Summary
Since native hirudin blocks the thrombin induced chemotaxis response of neutrophils,
we examined whether hirudin C-terminal peptides were also capable of this inhibition.
The studies showed that thrombin induced human neutrophil chemotaxis was effectively
blocked by the C-terminal hirudin peptide analogs, Gly-Asp-Phe-Glu-Glu-Ile-Pro-Glu-Glu-Tyr-Leu-Gin
(12-mer[54-65]) and Thr-Pro-Lys-Pro-Gln-Ser-His-Asn-Asp-Gly-Asp-Phe-Glu-Glu-Ile-Pro-Glu-Glu-Tyr-Leu-Gln
(21-mer[45-65]). Furthermore, neither peptide had an effect on formyl-L-methionyl-L-leucyl-L-phenylalanine
induced chemotaxis. The results suggest that binding of the hirudin C-terminal peptides
block the thrombin chemotactic domain.