Bodmer J L, Burns K, Schneider P, Hofmann K, Steiner V, Thome M, Bornand T, Hahne M, Schröter M, Becker K, Wilson A, French L E, Browning J L, MacDonald H R, Tschopp J
Institute of Biochemistry, University of Lausanne, Switzerland.
Immunity. 1997 Jan;6(1):79-88. doi: 10.1016/s1074-7613(00)80244-7.
A novel member of the tumor necrosis factor (TNF) receptor family, designated TRAMP, has been identified. The structural organization of the 393 amino acid long human TRAMP is most homologous to TNF receptor 1. TRAMP is abundantly expressed on thymocytes and lymphocytes. Its extracellular domain is composed of four cysteine-rich domains, and the cytoplasmic region contains a death domain known to signal apoptosis. Overexpression of TRAMP leads to two major responses, NF-kappaB activation and apoptosis. TRAMP-induced cell death is inhibited by an inhibitor of ICE-like proteases, but not by Bcl-2. In addition, TRAMP does not appear to interact with any of the known apoptosis-inducing ligands of the TNF family.
已鉴定出肿瘤坏死因子(TNF)受体家族的一个新成员,命名为TRAMP。393个氨基酸长的人TRAMP的结构组织与TNF受体1最为同源。TRAMP在胸腺细胞和淋巴细胞上大量表达。其细胞外结构域由四个富含半胱氨酸的结构域组成,细胞质区域含有已知可发出凋亡信号的死亡结构域。TRAMP的过表达导致两种主要反应,即NF-κB激活和凋亡。TRAMP诱导的细胞死亡被ICE样蛋白酶抑制剂抑制,但不受Bcl-2抑制。此外,TRAMP似乎不与TNF家族任何已知的凋亡诱导配体相互作用。