Chloride transport in functionally active phagosomes isolated from Human neutrophils

Article ID	Journal	Published Year	Pages	File Type
10737920	Free Radical Biology and Medicine	2012	10 Pages	PDF

Abstract

âº We isolated functionally active phagosomes from human neutrophils. âº V-ATPase functions independent of NADPH oxidase in the phagosomes. âº Chloride transport facilitates V-ATPase-mediated proton translocation to the phagosomal lumen. âº CFTR and other chloride channels largely account for chloride influx to the phagosomes. âº Active NADPH oxidase and MPO suppress phagosomal pH change due to proton consumption for oxidant production.

Keywords

DFP diisopropylfluorophosphate CFTR Nppb pKa DHR phagosomes V-ATPase Chloride transporter CFTRinh-172 ClC-3 Ap5A Sp-cAMPS HEPES 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid 4-aminobenzoic acid hydrazide 5-nitro-2-(3-phenylpropylamino)benzoic acid MPO Rp-cAMPS Acridine orange ABAH hypochlorous acid dihydrorhodamine 123 Free radicals cystic fibrosis transmembrane conductance regulator SOD Superoxide dismutase LAMP-1 lactate dehydrogenase LDH Lactoferrin myeloperoxidase Neutrophils lysosomal-associated membrane protein-1