Contribution of chondroitin sulfate A to the binding of complement proteins to activated platelets

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Contribution of chondroitin sulfate A to the binding of complement proteins to activated platelets

Hamad, Osama A., 1978- (author): Uppsala universitet,Enheten för klinisk immunologi,Complement And Biomaterials,Uppsala University

Nilsson Ekdahl, Kristina (author): Linnéuniversitetet,Institutionen för naturvetenskap, NV,Uppsala University

Nilsson, Per H. (author): Linnéuniversitetet,Institutionen för naturvetenskap, NV

Lasaosa, Maria (author): University of Pennsylvania, USA

Ricklin, Daniel (author): University of Pennsylvania, USA

Lambris, John D. (author): University of Pennsylvania, USA

Nilsson, Bo (author): Uppsala University

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(creator_code:org_t)

2010-09-23
2010
English.
In: PLoS ONE. - : Public Library of Science (PLoS). - 1932-6203. ; 5:9, s. e12889-

Related links:: https://journals.plo...; show more...; https://doi.org/10.1...; https://urn.kb.se/re...; https://doi.org/10.1...; https://urn.kb.se/re...; show less...

Journal article (peer-reviewed)

Abstract Subject headings

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.

Subject headings

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)

Keyword

chondroitin sulfate
activated platelets
complement proteins
complement inhibitors
TRAP
C1q
Immunology
Immunologi
Klinisk immunologi
Clinical Immunology
MEDICINE
Biomedical Sciences

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MEDICAL AND HEALTH SCIENCES: MEDICAL AND HEAL ...; and Basic Medicine; and Immunology in th ...

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By the university: Uppsala University; Linnaeus University

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