On the mechanism of human polymorphonuclear leukocyte deactivation of chemotaxis by the synthetic peptide formyl-methiony-leucyl-phenylalanine
Polymorphonuclear leukocytes respond chemotactically in vitro to a variety of compounds including denatured proteins1 factors derived from complement2, bacterial products3 and synthetic peptides, the most potent being the peptide formyl-methionyl-leucyl-phenylalanine (f-Met-Leu-Phe)4,5. In addition f-Met-Leu-Phe induces granule enzyme secretion and superoxide production when added with cytochalasin B to rabbit neutrophils in suspension4,6 and aggregates these cells7. There is evidence that all these functions result from the interaction of the peptide with a common membrane receptor4,6–8 which has been demonstrated, by direct binding studies, to exist on the cell surface of rabbit9 and human neutrophils10.
KeywordsHuman Neutrophil Cellulose Nitrate Calcium Ionophore A23187 Chemotactic Peptide Lower Filter
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