The expression of extracellular-superoxide dismutase is increased by lysophosphatidylcholine in human monocytic U937 cells.

Extracellular-superoxide dismutase (EC-SOD) [EC 1.15.1.1] is a secretory glycoprotein with an affinity for heparin-like proteoglycans. This enzyme locates in blood vessel walls at high levels and may be important for the antioxidant capability of vascular walls. Oxidative process plays an important role in atherogenesis. Lysophosphatidylcholine (lysoPC) is generated during oxidation of low-density lipoprotein (LDL) and is located within atherosclerotic plaques. Recently, lysoPC has been reported to induce transcription of a variety of cellular genes. In this study, we observed that lysoPC significantly increased the expression of EC-SOD mRNA and protein in human monocytic U937 cells, but not those of CuZn-SOD or Mn-SOD. Induced EC-SOD by lysoPC had a high affinity for heparin, and may bind to the endothelial cell surface. Very recently, it has been reported that exogenous addition of EC-SOD or overexpression of EC-SOD prevented endothelial cell-mediated oxidative modification of LDL. Therefore, it is speculated that EC-SOD is induced by lysoPC-stimulated monocytes as a feedback mechanism in vascular homeostasis.