Abstract
Pepstatin, a chemotactic microbial pentapeptide, competes with f-Met-Leu-[3H]Phe for binding to human neutrophils. Furthermore, porcine neutrophils, which neither specifically bind nor respond chemotactically to the synthetic f-methionyl peptides, also fail to respond chemotactically to pepstatin. These results suggest that pepstatin shares a receptor on the neutrophil with f-methionyl peptides, despite their completely different amino acid compositions. The specificity of this cytotaxin receptor may therefore be broader than expected and depend on ligand characteristics distinct from primary structure.
MeSH Terms
Animals
Binding Sites
Binding, Competitive
Chemotactic Factors/metabolism
Chemotaxis, Leukocyte
Dipeptides/metabolism
Humans
Methionine/analogs & derivatives
N-Formylmethionine/analogs & derivatives,metabolism
Neutrophils/metabolism,physiology
Oligopeptides/metabolism
Pepstatins/metabolism
Swine
Chemicals
Chemotactic Factors
Dipeptides
Oligopeptides
Pepstatins
N-Formylmethionine
Methionine
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Nelson R D
Ackerman S K
Fiegel V D
Bauman M P
Douglas S D
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