The role of lymphocyte surface binding sites for wheat germ agglutinin in the negative regulation of cancer patients

Surgery Today ◽  
1993 ◽  
Vol 23 (9) ◽  
pp. 765-770 ◽  
Author(s):  
Tetsuya Toge ◽  
Yoshiyuki Yamaguchi ◽  
Akihiro Sawamura
Keyword(s):  
Cancer Patients ◽  
Binding Sites ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Negative Regulation ◽  
Surface Binding ◽  
Lymphocyte Surface

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

scholarly journals Wheat-germ-agglutinin and Ricinus communis-agglutinin-binding sites of BHK cells compared with each other and with 140 kDa fibronectin receptors

1988 ◽  
Vol 251 (1) ◽  
pp. 269-277 ◽  
Author(s):  
T L Tuan ◽  
F Grinnell
Keyword(s):  
Cell Surface ◽  
Binding Sites ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Ricinus Communis ◽  
Chinese Hamster ◽  
Surface Binding ◽  
Bhk Cells ◽  
Receptor Complexes ◽  
Ricinus Communis Agglutinin

We compared the wheat-germ agglutinin (WGA) and Ricinus communis agglutinin (RCA) binding sites of baby-hamster kidney (BHK) cells. There were 1.01 × 10(8) WGA-binding sites per cell (Kd = 0.027 nM) and 6 × 10(6) RCA-binding sites per cell (Kd = 0.014 nM). Binding of WGA or RCA to BHK cells resulted in more than 75% of the cell-surface binding sites becoming associated with the cytoskeleton (i.e. resistant to extraction with detergent), although no more than 10% of these sites were associated with the cytoskeleton before addition of the lectins. After binding of WGA to the cells, the cell surface was cross-linked so extensively that it remained intact even after detergent extraction of the treated cells, and could be observed by electron microscopy. A similar cross-linking effect did not occur after binding of RCA to cells, which may be because there were so many more binding sites for WGA than for RCA. The composition of WGA- and RCA-binding molecules was analysed by lectin affinity chromatography of metabolically radiolabelled BHK cells. We found that in the WGA-binding-molecule preparations there were eight major polypeptides, ranging in molecular mass from 93 to 340 kDa, and that the RCA-binding molecules were a subpopulation of the WGA-binding molecules. A polyclonal antibody against the 140 kDa fibronectin (FN) receptors of Chinese-hamster ovary (CHO) cells immunoblotted a 145 kDa polypeptide component in both WGA- and RCA-binding-molecule preparations. The results indicated that the 145 kDa component was present in at least two FN-receptor complexes that differed in glycosylation, only one of which was able to bind to RCA affinity columns. The oligomeric nature of the FN-receptor complex, which contained three polypeptides with molecular masses of 120-145 kDa, was demonstrated by using anti-(CHO-cell FN receptor) antibodies to immunoprecipitate extracts prepared from radioiodinated BHK cells.

scholarly journals Compartmentalization of intracellular membrane glycocomponents is revealed by fracture-label.

1984 ◽  
Vol 98 (1) ◽  
pp. 29-34 ◽  
Author(s):  
M R Torrisi ◽  
P Pinto da Silva
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Binding Sites ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Secretory Granules ◽  
The Other ◽  
Rat Tissues ◽  
Intracellular Membrane ◽  
Definition Of

We used thin-section fracture-label to determine the distribution of wheat-germ agglutinin binding sites in intracellular membranes of secretory and nonsecretory rat tissues as well as in human leukocytes. In all cases, analysis of the distribution of wheat germ agglutinin led to the definition of two endomembrane compartments: one, characterized by absence of the label, includes the membranes of mitochondria and peroxisomes as well as those of the endoplasmic reticulum and nuclear envelope; the other, strongly labeled, comprises the membrane of lysosomes, phagocytic vacuoles, and secretory granules, as well as the plasma membrane. The Golgi apparatus was weakly labeled in all studied tissues.

Wheat germ agglutinin binding sites in the organ of Corti as revealed by lectin-gold labeling

1987 ◽  
Vol 27 (3) ◽  
pp. 239-244 ◽  
Author(s):  
Masayoshi Tachibana ◽  
Hiroyuki Morioka ◽  
Mitsuo Machino ◽  
Masaki Yoshimatsu ◽  
Osamu Mizukoshi
Keyword(s):  
Binding Sites ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Organ Of Corti

scholarly journals Expression of 5′Nucleotidase Activity and Wheat-Germ Agglutinin Binding Sites in Mononuclear Phagocytes From Bone Marrow Cultures

1985 ◽  
Vol 37 (3) ◽  
pp. 263-277 ◽  
Author(s):  
R. de Water ◽  
J.W.M. van der Meer ◽  
J.M. van't Noordende ◽  
J.J.M. Onderwater ◽  
J.S. van de Gevel ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Binding Sites ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Mononuclear Phagocytes ◽  
Nucleotidase Activity ◽  
Bone Marrow Cultures ◽  
Marrow Cultures
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