The subcellular localization of the receptor for platelet-activating factor in neutrophils affects signaling and activation characteristics.

ABSTRACT: The localization in neutrophils, of the receptor for platelet-activating factor (PAFR), has been determined using subcellular fractionation and a receptor mobilization protocol. We show that the PAFR is expressed primarily in the plasma membrane. Although activation of neutrophils by PAF induces responses typical also of agonists that bind the formyl peptide receptors (FPR), known to be stored in mobilizable organelles, some quantitative as well as qualitative differences were observed when neutrophils were activated through these receptors. PAF is equipotent to fMLF (high affinity agonist for FPR1) to cleave off L-selectin and to induce granule/vesicle secretion but is more potent than fMLF to induce a rise in intracellular Ca(2+). Similar to fMLF, PAF induced also a robust release of rea

SUBMITTER: Andreasson E 

PROVIDER: S-EPMC3773398 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature