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 erythr...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1983-12, Vol.80 (24), p.7542-7546
Main Authors: Kosower, Nechama S., Glaser, Tova, Kosower, Edward M.
Format: Article
Language:English
Subjects:
Animals
Calcium
Calcium - pharmacology
Cell fusion
Cell Fusion - drug effects
Cell membranes
Cells
Chemical suspensions
Erythrocyte membrane
Erythrocyte Membrane - drug effects
Erythrocyte Membrane - physiology
Erythrocytes
Erythrocytes - physiology
Female
Gels
Humans
man
Membrane Fluidity
membrane fusion
Membrane proteins
Membrane Proteins - blood
Membrane Proteins - isolation & purification
Molecular Weight
P branes
Peptide Hydrolases - metabolism
Rats
Species Specificity
Stearates - pharmacology
Stearic Acids - pharmacology
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.80.24.7542