Metalloproteases and Serineproteases are Involved in the Cleavage of the Two Tumour Necrosis Factor (TNF) Receptors to Soluble Forms in the Myeloid Cell Lines U-937 and THP-1
| Autor: | Mikael Lantz, F Björnberg, U Gullberg |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Metalloproteinase
Proteases Protease medicine.medical_treatment Serine Endopeptidases Immunology Metalloendopeptidases General Medicine Biology Molecular biology Receptors Tumor Necrosis Factor Biochemistry Cell culture Tumor Cells Cultured medicine Humans Tetradecanoylphorbol Acetate Metalloprotease inhibitor THP1 cell line Enzyme Inhibitors Signal transduction Receptor Signal Transduction |
| Zdroj: | Scandinavian Journal of Immunology. 42:418-424 |
| ISSN: | 1365-3083 0300-9475 |
| Popis: | The proteolytic processing of the two TNF receptors (TNF-R55 and TNF-R75) into soluble forms was investigated in the myeloid cell lines U-937 and THP-1. Phorbol myristate acetate (PMA) rapidly stimulated release of soluble forms of both TNF-receptors. Incubations were made with PMA and protease inhibitors directed against different target protease groups. The serineprotease inhibitors TPCK and dichloroisocoumarin and the metalloprotease inhibitor 1,10-phenanthroline reduced PMA-induced release of both soluble receptor forms with about 60-70%. Furthermore, 1,10-phenanthroline also reduced PMA-induced down-regulation of TNF-receptors in both cell lines as judged by TNF-binding to cells. Reduced down-regulation and TNF-receptor shedding by 1,10-phenanthroline was reversed by Zn2+, indicating involvement of a Zn(2+)-dependent metalloprotease. Thus, both serine proteases and metalloproteases are involved in the processing of TNF-receptors. |
| Databáze: | OpenAIRE |
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