Biomaterial Database

Adhesion of human red blood cells and surface charge of the membrane. 1998

E Nishiguchi, and K Okubo, and S Nakamura

Department of Dental Hygiene, Shonan Junior College, Yokosuka, Japan.

To elucidate the mechanism by which red blood cells (RBC) participate in thrombus formation, we investigated the mechanism of adhesion between human RBC. Our study showed that the morphology of RBC was changed by various cationic reagents, inducing adhesion between RBC. When RBC suspended in PBS buffer containing sodium phosphate (PBS(Na)) or potassium phosphate (PBS(K)) were treated with cationic reagents, stronger adhesion occurred between RBC treated with the latter. When concentrations of the reagents were low, adhesion was released and the RBC resumed its original morphology after washing. However, when the concentrations of reagents were high, the morphology did not normalize, although the adhesion was released. When fresh RBC were treated with cationized ferritin (CF), CF bound to the periphery of RBC membranes and induced adhesion. However, when RBC were induced to adhere strongly by a cationic reagent, no binding of CF to the membrane was not observed. When RBC were treated with CF, bindings between substances outside the membranes and bindings between the membranes and substances outside the membranes were observed. When RBC treated with neuraminidase to remove 85-90% of sialic acid were treated with the cationic reagents, both adhesion between RBC and morphological change were reduced. When RBC were pretreated with polyclonal antibody against human RBC membrane band 3 protein, treatment with the cationic reagents did not induce adhesion and morphological change of RBC. Further, when RBC induced to adhere by the cationic reagents were treated with the polyclonal antibody against band 3, in the case of weak adhesion, the adhesion was released and the RBC resumed its original morphology. However, in the case of strong adhesion, the morphology did not return to normal although the adhesion was released. These results suggest that the adhesion between RBC induced by cationic reagents was due to changes in the charge on the membrane surface, involving polysaccharide chains and membrane surface proteins.

UI	MeSH Term	Description	Entries
D008564	Membrane Potentials	The voltage differences across a membrane. For cellular membranes they are computed by subtracting the voltage measured outside the membrane from the voltage measured inside the membrane. They result from differences of inside versus outside concentration of potassium, sodium, chloride, and other ions across cells' or ORGANELLES membranes. For excitable cells, the resting membrane potentials range between -30 and -100 millivolts. Physical, chemical, or electrical stimuli can make a membrane potential more negative (hyperpolarization), or less negative (depolarization).	Resting Potentials,Transmembrane Potentials,Delta Psi,Resting Membrane Potential,Transmembrane Electrical Potential Difference,Transmembrane Potential Difference,Difference, Transmembrane Potential,Differences, Transmembrane Potential,Membrane Potential,Membrane Potential, Resting,Membrane Potentials, Resting,Potential Difference, Transmembrane,Potential Differences, Transmembrane,Potential, Membrane,Potential, Resting,Potential, Transmembrane,Potentials, Membrane,Potentials, Resting,Potentials, Transmembrane,Resting Membrane Potentials,Resting Potential,Transmembrane Potential,Transmembrane Potential Differences
D008854	Microscopy, Electron	Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.	Electron Microscopy
D011134	Polysaccharides	Long chain polymeric CARBOHYDRATES composed of MONOSACCHARIDES linked by glycosidic bonds.	Glycan,Glycans,Polysaccharide
D002021	Buffers	A chemical system that functions to control the levels of specific ions in solution. When the level of hydrogen ion in solution is controlled the system is called a pH buffer.	Buffer
D002448	Cell Adhesion	Adherence of cells to surfaces or to other cells.	Adhesion, Cell,Adhesions, Cell,Cell Adhesions
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
D000906	Antibodies	Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).
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
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining