Receptor-mediated binding of C1q on pulmonary endothelial cells.
Normal undamaged pulmonary endothelial cells appear to be immunologically privileged in that they do not express receptors for the Fc portion of IgG nor for C3b. However, these receptors become unmasked on endothelial cells injured by viral infection or exposure to white cell lysates. We now present evidence to indicate that C1q binds to specific receptors on the surface of normal healthy endothelial cells. The binding is dose-dependent, reversible and saturable. Furthermore our data show that binding of C1q to endothelial cells is via the collagenous portion of the molecule not via the globular head regions. Thus binding of C1q to endothelium would have the effect of exposing Fc receptors that could then bind to IgG of circulating immune complexes. That Fc receptors are in fact exposed is shown by rosette formation with antibody sensitized erythrocytes. With 2C1r-2C1s-associated C1q, no binding occurred using C1 fixation and transfer assays. Our results indicate that C1q binding to endothelium provides a means for localizing immune complexes on pulmonary vessels and may be important in the initiation and progression of the inflammatory response.
D000818:Animals; D002352:Carrier Proteins; D002417:Cattle; D003094:Collagen / Q000378:metabolism / Q000502:physiology; D003166:Complement Activating Enzymes / Q000378:metabolism*; D015922:Complement C1q; D004727:Endothelium / Q000378:metabolism; D006801:Humans; D018960:Hyaluronan Receptors; D007700:Kinetics; D008562:Membrane Glycoproteins; D024101:Mitochondrial Proteins; D011651:Pulmonary Artery / Q000378:metabolism*; D011951:Receptors, Complement / Q000032:analysis / Q000502:physiology*
C087299:C1QBP protein, human; D002352:Carrier Proteins; D018960:Hyaluronan Receptors; D008562:Membrane Glycoproteins; D024101:Mitochondrial Proteins; D011951:Receptors, Complement; C032402:complement 1q receptor; D015922:Complement C1q; D003094:Collagen; D003166:Complement Activating Enzymes