The analysis of lymphocyte surface receptors recognized by wheat germ agglutinin for negative regulation of immune responses in cancer patients

1990 ◽  
Vol 20 (1) ◽  
pp. 51-55 ◽  
Author(s):  
Yoshiyuki Yamaguchi ◽  
Tetsuya Toge ◽  
Nobutoshi Baba ◽  
Hiroshi Kuninobu ◽  
Yasuhide Kegoya ◽  
...  
Keyword(s):  
Immune Responses ◽  
Cancer Patients ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Negative Regulation ◽  
Surface Receptors ◽  
Lymphocyte Surface

Cell surface receptors for wheat germ agglutinin and limulin in baby hamster kidney cells and ricin resistant variants

Biochimie ◽  
1981 ◽  
Vol 63 (3) ◽  
pp. 169-175 ◽  
Author(s):  
Angèle Obrenovitch ◽  
Claude Sene ◽  
Annie Claude Roche ◽  
Michel Monsigny ◽  
Peter Visher ◽  
...  
Keyword(s):  
Cell Surface ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Cell Surface Receptors ◽  
Kidney Cells ◽  
Baby Hamster Kidney ◽  
Surface Receptors ◽  
Baby Hamster Kidney Cells

Further Characterization of Wheat Germ Agglutinin Interaction with Human Platelets: Exposure of Fibrinogen Receptors

1986 ◽  
Vol 56 (03) ◽  
pp. 323-327
Author(s):  
Marilyne Lebret ◽  
Francine Rendu
Keyword(s):  
Platelet Activation ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Lectin Binding ◽  
Human Platelets ◽  
Cyclooxygenase Inhibitors ◽  
Platelet Surface ◽  
Surface Receptors ◽  
Fibrinogen Binding ◽  
Exogenous Calcium

SummaryIt was previously shown that (i) Wheat germ agglutinin, (WGA)-induced platelet activation occurred when only 17% of the lectin binding sites were occupied on the platelet surface and (ii) WGA caused the release of a platelet constituent which in turn participates in the observed effect. We now further define the platelet activation induced by WGA: the lectin induces a binding of fibrinogen to specific surface receptors. 125I-fibrinogen binding increases with the WGA concentration from 5 to 15 ug/ ml. Binding occurs without addition of exogenous calcium; its analysis demonstrated 54000 sites with a Ka = 0.8 × 106 M-1, Addition of 1 mM Ca2+ enhances the 125I-fibrinogen binding and reveals a second class of sites with higher affinity (9200 sites, Ka = 0.17 x 108 M-1). This 125I-fibrinogen binding is totally abolished by EDTA, ATP and arginine, and inhibited by 75% by CP/CPK; cyclooxygenase inhibitors and PGE1 also reduce the fibrinogen binding. Thus the WGA-induced fibrinogen binding is (1) release-dependent and (2) responsible for the aggregation process but not for the agglutinating effect of the lectin.

Failure of 6D1 or Exposure of Platelets to ADP to Affect Agglutination Induced by Wheat Germ Agglutinin

1989 ◽  
Vol 62 (02) ◽  
pp. 815 ◽  
Author(s):  
Marjorie B Zucker ◽  
Robert A Grant ◽  
Evelyn A Mauss
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ

Transport Characteristics of Wheat Germ Agglutinin-Modified Insulin-Liposomes and Solid Lipid Nanoparticles in a Perfused Rat Intestinal Model

2006 ◽  
Vol 6 (9) ◽  
pp. 2959-2966 ◽  
Author(s):  
Na Zhang ◽  
Qineng Ping ◽  
Guihua Huang ◽  
Xiuzhen Han ◽  
Yanna Cheng ◽  
...  
Keyword(s):  
Solid Lipid Nanoparticles ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Serum Insulin ◽  
Lipid Nanoparticles ◽  
Solid Lipid ◽  
Mucosal Absorption ◽  
Perfusion Experiment ◽  
Absorption Sites

Wheat germ agglutinin (WGA) modified liposomes and solid lipid nanoparticles (SLNs) were evaluated for improving intestinal absorption of insulin. In an in situ local intestinal perfusion experiment, formulations containing 100 IU/kg insulin were administered to the duodenum, jejunum, and ileum of fasted rats. As hypothesized, ileum was the best intestinal location for the absorption of insulin-containing liposomes. Serum insulin concentrations decreased for the various formulations in different absorption sites according to the following trends: Duodenum > ileum > jejunum for WGA-modified insulin-containing liposomes; duodenum > jejunum > ileum for WGA-modified insulin-containing SLNs; ileum > jejunum > duodenum for insulin-containing liposomes; ileum > duodenum > jejunum for insulin-containing SLNs; and duodenum ≥ ileum > jejunum for aqueous solution of insulin. These results imply that the nanoparticle type and delivery site were important factors with respect to increasing the bioavailability of insulin following oral administration. The proteolytic degradation as well as the epithelial permeability were primary determinants influcing insulin mucosal absorption.

Identification of distinct haemocyte populations from the freshwater bivalves swan mussel (Anodonta cygnea) and duck mussel (Anodonta anatina) using wheat-germ agglutinin

2017 ◽  
Vol 95 (12) ◽  
pp. 937-947 ◽  
Author(s):  
M. Hinzmann ◽  
M. Lopes-Lima ◽  
F. Cerca ◽  
A. Correia ◽  
J. Machado ◽  
...  
Keyword(s):  
Flow Cytometry ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Transmission Microscopy ◽  
Anodonta Cygnea ◽  
Functional Studies ◽  
Lectin Staining ◽  
Surface Staining ◽  
Cytological Features ◽  
Freshwater Bivalves

Haemocytes play a major role in molluscs immunity. Functional studies are, however, impaired by limited available experimental tools to identify and sort distinct haemocyte populations. Therefore, using nonlethal methods, we aimed at evaluating whether lectin staining combined with flow cytometry could be used to distinguish circulating haemocyte populations from two freshwater bivalves of the family Unionidae, the duck mussel (Anodonta anatina (L., 1758)) and the swan mussel (Anodonta cygnea (L., 1758)). Based on classical classification, haemocytes were distinguished as granulocytes and hyalinocytes and cytological features were visualized using transmission microscopy and staining techniques. Size, granularity, viability, and surface staining using lectins as specific probes were analysed by flow cytometry and fluorescence microscopy. The microscopic proportions of granulocytes and hyalinocytes significantly differed, being of 70% and 30% for A. cygnea and of 85% and 15% for A. anatina, respectively. Two haemocyte populations were sorted by flow cytometry based on size and granularity and confirmed as granulocytes and hyalinocytes. Interestingly, two different granulocyte populations could be further discriminated in A. cygnea according to their binding affinity to wheat-germ agglutinin (WGA), whereas granulocytes of A. anatina all stained similarly. Our results show that WGA labelling combined with flow cytometry can be used to better discriminate Anodonta haemocyte populations and obtain purified populations for functional studies.

Protein phosphorylation and activation of platelets by wheat germ agglutinin

1985 ◽  
Vol 132 (1) ◽  
pp. 313-319 ◽  
Author(s):  
Chhanda L. Ganguly ◽  
Mohanathasan Chelladurai ◽  
Pankaj Ganguly
Keyword(s):  
Protein Phosphorylation ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ
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