Abstract
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.
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Abita, J.P. (1980). On the mechanism of human polymorphonuclear leukocyte deactivation of chemotaxis by the synthetic peptide formyl-methiony-leucyl-phenylalanine. In: Willoughby, D.A., Giroud, J.P. (eds) Inflammation: Mechanisms and Treatment. Inflammation: Mechanisms and Treatment, vol 4. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-9423-8_61
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DOI: https://doi.org/10.1007/978-94-010-9423-8_61
Publisher Name: Springer, Dordrecht
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