Identification of novel matrix metalloproteinase-7 (matrilysin) cleavage sites in murine and human Fas ligand.

@article{VargoGogola2002IdentificationON,
  title={Identification of novel matrix metalloproteinase-7 (matrilysin) cleavage sites in murine and human Fas ligand.},
  author={Tracy Vargo-Gogola and Howard C. Crawford and Barbara Fingleton and Lynn M Matrisian},
  journal={Archives of biochemistry and biophysics},
  year={2002},
  volume={408 2},
  pages={155-61}
}
Soluble Fas ligand (sFasL) is released from the cell surface by matrix metalloproteinases (MMPs), one of which is MMP-7. We have reported that MMP-7-generated sFasL is pro-apoptotic in both in vitro and in vivo systems. However, there are contradictory reports that the soluble form of FasL is inactive or anti-apoptotic, resulting in significant controversy in the literature. One potential explanation for these discrepancies is that forms of sFasL with different amino-terminal sequences have… CONTINUE READING
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