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Properdin binding t...
Properdin binding to complement activating surfaces depends on initial C3b deposition
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- Harboe, Morten (författare)
- Oslo University Hospital, Norway,Natl Hosp Norway, Oslo Univ Hosp, Dept Immunol, N-0424 Oslo, Norway.
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- Johnson, Christina (författare)
- Oslo University Hospital, Norway,Natl Hosp Norway, Oslo Univ Hosp, Dept Immunol, N-0424 Oslo, Norway.
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- Nymo, Stig (författare)
- Nordland Hospital, Norway,Nordland Hosp, Res Lab, N-8092 Bodo, Norway.
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- Ekholt, Karin (författare)
- Oslo University Hospital, Norway,Natl Hosp Norway, Oslo Univ Hosp, Dept Immunol, N-0424 Oslo, Norway.
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- Schjalm, Camilla (författare)
- Oslo University Hospital, Norway,Natl Hosp Norway, Oslo Univ Hosp, Dept Immunol, N-0424 Oslo, Norway.
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- Lindstad, Julie K. (författare)
- Oslo University Hospital, Norway,Natl Hosp Norway, Oslo Univ Hosp, Dept Immunol, N-0424 Oslo, Norway.
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- Pharo, Anne (författare)
- Oslo University Hospital, Norway,Natl Hosp Norway, Oslo Univ Hosp, Dept Immunol, N-0424 Oslo, Norway.
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- Hellerud, Bernt Christian (författare)
- Oslo University Hospital, Norway,Natl Hosp Norway, Oslo Univ Hosp, Dept Immunol, N-0424 Oslo, Norway.
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- Nilsson Ekdahl, Kristina (författare)
- Uppsala universitet,Linnéuniversitetet,Institutionen för kemi och biomedicin (KOB),Uppsala University,Linnaeus Ctr Biomat Chem, BMC,Klinisk immunologi,Linnaeus Univ, Linnaeus Ctr Biomat Chem, S-39182 Kalmar, Sweden.
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- Mollnes, Tom Eirik (författare)
- Oslo University Hospital, Norway ; Nordland Hospital, Norway ; University of Oslo, Norway ; University of Tromsø, Norway ; Norwegian University of Science and Technology, Norway,Natl Hosp Norway, Oslo Univ Hosp, Dept Immunol, N-0424 Oslo, Norway.;Nordland Hosp, Res Lab, N-8092 Bodo, Norway.;Univ Oslo, KG Jebsen Inflammatory Res Ctr, N-0424 Oslo, Norway.;Univ Tromso, Fac Hlth Sci, KG Jebsen Thrombosis Res & Expertise Ctr, N-9037 Tromso, Norway.;Norwegian Univ Sci & Technol, Ctr Mol Inflammat Res, N-7491 Trondheim, Norway.
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- Nilsson, Per H. (författare)
- Linnéuniversitetet,Institutionen för kemi och biomedicin (KOB),Oslo University Hospital, Norway;University of Oslo, Norway,Linnaeus Ctr Biomat Chem, BMC;HoRB,Natl Hosp Norway, Oslo Univ Hosp, Dept Immunol, N-0424 Oslo, Norway.;Linnaeus Univ, Linnaeus Ctr Biomat Chem, S-39182 Kalmar, Sweden.;Univ Oslo, KG Jebsen Inflammatory Res Ctr, N-0424 Oslo, Norway.
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Oslo University Hospital, Norway Natl Hosp Norway, Oslo Univ Hosp, Dept Immunol, N-0424 Oslo, Norway (creator_code:org_t)
- 2017-01-09
- 2017
- Engelska.
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 114:4, s. E534-E539
- Relaterad länk:
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https://www.pnas.org...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- Two functions have been assigned to properdin; stabilization of the alternative convertase, C3bBb, is well accepted, whereas the role of properdin as pattern recognition molecule is controversial. The presence of nonphysiological aggregates in purified properdin preparations and experimental models that do not allow discrimination between the initial binding of properdin and binding secondary to C3b deposition is a critical factor contributing to this controversy. In previous work, by inhibiting C3, we showed that properdin binding to zymosan and Escherichia coli is not a primary event, but rather is solely dependent on initial C3 deposition. In the present study, we found that properdin in human serum bound dose-dependently to solid-phase myeloperoxidase. This binding was dependent on C3 activation, as demonstrated by the lack of binding in human serum with the C3-inhibitor compstatin Cp40, in C3-depleted human serum, or when purified properdin is applied in buffer. Similarly, binding of properdin to the surface of human umbilical vein endothelial cells or Neisseria meningitidis after incubation with human serum was completely C3-dependent, as detected by flow cytometry. Properdin, which lacks the structural homology shared by other complement pattern recognition molecules and has its major function in stabilizing the C3bBb convertase, was found to bind both exogenous and endogenous molecular patterns in a completely C3-dependent manner. We therefore challenge the view of properdin as a pattern recognition molecule, and argue that the experimental conditions used to test this hypothesis should be carefully considered, with emphasis on controlling initial C3 activation under physiological conditions.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Immunologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Immunology in the medical area (hsv//eng)
Nyckelord
- complement
- properdin
- C3
- myeloperoxidase
- Neisseria meningitidis
- Biomedical Sciences
- Biomedicinsk vetenskap
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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Harboe, Morten
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Johnson, Christi ...
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Nymo, Stig
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Ekholt, Karin
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Schjalm, Camilla
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Lindstad, Julie ...
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visa fler...
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Pharo, Anne
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Hellerud, Bernt ...
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Nilsson Ekdahl, ...
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Mollnes, Tom Eir ...
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Nilsson, Per H.
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Linnéuniversitetet
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