The capacity of basic peptides to trigger exocytosis from mast cells correlates with their capacity to immobilize band 3 proteins in erythrocyte membranes.
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.
D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism*; D005089:Exocytosis / Q000187:drug effects*; D006801:Humans; D066298:In Vitro Techniques; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D008407:Mast Cells / Q000187:drug effects / Q000378:metabolism*; D009904:Optical Rotation; D010455:Peptides / Q000494:pharmacology*; D051381:Rats; D012701:Serotonin / Q000378:metabolism; D013329:Structure-Activity Relationship
D001457:Anion Exchange Protein 1, Erythrocyte; D010455:Peptides; D012701:Serotonin; D007770:L-Lactate Dehydrogenase