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(American Journal of Pathology. 2000;156:1549-1556.)
© 2000 American Society for Investigative Pathology

Regular Articles

Complement Activation after Oxidative Stress

Role of the Lectin Complement Pathway

Charles D. Collard*, Antti Väkevä{dagger}, Margaret A. Morrissey*, Azin Agah*, Scott A. Rollins{ddagger}, Wende R. Reenstra§, Jon A. Buras, Seppo Meri{dagger} and Gregory L. Stahl*

From the Center for Experimental Therapeutics and Reperfusion Injury,*
Department of Anesthesiology, Perioperative and Pain Medicine, Brigham and Women’s Hospital, Harvard Medical School, Boston, Massachusetts; the Department of Bacteriology and Immunology,{dagger}
University of Helsinki and the Helsinki University Central Hospital, Helsinki, Finland; Alexion Pharmaceuticals,{ddagger}
New Haven, Connecticut; the Department of Clinical Pathology,§
Boston University School of Medicine, Boston, Massachusetts; and the Department of Emergency Medicine,
Brigham and Women’s Hospital, Harvard Medical School, Boston, Massachusetts

The complement system plays an important role in mediating tissue injury after oxidative stress. The role of mannose-binding lectin (MBL) and the lectin complement pathway (LCP) in mediating complement activation after endothelial oxidative stress was investigated. iC3b deposition on hypoxic (24 hours; 1% O2)/reoxygenated (3 hours; 21% O2) human endothelial cells was attenuated by N-acetyl-D-glucosamine or D-mannose, but not L-mannose, in a dose-dependent manner. Endothelial iC3b deposition after oxidative stress was also attenuated in MBL-deficient serum. Novel, functionally inhibitory, anti-human MBL monoclonal antibodies attenuated MBL-dependent C3 deposition on mannan-coated plates in a dose-dependent manner. Treatment of human serum with anti-MBL monoclonal antibodies inhibited MBL and C3 deposition after endothelial oxidative stress. Consistent with our in vitro findings, C3 and MBL immunostaining throughout the ischemic area at risk increased during rat myocardial reperfusion in vivo. These data suggest that the LCP mediates complement activation after tissue oxidative stress. Inhibition of MBL may represent a novel therapeutic strategy for ischemia/reperfusion injury and other complement-mediated disease states.




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