. Chemical and electrophoretic data indicated that urothelium contains glycoproteins, glycosaminoglycans and glycolipids.The glycocalyx of the fat globule membrane of milk of several species has a granular appearance as shown by cationic dyes and by concanavalin A (2, 3, fig. 4 and 5). Also, several glycoproteins were isolated and identified on polyacrilamide gel electrophoresis (fig. 6). Glycosaminoglycans and certain glycolipids such as sulfatides were chemically identified in this glycocalyx.


2015 ◽  
Vol 41 (08) ◽  
Author(s):  
C Klein ◽  
T Wuestefeld ◽  
M Miyazaki ◽  
MP Manns ◽  
C Trautwein
Keyword(s):  

2018 ◽  
Vol 56 (01) ◽  
pp. E2-E89
Author(s):  
B Schiller ◽  
C Wegscheid ◽  
L Berkhout ◽  
A Zarzycka ◽  
U Steinhoff ◽  
...  
Keyword(s):  

1975 ◽  
Vol 33 (02) ◽  
pp. 354-360 ◽  
Author(s):  
Heinrich Patscheke ◽  
Reinhard Brossmer

SummaryConcanavalin A (CON A) causes platelets to aggregate. A Ca++-independent effect of CON A could be separated from a main effect which depends on Ca++. The main effect probably is a consequence of the CON A-induced platelet release reaction and therefore is platelet-specific. The weak residual effect observed in the presence of Na2EDTA may be due to a similar mechanism as has been demonstrated for CON A-induced aggregations of several other normal and malignant transformed animal cells.Na2EDTA did not inhibit the carbohydrate-specific binding capacity of CON A. Therefore, Na2EDTA appears not to demineralize the CON A molecules under these experimental conditions.α-methyl-D-glucoside inhibits the Ca++-independent as well as the Ca++-dependent effect of CON A.Pretreatment by neuraminidase stimulated the platelet aggregation induced by CON A. It is possible that removal of terminal sialic acid residues makes additional receptors accessible for the binding of CON A.


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