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1.
Article in English | MEDLINE | ID: mdl-6159284

ABSTRACT

The study on procainized human erythrocytes revealed a) temperature dependent changes of cellshapes, b) a significant increase of deformability, c) low amounts of cross-linked membrane proteins, d) a mean cell volume identical with the volume of nonprocainized cells, e) severe reduction of induced anisotropy, f) no loss of negatively charged groups of the glycocalyx, g) decrease of electrophoretic velocity, h) a significant rise of adhesiveness to glass, and i) increase of agglutinability with antiserum and lectin. The findings are discussed in their relationships to alterations of the molecular structure of the red cell membrane.


Subject(s)
Erythrocyte Membrane/drug effects , Erythrocytes/drug effects , Membrane Fluidity/drug effects , Membrane Proteins/metabolism , Procaine/pharmacology , Spectrin/metabolism , Adhesiveness , Erythrocyte Membrane/physiology , Erythrocyte Volume/drug effects , Erythrocytes/cytology , Hemagglutination/drug effects , Humans
2.
Exp Pathol (Jena) ; 17(3): 171-5, 1979.
Article in English | MEDLINE | ID: mdl-225191

ABSTRACT

The present study is concerned with the interaction of rat endo- and mesothelium with homologous erythrocytes under various conditions of pretreatment and incubation. Its findings show rat endo- and mesothelial cells a) nonadhesive to native or pretreated erythrocytes irrespective of the presence of gamma-globulin in the medium, b) devoid of primary or cryptic receptors sensitive to the Fc segment of the IgG molecule, and c) provided with binding sites at the oxidized glycocalyx which together with receptor groups of modified erythrocytes share the same class of IgG.


Subject(s)
Endothelium/metabolism , Erythrocytes/physiology , Immunoglobulin Fc Fragments/metabolism , Agglutination , Animals , Binding Sites , Cell Adhesion , Erythrocyte Membrane/physiology , Female , In Vitro Techniques , Male , Periodic Acid/pharmacology , Rats , Trypsin/pharmacology
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