Membrane-mobility agent-promoted fusion of erythrocytes: fusibility is correlated with attack by calcium-activated cytoplasmic proteases on membrane proteins.
Rat, but not human, erythrocytes undergo fusion promoted by the membrane-mobility agent 2-(2-methoxyethoxy)-ethyl cis-8-(2-octylcyclopropyl)octanoate (A2C). The difference in behavior is correlated with rat erythrocyte membrane protein degradation caused by Ca2+-activated proteases. The human erythrocyte is deficient in such protease activity. Membrane protein degradation is a necessary, but not sufficient, requirement for membrane fusion. Membrane protein degradation probably releases membrane components from certain constraints. In addition, the motion of membrane components precedes fusion and must be promoted by reagents such as A2C, leading to the creation of fusion-potent lipid areas. This sequence of chemical and physical events occurs in other fusion processes.
D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D002459:Cell Fusion / Q000187:drug effects; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000502:physiology*; D004912:Erythrocytes / Q000502:physiology; D005260:Female; D006801:Humans; D008560:Membrane Fluidity; D008565:Membrane Proteins / Q000097:blood* / Q000302:isolation & purification; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism; D051381:Rats; D013045:Species Specificity; D013228:Stearates / Q000494:pharmacology*; D013229:Stearic Acids / Q000494:pharmacology*
D008565:Membrane Proteins; D013228:Stearates; D013229:Stearic Acids; C023714:A(2)C; D010447:Peptide Hydrolases; D002118:Calcium