Possible identity of IL-8 converting enzyme in human fibroblasts as a cysteine protease
| Autor: | Kensaku Ohashi, Emiko Sano, Toshio Nakaki, Masanobu Naruto |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
medicine.medical_treatment
Immunology Cysteine Proteinase Inhibitors Biology chemistry.chemical_compound medicine Humans Immunology and Allergy Secretion Fibroblast Polyacrylamide gel electrophoresis Cells Cultured Pharmacology chemistry.chemical_classification Protease Interleukin-8 Interferon-beta Fibroblasts Molecular biology Cysteine protease In vitro Cysteine Endopeptidases Poly I-C Enzyme medicine.anatomical_structure Biochemistry chemistry Antipain Protein Processing Post-Translational |
| Zdroj: | International Immunopharmacology. 3:609-614 |
| ISSN: | 1567-5769 |
| DOI: | 10.1016/s1567-5769(03)00023-7 |
| Popis: | A converting activity was characterized in human diploid fibroblasts, which secrete 72IL-8 and 77IL-8 in treatment with IFN-β and poly I: poly C. 77IL-8 was significantly converted to 72IL-8 by a partially purified fraction of the culture supernatant of human diploid fibroblasts. The converting activity, which was temperature-dependent and optimal at pH 6, was completely inhibited by cysteine protease inhibitors, antipain dihydrochloride and E-64, but not by other types of protease inhibitors. These data clearly show that human diploid fibroblasts are capable of processing IL-8 to produce a mature IL-8 and that the putative converting enzyme appears to be a cysteine protease. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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