Effect of Aging on the Heterosaccharide Moiety of Glycoproteins: Study of Concanavalin A-Bound Glycoproteins and Glycosidases

2015 ◽  
pp. 78-84 ◽  
Author(s):  
Antonio Federico ◽  
Pasquale Annunziata ◽  
Isabella d�Amore ◽  
Silvia Palmeri
Keyword(s):  
Concanavalin A

Ultrastructural and chemical evidences of heterogeneity and hormone dependence of certain glycocalyces

1978 ◽  
Vol 36 (2) ◽  
pp. 322-323
Author(s):  
B. Monis ◽  
D. Lis ◽  
I. Parlanti ◽  
A. R. Eynard ◽  
M. A. Valentich ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Concanavalin A ◽  
Ruthenium Red ◽  
Transitional Epithelium ◽  
Membrane Material ◽  
Hormone Dependence ◽  
Cellulose Acetate Electrophoresis ◽  
Electrophoretic Data ◽  
Fat Globule ◽  
Collecting Tubules

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.

Die Aktivierung IL6/gp130 abhängiger Signalwege in Hepatozyten schützt die Leber vor Concanavalin A induzierter Hepatitis

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

The role of microbiota in concanavalin A-mediated liver injury

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

Concanavalin A-induced Aggregation of Human Blood Platelets

1975 ◽  
Vol 33 (02) ◽  
pp. 354-360 ◽  
Author(s):  
Heinrich Patscheke ◽  
Reinhard Brossmer
Keyword(s):  
Concanavalin A ◽  
Binding Capacity ◽  
Specific Binding ◽  
Blood Platelets ◽  
Residual Effect ◽  
Independent Effect ◽  
Con A ◽  
Experimental Conditions ◽  
Main Effect ◽  
Induced Aggregation

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.

Factor VIII-Related Activities in Normal, Haemophilic and von Willebrand’s Disease Platelet Fractions

1978 ◽  
Vol 40 (02) ◽  
pp. 288-301 ◽  
Author(s):  
P Meucci ◽  
I R Peake ◽  
A L Bloom
Keyword(s):  
Factor Viii ◽  
Electrophoretic Mobility ◽  
Concanavalin A ◽  
Freezing And Thawing ◽  
Von Willebrand's Disease ◽  
Factor Viii Related Antigen ◽  
Von Willebrand’S Disease ◽  
Normal Plasma ◽  
Significant Difference ◽  
Ristocetin Cofactor

SummaryFactor VIII-related activities have been studied in platelet fractions in order to try to reconcile the conflicting findings of other workers, and to extend the studies. In platelets from 16 normal subjects procoagulant factor VIII was not detected. The amount of factor VIII-related antigen (FVIIIR: AG) in the cytosol per mg of protein was about twice that in the membrane fraction and about ten times that in the debris fraction. There was no significant difference between the amount of FVIIIR: AG and ristocetin cofactor (RistCof) activity in each fraction. The findings in haemophilic platelets were similar. In von Willebrand’s disease (vWd) one serverely affected patient had no detectable factor VIII related activities in any platelet fraction. In 5 patients with intermediate vWd results were normal. In a further 5, with more prolonged bleeding times, no FVIIIR: RistCof was detected in platelets, despite a normal amount of FVIIIR: AG in the cytosol and debris. The electrophoretic mobility of cytosol FVIIIR: AG was increased in all normals and patients, while that in the membrane and debris fractions had normal mobility. Cytosol FVIIIR: AG eluted later than normal FVIIIR: AG on gel filtration on Sepharose 2B, and also showed reduced antibody binding in an immunoradiometric assay. Precipitation of FVIIIR: AG by concanavalin A was incomplete in all platelet fractions from normals, and even more reduced in vWd platelet fractions. The results suggest the possibility of two types of platelet FVIIIR: AG.A factor VIII-related antigen was shown to be associated with normal washed platelets by immunofluorescence techniques (Bloom et al. 1973). Since then, several studies have been reported on the localisation of factor VIII related antigen (FVIIIR: AG), factor VIII procoagulant activity (FVIII: C) and factor VIII related ristocetin cofactor activity (FVIIIR: RistCof) within the platelets. Initially, Howard et al. (1974) indicated that FVIIIR: AG was firmly bound to the platelet membrane, and noted that in lysed platelets the level of FVIIIR: AG as measured by electroimmunodiffusion was higher than that in whole platelet suspensions. However, further studies by Nachman and Jaffe (1975) showed that FVIIIR: AG was also present to a considerable extent in the granules, and they detected none in the platelet cytosol. Bouma and colleagues (1975) were, however, able to find FVIIIR: AG and FVIIIR: RistCof in the cytosol upon freezing and thawing platelets. This FVIIIR: AG had an electrophoretic mobility comparable to that of normal plasma. They also noted that platelets which were air dried apparently had a granular FVIIIR:AG localisation by immunfluorescence; however, intact platelets in suspension did not stain by this method.Recently Ruggeri et al. (1977) and Sultan et al. (1977) have also found FVIIIR: AG in the cytosol, and the former authors reported it to have increased electrophoretic mobility when compared to normal plasma FVIIIR:AG. Results concerning the localisation of FVIIIR: AG in normal platelets have thus been conflicting. Similarly, in the few reports available concerning platelet FVIIIR: AG in von Willibrand’s disease variable results have also been obtained (Ruggeri et al. 1977, Howard et al. 1974, Shearn et al. 1974 and Bouma et al. 1975).In this study we report on the localisation of factor VIII-related activities in normal, haemophilic and von Willebrand’s disease platelets using available standard techniques as well as precipitation of FVIIIR: AG with the plant lectin concanavalin A, a procedure which has been shown to detect abnormal forms of FVIIIR:AG in certain types of von Willebrand’s disease (Peake and Bloom 1977).

Partial Characterization of a Fibrinolytic Inhibitor Produced by Cultured Endothelial Cells Derived from Human Umbilical Vein

1982 ◽  
Vol 47 (02) ◽  
pp. 128-131 ◽  
Author(s):  
F Esnard ◽  
E Dupuy ◽  
A M Dosne ◽  
E Bodevin
Keyword(s):  
Endothelial Cells ◽  
Primary Culture ◽  
Ammonium Sulphate ◽  
Concanavalin A ◽  
Umbilical Vein ◽  
Human Umbilical Vein ◽  
Preliminary Characterization ◽  
Umbilical Vein Endothelial Cells ◽  
Ammonium Sulphate Saturation

SummaryA preliminary characterization of a fibrinolytic inhibitor released by human umbilical vein endothelial cells in primary culture is reported. This molecule of Mr comprised between 2 × 105 and 106 and of μ2 mobility precipitates at 43% ammonium sulphate saturation and is totally adsorbed on Concanavalin A Sepharose 4 B. A possible relationship with a macroglobulins is discussed.

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