Key result
Apolipoproteins A-I and A-II bind to C9 polymers and completely inhibit zinc-catalyzed C9 polymerization at concentrations ≥5 µM, preventing C9 incorporation into C5b-9 complexes on endothelial cells.
Population
Human endothelial cells and purified complement components (C9) and apolipoproteins (A-I and A-II)
Design
Preclinical
Authors
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May protect endothelium from complement injury; hypothesis-generating for HDL mechanisms in human vascular disease.
Apolipoproteins A-I and A-II inhibit C9 polymerization, providing a mechanistic explanation for the protective effect of HDL on cells exposed to activated complement.
Hamilton et al. (1993) studied this question. Apolipoproteins A-I and A-II was evaluated on C9 polymerization and incorporation into C5b-9 complexes. Apolipoproteins A-I and A-II bind to C9 polymers and completely inhibit zinc-catalyzed C9 polymerization at concentrations ≥5 µM, preventing C9 incorporation into C5b-9 complexes on endothelial cells.
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