Tumor Necrosis Factor (TNF)-Soluble High-Affinity Receptor Complex as a TNF Antagonist

2007 ◽  
Vol 322 (2) ◽  
pp. 822-828 ◽  
Author(s):  
Sean D. McKenna ◽  
Georg Feger ◽  
Christie Kelton ◽  
Meijia Yang ◽  
Vittoria Ardissone ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Receptor Complex ◽  
High Affinity ◽  
Tnf Antagonist ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Necrosis Factor

scholarly journals Tumor Necrosis Factor (TNF) Receptor Superfamily Member TACI Is a High Affinity Receptor for TNF Family Members APRIL and BLyS

2000 ◽  
Vol 275 (45) ◽  
pp. 35478-35485 ◽  
Author(s):  
Youmei Wu ◽  
Dana Bressette ◽  
Jeff A. Carrell ◽  
Thomas Kaufman ◽  
Ping Feng ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Family Members ◽  
Tnf Receptor ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Necrosis Factor

scholarly journals Costimulation of mast cells by 4-1BB, a member of the tumor necrosis factor receptor superfamily, with the high-affinity IgE receptor

Blood ◽  
2005 ◽  
Vol 106 (13) ◽  
pp. 4241-4248 ◽  
Author(s):  
Hajime Nishimoto ◽  
Seung-Woo Lee ◽  
Hong Hong ◽  
Karen G. Potter ◽  
Mari Maeda-Yamamoto ◽  
...  
Keyword(s):  
Mast Cells ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Cytokine Production ◽  
Immunoglobulin E ◽  
Tumor Necrosis Factor Receptor ◽  
Protein Levels ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Necrosis Factor

Mast cells are the major effector-cell type for immediate hypersensitivity and other forms of allergic reactions. Expression of 4-1BB, a member of the tumor necrosis factor receptor superfamily, is induced at mRNA and protein levels on stimulation through the high-affinity receptor for immunoglobulin E (IgE; FcϵRI). In this study, we present evidence that agonistic anti-4-1BB antibodies can enhance FcϵRI-induced cytokine production and secretion. Consistent with this, 4-1BB-deficient mast cells exhibit reduced degranulation and cytokine production on FcϵRI stimulation. Analysis of 4-1BB ligand (4-1BBL)-deficient cells supported this notion. As a potential mechanism for these defects, we identified a defect in Ca2+ flux induced by FcϵRI stimulation. The defective Ca2+ flux could be accounted for by the reduced activity of Lyn/Btk/phospholipase C-γ2 pathway and constitutive interactions between 4-1BB and Lyn. Therefore, FcϵRI-inducible 4-1BB plays a costimulatory function together with FcϵRI stimulation.

Homodimeric Murine Interleukin-3 Agonists Indicate that Ligand Dimerization is Important for High-Affinity Receptor Complex Formation

1994 ◽  
Vol 10 (1) ◽  
pp. 17-27 ◽  
Author(s):  
Horst Müther ◽  
Klaus Kühlcke ◽  
André Gessner ◽  
Said Abdallah ◽  
Heinz Lother
Keyword(s):  
Complex Formation ◽  
Receptor Complex ◽  
Interleukin 3 ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor

scholarly journals Assembly and Regulation of the CD40 Receptor Complex in Human B Cells

1997 ◽  
Vol 186 (2) ◽  
pp. 337-342 ◽  
Author(s):  
Michelle R. Kuhné ◽  
Michael Robbins ◽  
John E. Hambor ◽  
Matthew F. Mackey ◽  
Yoko Kosaka ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
B Cells ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Receptor Complex ◽  
Tnf Receptor ◽  
B Cell Differentiation ◽  
Membrane Immunoglobulin ◽  
Human B Cells ◽  
Necrosis Factor

CD40 is a member of the tumor necrosis factor (TNF) receptor superfamily. Studies with human B cells show that the binding of CD154 (gp39, CD40L) to CD40 recruits TNF receptor– associated factor 2 (TRAF2) and TRAF3 to the receptor complex, induces the downregulation of the nonreceptor-associated TRAFs in the cell and induces an increased expression of Fas on the cell surface. Combined signaling through the interluekin 4 receptor and CD40 induces an increased expression of Fas with a commensurate increase in the level of TRAF2, but not TRAF3, that is recruited to the receptor complex. In contrast, engagement of the membrane immunoglobulin and CD40 limits Fas upregulation and reduces the recruitment of TRAF2, relative to TRAF3, to the CD40 receptor complex. These studies show that the TRAF composition of the CD40 receptor complex can be altered by signals that influence B cell differentiation.

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