Matrix metalloproteinase-1, soluble Fas ligand, and soluble Fas antigen levels in patients with multiple organ dysfunction syndrome
© Current Science Ltd 1998
Published: 1 March 1998
Fas L induces apoptosis by binding to Fas. It is reported that the extracellular matrix degrading enzyme, metalloproteinase, is involved in conversion from membrane Fas L to soluble Fas (sFas).
In this study, the involvement of matrix metalloproteinase-1 (MMP-1), soluble Fas ligand (sFasL), and soluble Fas antigen (sFas) in apoptosis at the onset of multiple organ dysfunction syndrome (MODS) was examined.
The subjects were 52 patients. Blood sampling was continued from the time before or at the onset of MODS up to its recovery or death. MMP-1, the tissue inhibitor of metalloproteinase-1 (TIMP-1), MMP-1/TIMP-1 complex, sFas L, sFas, tumor necrosis factor-α (TNF-α), TNF receptor I (TNFR I), TNFR II, nitrite/nitrate (NOx), transforming growth factor β (TGF-β), and endotoxin were measured.
With the increase in dysfunctional organs, sFas, TNF-α, and NOx increased, and showed significantly higher levels in those that died than in the survivors. Their levels were significantly correlated with the MMP-1 level, and the MMP-1 level was negatively correlated with the TGF-β level.
At the onset of MODS, the sFas, TNF-α, and NOx levels were high, suggesting that apoptosis occurred. It was also suggested that MMP-1 was involved in sFas and TNF-α production, and TGF-β suppressed MMP-1 production.