Journal
MOLECULAR IMMUNOLOGY
Volume 41, Issue 2-3, Pages 185-190Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.molimm.2004.03.029
Keywords
ClqRO(2)(-); methyl beta cyclodextrin; CD59; calreticulin
Categories
Funding
- NIAID NIH HHS [R01 AI42987] Funding Source: Medline
- NIAMS NIH HHS [R01 AR47243] Funding Source: Medline
- NIDDK NIH HHS [P30 DK34845] Funding Source: Medline
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Calreticulin, a candidate C1q receptor, was shown recently to be present on the surface of human neutrophils in association with glycosylphosphatidylinositol (GPI) anchored proteins, particularly CD59. In this study, we show that antibodies to CD59, as well as to every other GPI-anchored protein tested, inhibited the C1q-triggered release of O-2(-) from PMN. Methyl beta cyclodextrin (MbetaCD) treatment of the cells to disrupt lipid rafts also prevented C1q-triggered O-2(-) production. beta(2) integrin-dependent co-stimulation is required for O-2(-) production from PMN, however MbetaCD had no effect on LFA-1 or Mac-1-mediated adhesion, soluble iC3b binding to PMN, or spreading and migration, all of which suggested that PMN integrin function remained intact. Flow cytometric analysis of PMN treated with MbetaCD showed upregulation of PMN granule-associated integrins and a corresponding increase in integrin activation-reporter epitopes, in contrast to the decreased expression of GPI-anchored antigens. These data support a model where lipid rafts and their associated GPI-anchored proteins are critical for C1q-triggered O-2(-) production, consistent with a model where calreticulin serves as the C1q receptor for O-2(-) production from PMN. (C) 2004 Elsevier Ltd. All rights reserved.
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