[The altered membrane of the erythrocyte. I. Ultrahistochemical and biocellular investigations for the detection of activated acetylcholinesterase (ACHE) and demasking of IgG receptor sites (author's transl)].
Different states of the erythrocyte membrane with regard to its disintegration are characterized. The binding power of autologous and allogenic IgG, the degree of the activation of the membrane associated acetylcholinesterase (inhibited in the intact plasmalemma of red blood cells), and the membrane vesiculation served as criteria. The findings demonstrate that, obviously, the IgG binding increases in dependence on the extent of the disturbance of the membrane structure. The acetylcholinesterase is increasingly activated. The enzyme can be demonstrated by spectrophotometrical and ultrahistochemical methods. Microvesiculation is understood as expression of fundamental disturbances of the membrane structure. These disturbances express local remodelling processes in the membrane of banked red blood cells. Highly extended damage of red blood cells after mechanical stress, heat or urea incubation lead to comparatively high rates of vesiculation, partially even to cell fragmentation. Extremely spectrindeficient ghosts tend to microvesiculation, which leads to complete microvesicular decay of the ghost membrane. The membrane associated autologous IgG is demonstrated by means of immuneological and ultrahistochemical methods. Its importance as homeostatically effective immun-signal for the elimination of red blood cells aged in vivo or in vitro, ghosts and microvesicles by the reticulohistiocytic-system is evidenced by means of model experiments. Molecular mechanisms for unmasking of IgG-receptor sites and activation of acetylcholineesterase in the altered erythrocyte membrane are discussed.
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D004905:Erythrocyte Aging; D004910:Erythrocyte Membrane / Q000201:enzymology* / Q000276:immunology / Q000648:ultrastructure; D004912:Erythrocytes / Q000201:enzymology*; D005613:Freeze Etching; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism; D008855:Microscopy, Electron, Scanning; D051381:Rats; D011971:Receptors, Immunologic / Q000378:metabolism*; D013053:Spectrophotometry
D007074:Immunoglobulin G; D011971:Receptors, Immunologic; D000110:Acetylcholinesterase
Die alterierte Erythrocytenmembran. I. Ultrahistochemische und zellbiologische Untersuchungen zur Aktivierung der Acetylcholinesterase (ACHE) und Demaskierung von IgG-Receptoren.