Metalloproteinase-mediated release of human Fas ligand
| Autor: | Kohichiro Yoshino, Akemi Kawasaki, Tomohiko Ebata, H Ohmoto, Hideo Yagita, Inoue S, Ko Okumura, Shoji Ikeda, Nobuhiko Kayagaki |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Fas Ligand Protein
medicine.drug_class Immunoprecipitation medicine.medical_treatment Immunology chemical and pharmacologic phenomena Biology Matrix metalloproteinase Transfection Monoclonal antibody Fas ligand Mice medicine Animals Humans Immunology and Allergy Protease Inhibitors Cells Cultured Metalloproteinase Membrane Glycoproteins Tumor Necrosis Factor-alpha Cell Membrane Membrane Proteins Metalloendopeptidases hemic and immune systems Articles Molecular biology Mice Mutant Strains Cell biology Cytokine Solubility Tumor necrosis factor alpha biological phenomena cell phenomena and immunity Protein Processing Post-Translational |
| Zdroj: | The Journal of Experimental Medicine |
| ISSN: | 1540-9538 0022-1007 |
| DOI: | 10.1084/jem.182.6.1777 |
| Popis: | Fas ligand (FasL) is a type II integral membrane protein homologous with tumor necrosis factor (TNF). Recent studies indicate that TNF is processed to yield the soluble cytokine by metalloproteinases at the cell surface of activated macrophages and T cells. In the present study, we investigated whether FasL is also released by metalloproteinases. Treatment with hydroxamic acid inhibitors of matrix metalloproteinases specifically led to accumulation of membrane-type FasL (p40) on the surface of human FasL cDNA transfectants and activated human T cells, as estimated by surface immunofluorescence and immunoprecipitation with newly established anti-human FasL monoclonal antibodies. This surface accumulation of mFasL was associated with the decrease of soluble FasL (p27) in the supernatant as estimated by quantitative ELISA and immunoprecipitation with anti-human FasL monoclonal antibodies. These results indicate that human FasL is efficiently released from the cell surface by metalloproteinases like TNF. |
| Databáze: | OpenAIRE |
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