A Cell Permeant Peptide Containing the Cytoplasmic Tail Sequence of Fc Receptor Type IIA Reduces Calcium Signaling and Phagolysosome Formation in Neutrophils
Overview
Cell Biology
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Receptors for the Fc domain of IgG mediate target recognition, signal transduction, and effector functions including antibody-dependent cytolysis, phagocytosis, and phagolysosome formation. To better understand FcR-mediated functions and to identify potential therapeutic strategies, we employed cell-penetrating ("Trojan") peptides to deliver "wild-type" (LTL) or modified (AAA) FcgammaRIIA tail sequences to the neutrophil's cytoplasm. The Trojan-LTL peptide appeared to label the endoplasmic reticulum whereas the Trojan-AAA peptide distributed throughout the cytoplasm. The Trojan-LTL peptide, but not the Trojan-AAA peptide, decreased Ca(2+) signaling at the phagosome and reduced phagolysosome formation. These studies suggest that FcgammaRIIA's tail can act as a peptide decoy thereby blunting FcgammaRIIA-mediated processes, which, in turn, suggests a possible route in managing inflammatory tissue damage.
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