The collagen-breakdown product N-acetyl-Proline-Glycine-Proline (N-alpha-PGP) does not interact directly with human CXCR1 and CXCR2

P. De Kruijf, H.D. Lim, S.A. Overbeek, G.J.R. Zaman, A.D. Kraneveld, G. Folkerts, R. Leurs, M.J. Smit

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Neutrophils transmigrate from the blood into inflamed tissue via the interaction of chemokines produced in this tissue with chemokine receptors, such as CXCR1 and CXCR2, that are expressed on the membranes of neutrophils. Subsequently, activation of neutrophils will in turn lead to increased tissue damage and thereby enhanced clinical symptoms of inflammatory diseases like chronic obstructive pulmonary disease, inflammatory bowel disease and psoriasis. Besides chemokines, also the collagen-breakdown product N-acetyl-Proline-Glycine-Proline (N-α-PGP) attracts neutrophils. In a recent article (Weathington et al., 2006) it was suggested that N-α-PGP exerts its effect via CXCR1 and CXCR2. In this study, we show that N-α-PGP, in contrast to CXCL8, does not directly activate or interact with CXCR1 or CXCR2. N-α-PGP was not able to displace the radioligand [
Original languageEnglish
Pages (from-to)29-33
JournalEuropean Journal of Pharmacology
Volume643
Issue number1
DOIs
Publication statusPublished - 2010

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