Biomaterial Database

[The effect of wheat germ agglutinin on anion transport in the erythrocyte membranes]. 1994

H Xu, and Y Xu, and Z H Zhang

Department of Physiology and Biophysics, Fudan University, Shanghai.

The wheat germ agglutinin (WGA) has been recognized as the lectin that can agglutinate human erythrocytes. It is reported recently that the binding of WGA to the glycophorin blocks the morphological conversions of discocyte<-->echinocyte. Glycophorin is thought to be associated with Band 3, the anion transport protein, via the cytoskeleton proteins Band 4.1, spectrin and ankyrin. The effect of WGA on the anion transport across the erythrocyte membranes was measured by NO2- transport and NH4 Cl isotonic swelling, two different methods developed by our laboratory in recent years. The results showed that the rate of anion transport was decreased, depending on WGA concentration. This effect became saturated when WGA concentration reached 2-3 micrograms/ml. We have also observed that in certain conditions when the morphological conversion of discocyte-->elliptocyte was induced by high concentration of WGA, the rate of anion transport could be reversely increased. Furthermore, the effect of WGA on erythrocyte osmotic fragility was studied. The results indicated that the osmotic fragility was reduced after adding WGA to the erythrocyte suspension, which means the erythrocyte cytoskeleton is more stable under this condition. All effects that WGA exerted above were instantly abolished by adding N-acetylglucosamine which has specific binding sites on WGA. In conclusion, the binding of WGA to the sialic acid groups of glycophorin can lead to the conformational changes in saccharides and such changes will be transferred via glycophorin, cytoskeleton to Band 3, which causes the final change of anion transport. The effect is indirect, so the change is small (approximately 10%).(ABSTRACT TRUNCATED AT 250 WORDS)

UI	MeSH Term	Description	Entries
D009996	Osmotic Fragility	RED BLOOD CELL sensitivity to change in OSMOTIC PRESSURE. When exposed to a hypotonic concentration of sodium in a solution, red cells take in more water, swell until the capacity of the cell membrane is exceeded, and burst.	Saline Fragility,Fragility, Osmotic,Fragility, Saline
D004305	Dose-Response Relationship, Drug	The relationship between the dose of an administered drug and the response of the organism to the drug.	Dose Response Relationship, Drug,Dose-Response Relationships, Drug,Drug Dose-Response Relationship,Drug Dose-Response Relationships,Relationship, Drug Dose-Response,Relationships, Drug Dose-Response
D004910	Erythrocyte Membrane	The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS.	Erythrocyte Ghost,Red Cell Cytoskeleton,Red Cell Ghost,Erythrocyte Cytoskeleton,Cytoskeleton, Erythrocyte,Cytoskeleton, Red Cell,Erythrocyte Cytoskeletons,Erythrocyte Ghosts,Erythrocyte Membranes,Ghost, Erythrocyte,Ghost, Red Cell,Membrane, Erythrocyte,Red Cell Cytoskeletons,Red Cell Ghosts
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000117	Acetylglucosamine	The N-acetyl derivative of glucosamine.	Acetyl Glucosamine,N-Acetyl Glucosamine,N-Acetyl-beta-D-Glucosamine,N-Acetylglucosamine,beta-N-Acetylglucosamine,2-Acetamido-2-Deoxy-D-Glucose,2-Acetamido-2-Deoxyglucose,N-Acetyl-D-Glucosamine,2 Acetamido 2 Deoxy D Glucose,2 Acetamido 2 Deoxyglucose,Glucosamine, Acetyl,Glucosamine, N-Acetyl,N Acetyl D Glucosamine,N Acetyl Glucosamine,N Acetyl beta D Glucosamine,N Acetylglucosamine,beta N Acetylglucosamine
D001457	Anion Exchange Protein 1, Erythrocyte	A major integral transmembrane protein of the ERYTHROCYTE MEMBRANE. It is the anion exchanger responsible for electroneutral transporting in CHLORIDE IONS in exchange of BICARBONATE IONS allowing CO2 uptake and transport from tissues to lungs by the red blood cells. Genetic mutations that result in a loss of the protein function have been associated with type 4 HEREDITARY SPHEROCYTOSIS.	Anion Transport Protein, Erythrocyte,Band 3 Protein,Erythrocyte Anion Transport Protein,Erythrocyte Membrane Band 3 Protein,AE1 Anion Exchanger,AE1 Chloride-Bicarbonate Exchanger,AE1 Cl- HCO3- Exchanger,AE1 Gene Product,Anion Exchanger 1,Antigens, CD233,Band 3 Anion Transport Protein,Band III Protein,CD233 Antigen,CD233 Antigens,Capnophorin,EPB3 Protein,Erythrocyte Anion Exchanger,Erythrocyte Membrane Anion Transport Protein,Erythrocyte Membrane Protein Band 3, Diego Blood Group,Protein Band 3,SLC4A1 Protein,Solute Carrier Family 4 Member 1,Solute Carrier Family 4, Anion Exchanger, Member 1,AE1 Chloride Bicarbonate Exchanger,AE1 Cl HCO3 Exchanger,Anion Exchanger, Erythrocyte,Antigen, CD233,Chloride-Bicarbonate Exchanger, AE1,Exchanger 1, Anion,Protein, EPB3
D014909	Wheat Germ Agglutinins	Lectins purified from the germinating seeds of common wheat (Triticum vulgare); these bind to certain carbohydrate moieties on cell surface glycoproteins and are used to identify certain cell populations and inhibit or promote some immunological or physiological activities. There are at least two isoforms of this lectin.	Agglutinins, Wheat Germ,Lectins, Triticum Vulgare,Lectins, Wheat Germ,Triticum Vulgare Lectin,Triticum Vulgare Lectins,Wheat Germ Agglutinin,Wheat Germ Lectin,Wheat Germ Lectins,Wheat Germ Agglutinin Isolectin 1,Wheat Germ Agglutinin Isolectin 2,Agglutinin, Wheat Germ,Germ Agglutinin, Wheat,Germ Lectin, Wheat,Lectin, Triticum Vulgare,Lectin, Wheat Germ,Vulgare Lectin, Triticum
D017136	Ion Transport	The movement of ions across energy-transducing cell membranes. Transport can be active, passive or facilitated. Ions may travel by themselves (uniport), or as a group of two or more ions in the same (symport) or opposite (antiport) directions.	Antiport,Ion Cotransport,Ion Exchange, Intracellular,Symport,Uniport,Active Ion Transport,Facilitated Ion Transport,Passive Ion Transport,Cotransport, Ion,Exchange, Intracellular Ion,Intracellular Ion Exchange,Ion Transport, Active,Ion Transport, Facilitated,Ion Transport, Passive,Transport, Active Ion,Transport, Ion