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Particles binding β...
Particles binding β2-integrins mediate intracellular production of oxidative metabolites in human neutrophils independently of phagocytosis
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- Serrander, Lena (författare)
- Linköpings universitet,Medicinsk mikrobiologi,Hälsouniversitetet
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- Larsson, Jenny (författare)
- Linköpings universitet,Patologi,Hälsouniversitetet
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- Lundqvist, Helen, 1966- (författare)
- Linköpings universitet,Patologi,Hälsouniversitetet
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- Lindmark, Maria, 1972- (författare)
- Linköpings universitet,Medicinsk mikrobiologi,Hälsouniversitetet
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- Fällman, Maria (författare)
- Department of Medical Microbiology, University of Umeå, Umeå, Sweden
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- Dahlgren, Claes (författare)
- Department of Medical Microbiology, University of Göteborg, Göteborg, Sweden
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- Stendahl, Olle, 1946- (författare)
- Linköpings universitet,Medicinsk mikrobiologi,Hälsouniversitetet
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(creator_code:org_t)
- 1999
- 1999
- Engelska.
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Ingår i: Biochimica et Biophysica Acta. Molecular Cell Research. - 0167-4889 .- 1879-2596. ; 1452:2, s. 133-144
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Complement-opsonised particles are readily ingested by human neutrophils through a complement receptor-mediated process leading to phagolysosome fusion and production of oxidative metabolites. To investigate the complement receptor 3 (CR3)-associated signal system involved, cells were challenged with protein A-positive, heat-killed Staphylococcus aureus to which antibodies with specificity for the subunits of the β2-integrins, i.e. anti-CD11b (the α subunit of CR3) and anti-CD18 (the β subunit of CR3), were bound through their Fc moiety. Despite not being ingested by the neutrophils, the surface associated anti-CD18- and anti-CD11b-coated particles were able to activate the neutrophil NADPH-oxidase. Also anti-CD11a- (the α subunit of LFA-1) and to a lesser extent anti-CD11c- (the α subunit of CR4) coated particles were able to trigger the NADPH-oxidase. The NADPH-oxidase was activated without extracellular release of reactive oxygen species. The activity was inhibited by cytochalasin B, suggesting a necessary role for the cytoskeleton in the signalling pathway that activates the oxidase. We show that particle-mediated cross-linking of β2-integrins on the neutrophil surface initiates a signalling cascade, involving cytoskeletal rearrangements, leading to an activation of the NADPH-oxidase without phagosome formation or extracellular release of reactive oxygen species.
Nyckelord
- MEDICINE
- MEDICIN
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