The two neutrophil members of the formylpeptide receptor family activate the NADPH-oxidase through signals that differ in sensitivity to a gelsolin derived phosphoinositide-binding peptide |
| |
Authors: | Fu Huamei Björkman Lena Janmey Paul Karlsson Anna Karlsson Jennie Movitz Charlotta Dahlgren Claes |
| |
Institution: | Department of Rheumatology and Inflammation Research, University of G?teborg, Sweden. Huamei.fu@microbio.gu.se |
| |
Abstract: | Background The formylpeptide receptor family members FPR and FPRL1, expressed in myeloid phagocytes, belong to the G-protein coupled
seven transmembrane receptor family (GPCRs). They share a high degree of sequence similarity, particularly in the cytoplasmic
domains involved in intracellular signaling. The established model of cell activation through GPCRs states that the receptors
isomerize from an inactive to an active state upon ligand binding, and this receptor transformation subsequently activates
the signal transducing G-protein. Accordingly, the activation of human neutrophil FPR and FPRL1 induces identical, pertussis
toxin-sensitive functional responses and a transient increase in intracellular calcium is followed by a secretory response
leading to mobilization of receptors from intracellular stores, as well as a release of reactive oxygen metabolites. |
| |
Keywords: | |
本文献已被 PubMed SpringerLink 等数据库收录! |
|