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C1q induces a rapid up-regulation of P-selectin and modulates collagen- and collagen-related peptide-triggered activation in human platelets
Div Drug Res, Dept Med & Hlth Sci, Linkoping Univ, Linkoping, Sweden.
Rheumatol Autoimmun & Immune Regulat Unit, Dept Clin & Expt Med, Linkoping Univ, Linkoping, Sweden.
Inst Clin Sci, Dept Biomat, Sahlgrenska Acad, Univ Gothenburg, Gothenburg, Sweden.
Örebro University, School of Health and Medical Sciences. Div Drug Res, Dept Med & Hlth Sci, Linkoping Univ, Linkoping, Sweden.
2010 (English)In: Immunobiology, ISSN 0171-2985, E-ISSN 1878-3279, Vol. 215, no 12, p. 987-995Article in journal (Refereed) Published
Abstract [en]

Blood platelets are emerging as important immunomodulatory cells, but complement interaction with platelets is not well understood. Several platelet structures have been described as complement protein 1q (C1q) binding receptors, such as C1qRp/CD93 and gC1qR. However, there are conflicting results whether these receptors are C1q binding structures, or even at all expressed on the cell surface. Recently, the collagen-binding integrin alpha II beta I was reported to bind C1q on mast cells, and this receptor is also present on platelets. The aim of this study was to further characterize the effects of C1q on platelets, by quantifying the platelet surface expression of P-selectin (CD62P) and monitoring the formation of platelet-neutrophil aggregates. Using flow cytometry, we found that C1q dose-dependently triggered a rapid but moderate and transient up-regulation of P-selectin already within 5s of C1q exposure. Pre-incubation with an antibody directed against gC1qR significantly inhibited (with 57% compared to control) the up-regulation, whereas an antibody towards the alpha II beta I-integrin showed no effect. Stimulation with C1q did not change the cytosolic calcium-levels, as measured with the fluorescent ratiometric probe Fura-2, however, a protein kinase C inhibitor (GF109203x) blocked the C1q-induced P-selectin expression. Furthermore, pre-incubation of platelets with C1q diminished both the collagen as well as the collagen-related peptide-induced up-regulation of P-selectin, most evident after 90 s of stimulation. This indicates that C1q may regulate platelet activation via the GPVI receptor, which is a novel finding. Moreover, C1q antagonized the collagen-induced formation of platelet-neutrophil aggregates, indicating a reduced interaction between platelet P-selectin and neutrophil P-selectin glycoprotein ligand-1(PSGL-1/CD162). In summary, C1q induces a moderate rapid platelet P-selectin expression, modulates subsequent collagen and collagen-related peptide stimulation of platelets, and inhibits the formation of platelet-neutrophil aggregates. These immuno-regulatory effects of C1q may have a crucial role in innate immunity and inflammation. (C) 2009 Elsevier GmbH. All rights reserved.

Place, publisher, year, edition, pages
Jena, Germany: Elsevier, 2010. Vol. 215, no 12, p. 987-995
Keywords [en]
AlfaIIbetaI integrin (αIIβI, GpIa/IIa), Blood platelet, C1q, C1qR, Complement, P-selectin (CD62 P), Platelet-neutrophil aggregates
National Category
Medical and Health Sciences Cell and Molecular Biology
Research subject
Biomedicine
Identifiers
URN: urn:nbn:se:oru:diva-18864DOI: 10.1016/j.imbio.2009.11.004ISI: 000285532100007PubMedID: 20163886Scopus ID: 2-s2.0-78049244887OAI: oai:DiVA.org:oru-18864DiVA, id: diva2:445639
Available from: 2011-10-04 Created: 2011-09-30 Last updated: 2018-04-24Bibliographically approved

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