1. Advanced glycation end products stimulate plasminogen activator activity via GM-CSF in RAW 264.7 cells
- Author
-
Yoshiteru Jinnouchi, T. Saishoji, Kazuyoshi Ikeda, Hiroyuki Sano, Minetaro Ogawa, Takayuki Higashi, and Seikoh Horiuchi
- Subjects
Glycosylation ,Endocytic cycle ,Molecular Sequence Data ,Biophysics ,Serum albumin ,Plasminogen activator activity ,Biochemistry ,Cell Line ,Mice ,Plasminogen Activators ,Glycation ,Plasminogen Activator Inhibitor 1 ,Animals ,Humans ,RNA, Messenger ,Molecular Biology ,RAW 264.7 Cells ,DNA Primers ,Extracellular Matrix Proteins ,biology ,Base Sequence ,Chemistry ,Macrophages ,Granulocyte-Macrophage Colony-Stimulating Factor ,Cell Biology ,Urokinase-Type Plasminogen Activator ,In vitro ,Cell biology ,Tissue Plasminogen Activator ,biology.protein ,Antibody ,Plasminogen activator - Abstract
The effects of advanced glycation end products (AGE) on the plasminogen activator (PA) activity were investigated with murine macrophage cell line RAW 264.7 cells. AGE-bovine serum albumin (BSA) showed a dose-dependent induction for the urokinase-type PA (uPA) activity. The uPA induction by AGE-BSA was effectively suppressed by the antibody against Fl granulocyte-macrophage colony-stimulating factor (GM-CSF). The uPA activity of these cells was also induced by ligands for the macrophage scavenger receptor (MSR). These data provide evidence that AGE-BSA. stimulates the uPA activity via GM-CSF through MSR in RAW cells. These findings, taken together with a recent demonstration of endocytic uptake of AGE-proteins by MSR in vitro and the presence of AGE-proteins in atherosclerotic lesions, strongly suggest that the uPA induction by AGE-proteins via MSR plays an important role in human atherogenesis.
- Published
- 1995