| Autor: |
Harrop, J A, McDonnell, P C, Brigham-Burke, M, Lyn, S D, Minton, J, Tan, K B, Dede, K, Spampanato, J, Silverman, C, Hensley, P, DiPrinzio, R, Emery, J G, Deen, K, Eichman, C, Chabot-Fletcher, M, Truneh, A, Young, P R |
| Zdroj: |
Journal of Biological Chemistry; October 1998, Vol. 273 Issue: 42 p27548-56, 9p |
| Abstrakt: |
Herpesvirus entry mediator (HVEM), a member of the tumor necrosis factor (TNF) receptor family, mediates herpesvirus entry into cells during infection. Upon overexpression, HVEM activates NF-kappaB and AP-1 through a TNF receptor-associated factor (TRAF)-mediated mechanism. Using an HVEM-Fc fusion protein, we screened soluble forms of novel TNF-related proteins derived from an expressed sequence tag data base. One of these, which we designated HVEM-L, specifically bound to HVEM-Fc with an affinity of 44 nM. This association was confirmed with soluble and membrane forms of both receptor and ligand. HVEM-L mRNA is expressed in spleen, lymph nodes, macrophages, and T cells and encodes a 240-amino acid protein. A soluble, secreted form of the protein stimulates proliferation of T lymphocytes during allogeneic responses, inhibits HT-29 cell growth, and weakly stimulates NF-kappaB-dependent transcription. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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