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.
Published Web Locationhttps://doi.org/10.1006/bbrc.1996.0738
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.
Many UC-authored scholarly publications are freely available on this site because of the UC Academic Senate's Open Access Policy. Let us know how this access is important for you.