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. 1984 Oct 1;223(1):67–71. doi: 10.1042/bj2230067

The capacity of basic peptides to trigger exocytosis from mast cells correlates with their capacity to immobilize band 3 proteins in erythrocyte membranes.

M J Dufton, R J Cherry, J W Coleman, D R Stanworth
PMCID: PMC1144265  PMID: 6497847

Abstract

The effect of mast-cell-triggering peptides on the rotational properties of band 3, a protein component of the human erythrocyte membrane, was measured by observing flash-induced transient dichroism of the triplet probe eosin maleimide. In the presence of melittin, polylysine and five synthetic peptides, varying degrees of retardation in the rotational motion of band 3 were produced. When placed in order of band 3 immobilizing activity, the peptides formed a series identical with their order of efficacy in releasing 5-hydroxytryptamine from rat peritoneal mast cells. The correspondence in the abilities to immobilize band 3 in the erythrocyte and trigger mast cells is significant because structure-activity analyses of the peptides show both processes to have the same cationic, hydrophobic and stereochemical requirements. Probably, the immobilization of band 3 proteins reflects an ability of the basic peptides to aggregate anionic surface moieties, and therefore a similar mechanism is implied in mast-cell triggering.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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