Sökning: (WFRF:(Wetterö Jonas)) pers:(Bengtsson Torbjörn 1955) >
Solid-phase classic...
Solid-phase classical complement activation by C-reactive protein (CRP) is inhibited by fluid-phase CRP-C1q interaction.
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- Sjöwall, Christoffer (författare)
- Östergötlands Läns Landsting,Linköpings universitet,Reumatologi,Hälsouniversitetet,Länskliniken för Reumatologi i Östergötland
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- Wetterö, Jonas (författare)
- Linköpings universitet,Reumatologi,Hälsouniversitetet
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- Bengtsson, Torbjörn, 1955- (författare)
- Linköpings universitet,Farmakologi,Hälsouniversitetet
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- Askendal, Agneta (författare)
- Linköpings universitet,Institutionen för fysik, kemi och biologi,Tekniska högskolan
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- Almroth, Gunnel (författare)
- Division of Rheumatology, AIR, Department of Molecular and Clinical Medicine, Linköping, Sweden
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- Skogh, Thomas (författare)
- Östergötlands Läns Landsting,Linköpings universitet,Reumatologi,Tekniska högskolan,Länskliniken för Reumatologi i Östergötland
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- Tengvall, Pentti (författare)
- Linköpings universitet,Gothenburg University,Göteborgs universitet,Institutionen för kliniska vetenskaper,Institute of Clinical Sciences,Materials in Medicine, Division of Applied Physics, Department of Physics, Chemistry and Biology, Linköping, Sweden,Tillämpad Fysik,Tekniska högskolan
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(creator_code:org_t)
- Elsevier BV, 2007
- 2007
- Engelska.
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Ingår i: Biochemical and biophysical research communications. - : Elsevier BV. - 0006-291X .- 1090-2104. ; 352:1, s. 251-8
- Relaterad länk:
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http://urn.kb.se/res...
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https://liu.diva-por... (primary) (Raw object)
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https://gup.ub.gu.se...
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https://doi.org/10.1...
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https://urn.kb.se/re...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- C-reactive protein (CRP) interacts with phosphorylcholine (PC), Fcgamma receptors, complement factor C1q and cell nuclear constituents, yet its biological roles are insufficiently understood. The aim was to characterize CRP-induced complement activation by ellipsometry. PC conjugated with keyhole limpet hemocyanin (PC-KLH) was immobilized to cross-linked fibrinogen. A low-CRP serum with different amounts of added CRP was exposed to the PC-surfaces. The total serum protein deposition was quantified and deposition of IgG, C1q, C3c, C4, factor H, and CRP detected with polyclonal antibodies. The binding of serum CRP to PC-KLH dose-dependently triggered activation of the classical pathway. Unexpectedly, the activation was efficiently down-regulated at CRP levels > 150 mg/L. Using radial immunodiffusion, CRP-C1q interaction was observed in serum samples with high CRP concentrations. We propose that the underlying mechanism depends on fluid-phase interaction between C1q and CRP. This might constitute another level of complement regulation, which has implications for systemic lupus erythematosus where CRP is often low despite flare-ups.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Klinisk medicin -- Odontologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Clinical Medicine -- Dentistry (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)
Nyckelord
- C-Reactive Protein
- immunology
- metabolism
- Complement Activation
- drug effects
- immunology
- Complement C1q
- immunology
- metabolism
- Humans
- Immunoglobulin G
- immunology
- Phosphorylcholine
- pharmacology
- Protein Binding
- Silicon
- C-reactive protein; C1q; complement; inflammation; opsonization; pentraxins; systemic lupus erythematosus
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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