Barry and McGivan [22] reported that acetaldehyde, an intermediate product of alcohol metabolism, can bind to hepatocyte plasma membranes, resulting in the activation of C3 by causing a structural change in the surface of the plasma membrane. A previous study in rats revealed that the expression of complement components (C1, C3, and C8) was elevated, while the expression of complement receptor 1 (CR1)-related protein y (Crry) and CD59 was reduced after long-term alcohol feeding [26]. Wlazlo et al. [5] showed that the serum level of C3a, an indicator of C3 activation, was associated with liver steatosis and hepatocellular injury in individuals who are chronic alcohol abusers. In mouse models of ethanol feeding, Bykov et al. [27] found that C3+/+ mice developed AFLD, while C3–/– mice had reduced lipid accumulation in the liver. In a study of the role of C3 in AFLD, the authors suggested that C3a binding to the receptor C3aR, which is highly expressed on Kupffer cells, can promote the inflammatory response and stimulate the release of the inflammatory cytokine tumor necrosis factor-α (TNF-α). TNF-α participates in AFLD,
