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Contribution of cho...
Contribution of chondroitin sulfate A to the binding of complement proteins to activated platelets
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- Hamad, Osama A., 1978- (författare)
- Uppsala universitet,Enheten för klinisk immunologi,Complement And Biomaterials,Uppsala University
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- Nilsson Ekdahl, Kristina (författare)
- Linnéuniversitetet,Institutionen för naturvetenskap, NV,Uppsala University
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- Nilsson, Per H. (författare)
- Linnéuniversitetet,Institutionen för naturvetenskap, NV
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- Lasaosa, Maria (författare)
- University of Pennsylvania, USA
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- Ricklin, Daniel (författare)
- University of Pennsylvania, USA
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- Lambris, John D. (författare)
- University of Pennsylvania, USA
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- Nilsson, Bo (författare)
- Uppsala University
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(creator_code:org_t)
- 2010-09-23
- 2010
- Engelska.
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Ingår i: PLoS ONE. - : Public Library of Science (PLoS). - 1932-6203. ; 5:9, s. e12889-
- Relaterad länk:
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https://doi.org/10.1...
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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
- Exposure of chondroitin sulfate A (CS-A) on the surface of activated platelets is well established. The aim of the present study was to investigate to what extent CS-A contributes to the binding of C1q and the complement regulators C1 inhibitor (C1INH), C4b-binding protein (C4BP), and factor H to platelets. Human serum was passed over Sepharose conjugated with CS-A, and bound proteins were identified by Western blotting, and mass spectrometric analysis. C1q was identified as the main protein that specifically bound to CS-A, but C4BP and factor H were also shown to interact. Binding of C1INH was dependent of the presence of C1q and not bound to CS-A from C1q-depleted serum. The specific interactions observed of these proteins with CS-A were subsequently confirmed by surface plasmon resonance analysis using purified proteins. Importantly, C1q, C4BP, and factor H were shown to bind also to activated platelets and this interaction was inhibited by a CS-A-specific monoclonal antibody, thereby linking the binding of C1q, C4BP, and factor H to exposure of CS-A on platelets. CS-A-bound C1q was also shown to amplify the binding of model immune complexes to both microtiter plate-bound CS-A and to activated platelets. In conclusion, this study supports the concept that CS-A contributes to the binding of C1q, C4BP, and factor H to platelets, thereby adding CS-A to the previously reported binding sites for these proteins on the platelet surface. CS-A-bound C1q seems to amplify the binding of immune complexes to activated platelets, suggesting a role for this molecule in immune complex diseases.
Ämnesord
- 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)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi -- Biomedicinsk laboratorievetenskap/teknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology -- Biomedical Laboratory Science/Technology (hsv//eng)
Nyckelord
- chondroitin sulfate
- activated platelets
- complement proteins
- complement inhibitors
- TRAP
- C1q
- Immunology
- Immunologi
- Klinisk immunologi
- Clinical Immunology
- MEDICINE
- Biomedical Sciences
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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