Isolation and characterization of a wheat germ agglutinin-binding glycoprotein from B16 mouse melanoma cells

1986 ◽  
Vol 151 ◽  
pp. 51-64
Author(s):  
Purnima D. Pinnaduwage ◽  
V.P. Bhavanandan ◽  
Eugene A. Davidson
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Melanoma Cells ◽  
Mouse Melanoma ◽  
Isolation And Characterization ◽  
B16 Mouse Melanoma ◽  
Binding Glycoprotein

Isolation and characterization of glycoconjugates from B16 mouse melanoma tumors

1978 ◽  
Vol 65 (1) ◽  
pp. 73-83 ◽  
Author(s):  
V. Sheik Fareed ◽  
V.P. Bhavanandan ◽  
E.A. Davidson
Keyword(s):  
Mouse Melanoma ◽  
Isolation And Characterization ◽  
B16 Mouse Melanoma

Isolation and characterization of the potential receptor for wheat germ agglutinin from human neutrophils

2006 ◽  
Vol 23 (7-8) ◽  
pp. 591-598 ◽  
Author(s):  
Carlos Solórzano ◽  
Stéphane Bouquelet ◽  
M. Ali Pereyra ◽  
Francisco Blanco-Favela ◽  
Marie-Christine Slomianny ◽  
...  
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Human Neutrophils ◽  
Isolation And Characterization

scholarly journals Enzymatic basis for a lectin-resistant phenotype: increase in a fucosyltransferase in mouse melanoma cells.

1982 ◽  
Vol 92 (2) ◽  
pp. 277-282 ◽  
Author(s):  
J Finne ◽  
M M Burger ◽  
J P Prieels
Keyword(s):  
Sialic Acid ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Regulatory Gene ◽  
Fold Increase ◽  
Melanoma Cells ◽  
Sialic Acid Content ◽  
Biochemical Basis ◽  
Mouse Melanoma ◽  
Increased Sensitivity

In the search for the biochemical basis of the control of glycosylation of cell surface carbohydrates, revertant clones were isolated from previously characterized wheat germ agglutinin-resistant clones of B16 mouse melanoma cells by selection for resistance to Lotus tetragonolobus lectin or to ricin. Comparison of the wheat germ agglutinin-resistant clones with the parent and revertant clones indicated that this phenotype was correlated with an increased sensitivity to the Lotus lectin, a 60- to 70-fold increase in alpha 1 leads to 3 fucosyltransferase activity and a decreased sialic acid content of the N-glycosidic chains of glycoproteins. The results suggest a novel type of control mechanism for lectin resistance, an increase in a glycosyltransferase activity. The presence of alpha 1 leads to 3 bound fucose on N-acetylglucosamine residues would interfere with the addition of sialic acid by alpha 2 leads to 3 linkages to galactose residues in the carbohydrate units, and this change could explain the resistance to wheat germ agglutinin and the increased sensitivity to the Lotus lectin. A change in a regulatory gene for the fucosyltransferase as a possible primary cause for the changed phenotype is discussed.

Isolation and characterization of rat skeletal myoblast mutants resistant to lectins

1983 ◽  
Vol 3 (12) ◽  
pp. 2166-2171
Author(s):  
B Gilfix ◽  
J Rogers ◽  
B D Sanwal
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Wild Type ◽  
Skeletal Myoblast ◽  
Skeletal Myoblasts ◽  
Isolation And Characterization ◽  
Low Concentrations ◽  
High Concentrations ◽  
Made In

Mutants resistant to the lethal action of the lectins phytohemagglutinin A (PHA) and wheat germ agglutinin (WGA) have been made in a line of differentiating rat skeletal myoblasts. The WGA mutants are of two types, WGArII, resistant to low concentrations of the lectin, and WGArI, resistant to high concentrations of the lectin. WGArII and PHAr mutants are unable to differentiate, whereas WGArI mutants differentiate normally. WGArII mutants are not impaired in the binding of wheat germ agglutinin, but WGArI mutants bind the lectin only to the extent of about 50% of the wild-type values. All of the mutants are cross-resistant to lectins other than those used in their selection.

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