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Identification of the proteolytic enzyme which cleaves human p75 TNF receptor in vitro

  • Author(s): Katsura, K
  • Park, M
  • Gatanaga, M
  • Yu, EC
  • Takishima, K
  • Granger, GA
  • Gatanaga, T
  • et al.
Abstract

The extracellular domains of the human 55 and 75 kD TNF receptors (p55 and p75 TNF-R) are proteolytically cleaved to produce 30 and 40 kD soluble fragments, respectively. In this study, the enzymatic activity involved in the cleavage of human p75 TNF-R, named TNF-R releasing enzyme (TRRE), was identified in the culture supernatant of PMA-stimulated THP-1 cells using an activity assay system established by our group. When THP-1 cells were stimulated with PMA, TRRE was released rapidly into the supernatant, reaching maximal activity within 3 hours. The release of TRRE into the culture supernatant depended on tile concentration of PMA and FCS. TRRE activity was partially inhibited by chelating agents, suggesting that TRRE may be a metalloprotease-like enzyme. This is the first successful attempt to establish a stable TRRE source with a reliable assay system.

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