Role of surface sialic acid in the interaction of wheat germ agglutinin with human platelets

1979 ◽  
Vol 89 (4) ◽  
pp. 1154-1160 ◽  
Author(s):  
Pankaj Ganguly ◽  
Nancy G. Fossett
Keyword(s):  
Sialic Acid ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Human Platelets

scholarly journals The role of sialic acid in the activation of platelets by wheat germ agglutinin

Blood ◽  
1984 ◽  
Vol 63 (1) ◽  
pp. 181-187
Author(s):  
P Ganguly ◽  
NG Fossett
Keyword(s):  
Sialic Acid ◽  
Dissociation Constant ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Blood Platelets ◽  
Critical Role ◽  
Human Platelets ◽  
Apparent Dissociation Constant ◽  
Serotonin Secretion

Sialic acid is believed to play a critical role in the survival of blood platelets in circulation. Wheat germ agglutinin, which shows specificity for sialic acid, N-acetylglucosamine, and N- acetylgalactosamine, strongly activates platelets. The role of sialic acid in platelet activation by this lectin was studied utilizing neuraminidase-treated platelets and the succinylated lectin that has been reported not to recognize sialic acid. The succinylated lectin had a dimeric structure similar to the native lectin, but migrated more slowly in gel electrophoresis. The modified lectin bound to about 2.8 X 10(5) sites/cell, with an apparent dissociation constant of 2 microM compared to 5 X 10(5) sites/cell and a dissociation constant of 0.4 microM for the native lectin. The succinylated lectin neither aggregated nor agglutinated platelets, but agglutination of red cells in microtiter plates was normal. Aggregation of platelets by either wheat germ agglutinin or ristocetin was not affected by the succinylated lectin. Since the native wheat germ agglutinin is a strong activator of platelets and the succinylated derivative was devoid of all activity, it appears that a sialoprotein acts as the biologic receptor of wheat germ agglutinin in human platelets. This suggestion was strengthened by the observation that platelets treated with different concentrations of neuraminidase had a decreased capacity to bind this lectin. These platelets also showed reduced aggregation and serotonin secretion when activated with the native lectin. Since sialic acid has been implicated in the removal of platelets from circulation, wheat germ agglutinin may prove to be a useful tool to explore those clinical conditions in which platelet survival is shortened.

scholarly journals The role of sialic acid in the activation of platelets by wheat germ agglutinin

Blood ◽  
1984 ◽  
Vol 63 (1) ◽  
pp. 181-187 ◽  
Author(s):  
P Ganguly ◽  
NG Fossett
Keyword(s):  
Sialic Acid ◽  
Dissociation Constant ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Blood Platelets ◽  
Critical Role ◽  
Human Platelets ◽  
Apparent Dissociation Constant ◽  
Serotonin Secretion

Abstract Sialic acid is believed to play a critical role in the survival of blood platelets in circulation. Wheat germ agglutinin, which shows specificity for sialic acid, N-acetylglucosamine, and N- acetylgalactosamine, strongly activates platelets. The role of sialic acid in platelet activation by this lectin was studied utilizing neuraminidase-treated platelets and the succinylated lectin that has been reported not to recognize sialic acid. The succinylated lectin had a dimeric structure similar to the native lectin, but migrated more slowly in gel electrophoresis. The modified lectin bound to about 2.8 X 10(5) sites/cell, with an apparent dissociation constant of 2 microM compared to 5 X 10(5) sites/cell and a dissociation constant of 0.4 microM for the native lectin. The succinylated lectin neither aggregated nor agglutinated platelets, but agglutination of red cells in microtiter plates was normal. Aggregation of platelets by either wheat germ agglutinin or ristocetin was not affected by the succinylated lectin. Since the native wheat germ agglutinin is a strong activator of platelets and the succinylated derivative was devoid of all activity, it appears that a sialoprotein acts as the biologic receptor of wheat germ agglutinin in human platelets. This suggestion was strengthened by the observation that platelets treated with different concentrations of neuraminidase had a decreased capacity to bind this lectin. These platelets also showed reduced aggregation and serotonin secretion when activated with the native lectin. Since sialic acid has been implicated in the removal of platelets from circulation, wheat germ agglutinin may prove to be a useful tool to explore those clinical conditions in which platelet survival is shortened.

scholarly journals The investigation of the changes in the surface glycoconjugates using two different spheroid models of breast cancer cells and availability assessment of these spheroid models for rapid diagnosis

2021 ◽  
Vol 38 (3) ◽  
pp. 266-271
Author(s):  
Yosun MATER ◽  
Günnur DEMİRCAN
Keyword(s):  
Breast Cancer ◽  
Cell Culture ◽  
Sialic Acid ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Sialic Acids ◽  
Maackia Amurensis ◽  
Maackia Amurensis Lectin

The importance of early cancer diagnosis has led to development of many different diagnostic methods. In this context, the studies investigating the presence and amount of sugar residues to use as indicators in the identification of cancer cell type have become prominent. In the present study, sialic acids found on the membrane surfaces of ER (+) MCF-7 and ER (-) MDA-MB-231 breast cancer cell lines were labeled using three-dimensional (3D) cell culture (Spheroid) model as the closest method to the patient sample, thus its natural environment, among the cell culture methods. These sugar units that play a role in regulation of important immune characteristics such as recognition, binding and metastasis were made visualizable by applying fluorescent-labeled lectins such as FITC-(Wheat Germ Agglutinin) specifically binding to sialic acid units (GlcNAc, Neu5Ac) including particularly ß-GlcNAc and FITC-(Maackia Amurensis-Lectin-1) specifically binding to Galß4GlcNAc type sialic acids. These glycan units were specifically labeled with FITC-(Maackia Amurensis-Lectin-1) and FITC- (Wheat Germ Agglutinin) and radiation intensities were analyzed relatively. The two different breast cancer cell cultures were compared with respect to change in the amounts of sialic acid residues containing α-2,3- and α-2,6 bonds using fluorescent-labeled lectins. In the present study, we have performed a precise, accurate and rapid determination of the sugar content in the different breast cancer cell surface lines by means of fluorescent-labeled lectins and carried out a relative comparison between the micrographs.

Role of the nematode surface coat in the adhesion of Clavibacter sp. to Anguina funesta and Anguina tritici

Parasitology ◽  
1991 ◽  
Vol 103 (3) ◽  
pp. 421-427 ◽  
Author(s):  
M. A. McClure ◽  
Y. Spiegel
Keyword(s):  
Bacterial Adhesion ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Complete Removal ◽  
Surface Coat ◽  
Sodium Metaperiodate ◽  
Interspecific Differences ◽  
Bacterial Capsule ◽  
Before And After

Clavibacter sp. (syn. Corynebacterium rathayi) adhered to both Anguina funesta (syn. Anguina agrostis) and Anguina tritici, but differences in the nature of adhesion were noted. Similar patterns of binding of the bacteria and of anti-wheat germ agglutinin antibody initially led us to believe that the mechanism of bacterial adhesion was related to the presence of wheat-germ agglutinin (WGA) on the outer cuticle of both species of nematodes and its complementary carbohydrate on the bacterial capsule. However, treatment of either species of nematode with sodium metaperiodate inhibited bacterial adhesion but not the binding of anti-WGA antibody. Bacterial adhesion, therefore, is not mediated by WGA on the nematodes' surface. Moreover, differences in patterns of bacterial adhesion to Anguina species, both before and after treatments with NaCl and detergents, suggest basic interspecific differences in the nature of adhesion. Electron microscopy confirmed the contribution of the nematodes' cuticular surface coat (SC) to the process of adhesion, but it is still not clear how the SC interacts with the bacterial capsule or which of its components are involved. While complete removal of the SC with periodate prevented bacterial adhesion, juveniles that naturally resisted bacterial adhesion did not lack a SC. One explanation could be that the SC of individuals, to which bacteria do not adhere naturally, lacks crucial components that cannot be defined by conventional EM.

Interaction of wheat germ agglutinin with sialic acid

Biochemistry ◽  
1979 ◽  
Vol 18 (24) ◽  
pp. 5505-5511 ◽  
Author(s):  
Barry P. Peters ◽  
Shigeyuki Ebisu ◽  
Irwin J. Goldstein ◽  
Michael Flashner
Keyword(s):  
Sialic Acid ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ

The role of wheat germ agglutinin in the attachment of Pseudomonas sp. WS32 to wheat root

2014 ◽  
Vol 52 (12) ◽  
pp. 1020-1024 ◽  
Author(s):  
Jian Zhang ◽  
Liyuan Meng ◽  
Yuanyuan Cao ◽  
Huiping Chang ◽  
Zhongyou Ma ◽  
...  
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Wheat Root ◽  
Pseudomonas Sp
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