关于SP-D:
Surfactant Pulmonary-Associated Protein D (SP-D) is a 43 kDa member of the collectin family of innate immune modulators. Its principal components consist of a collagen-like region and a C-terminal carbohydrate recognition domain (CRD), a structure that places it in a subset of pattern recognition proteins termed defense collagens. SP-D is constitutively secreted by alveolar lining cells and epithelium associated with tubular structures and induced in cardiac smooth muscle and endothelial cells. It binds both secreted and transmembrane proteins that transduce its function. It binds human neutrophil defensins, modulating influenza anti-viral defense. It binds MD-2/LY96, a secreted protein that cooperates with Toll-like receptors (TLRs) in the response of macrophages to bacterial lipopolysaccharides (LPS) or cell wall components. It also binds macrophage CD14 and TLRs directly, blocking binding of LPS and down-regulating TNF-α secretion. SP-D binding of both SIRPα and the calreticulin/CD91 complex on macrophages allows for a graded response to environmental challenge.
关于TNFRSF10B:
Mouse tumor necrosis factor receptor superfamily member 10B (TNFRSF10B) is a member of the TNFR family which contains 1 death domain and 3 TNFR-Cys repeats. TNFRSF10B exhibits high structural and functional homology to TRAIL-R1 (DR-4). TNFRSF10B is highly expressed in heart, lung, lymphocytes, spleen and kidney. In addition, it is regulated by the tumor suppressor p53. TNFRSF10B is the receptor for the cytotoxic ligand TNFSF10/TRAIL. It promotes the activation of NF-kappa-B and is essential for ER stress-induced apoptosis. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases mediating apoptosis.