Hirudin C-terminal fragments inhibit thrombin induced neutrophil chemotaxis

J. K. Rowand, Phillip Marucha, L. J. Berliner

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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-Gln (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.

Original languageEnglish (US)
Pages (from-to)289-291
Number of pages3
JournalThrombosis and Haemostasis
Volume67
Issue number3
StatePublished - 1992
Externally publishedYes

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Hirudins
Chemotaxis
Thrombin
Neutrophils
Peptides
leucyl-phenylalanine
Phenylalanine

ASJC Scopus subject areas

  • Hematology

Cite this

Hirudin C-terminal fragments inhibit thrombin induced neutrophil chemotaxis. / Rowand, J. K.; Marucha, Phillip; Berliner, L. J.

In: Thrombosis and Haemostasis, Vol. 67, No. 3, 1992, p. 289-291.

Research output: Contribution to journalArticle

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