Abstract
The C-type lectin of the aggrecan G3 domain activates complement
Highlights
The complement system provides defense against foreign pathogens but it acts as a sensor of danger, aiding in the removal of dying cells, immune-complexes and misfolded molecules [1]
We assessed the ability of fragments of aggrecan G3 domain to activate complement by coating proteins onto microtiter plate wells followed by incubation with increasing concentrations of Normal human serum (NHS) and detection of deposited complement proteins with specific antibodies
Less of the MAC component C9 was detected on LCt and Lt compared to IgG but this deposition was still significantly higher than background observed for BSA (Fig. 2D)
Summary
The complement system provides defense against foreign pathogens but it acts as a sensor of danger, aiding in the removal of dying cells, immune-complexes and misfolded molecules [1]. Cartilage proteins are fragmented and released into the synovial fluid where they can interact with complement This has been proposed to contribute to the local pro-inflammatory milieu in joints of patients suffering from RA. C1q, the initiator of the classical pathway, binds to decorin [5,6], biglycan [5], fibronectin [7], laminin [8], osteoadherin [6], fibromodulin [9], cartilage oligomeric matrix protein (COMP) [10] and more weakly to lumican [6] and chondroadherin [6]. COMP, an established marker of joint destruction, activates the alternative complement pathway [10,12]
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