Intermolecular Cystine-Bonding of Murine Interleukin 2 Indicates that Ligand Dimerization is Important for the Formation of the High-Affinity Receptor Complex

1992 ◽  
Vol 7 (2) ◽  
pp. 117-129 ◽  
Author(s):  
Heinz Lother ◽  
Horst Müther ◽  
André Gessner ◽  
Said Abdallah ◽  
Klaus Küklhlcke
Keyword(s):  
Interleukin 2 ◽  
Receptor Complex ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor

scholarly journals Co-internalization of the p55 and p70 subunits of the high-affinity human interleukin 2 receptor. Evidence for a stable ternary receptor complex.

1988 ◽  
Vol 168 (5) ◽  
pp. 1923-1928 ◽  
Author(s):  
M R Fung ◽  
G Ju ◽  
W C Greene
Keyword(s):  
Binding Sites ◽  
Interleukin 2 ◽  
Affinity Binding ◽  
Receptor Complex ◽  
Homogeneous Population ◽  
High Affinity ◽  
Membrane Complex ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Receptor Assembly

The high-affinity IL-2-R complex is composed of at least two distinct IL-2-binding subunits, including p55 (Tac, IL-2-R alpha) and p70 (IL-2-R beta). Using a radiolabeled mAb specific for the p55 receptor subunit and cells expressing a homogeneous population of high-affinity binding sites, we demonstrate that p55 is co-internalized with p70 after IL-2 binding to the receptor complex. Endocytosis of p55 depends upon the presence of IL-2 in a form capable of effectively interacting with the p70 subunit. Whether IL-2 is required for high-affinity receptor assembly or triggering of the internalization of preassembled receptors remains unresolved. Together, these findings support the existence of a stable, high-affinity human IL-2-R membrane complex composed of at least the p55 and p70 receptor subunits and IL-2.

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

Reduced Secondary Cytokine Induction by BAY 50-4798, a High-Affinity Receptor-Specific Interleukin-2 Analog

2006 ◽  
Vol 26 (3) ◽  
pp. 171-178 ◽  
Author(s):  
Sonja Steppan ◽  
Michael R. Eckart ◽  
Krystyna Bajsarowicz ◽  
Lawrence R. Sternberg ◽  
Jeffrey M. Greve ◽  
...  
Keyword(s):  
Interleukin 2 ◽  
High Affinity ◽  
Cytokine Induction ◽  
High Affinity Receptor ◽  
Affinity Receptor

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

Structure, function, and regulation of the interleukin-2 receptor and identification of a novel immune activation gene

1990 ◽  
Vol 327 (1239) ◽  
pp. 187-192 ◽  
Keyword(s):  
Immune Activation ◽  
Interleukin 2 ◽  
Relative Molecular Mass ◽  
Activated T Cells ◽  
High Affinity ◽  
Significant Homology ◽  
High Affinity Receptor ◽  
A Subunit ◽  
Affinity Receptor ◽  
Β Chain

This chapter is divided into two sections, the first dealing with a novel immune activation gene, denoted Act -2. This gene encodes a secreted protein that may represent a new cytokine. The Act-2 protein shares significant homology with proteins in two related families of small secreted proteins. Act-2 is rapidly synthesized by activated T cells, B cells and monocytes. The second section deals with interleukin-2 receptors. These receptors are now known to be comprised of three distinct classes of receptors, formed by various combinations of two IL-2 binding proteins, the α and β chains. The low-affinity receptors contain α, but not β chains; the intermediate-affinity receptors contain β, but not α chains, and the high-affinity receptors contain both α and β chains. The β chain appears to be tyrosine phosphorylated. We discuss evidence for the existence of another protein of relative molecular mass 100 000, which appears to be a subunit of at least the high-affinity receptor.

Stoichiometry of the Interleukin-6 High Affinity Receptor Complex

2006 ◽  
Vol 762 (1) ◽  
pp. 471-473 ◽  
Author(s):  
L. D. WARD ◽  
G. J. HOWLETT ◽  
A. HAMMACHER ◽  
R. L. MORITZ ◽  
R. J. SIMPSON
Keyword(s):  
Interleukin 6 ◽  
Receptor Complex ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor

Assessing the role of Asp 194 in the transmembrane domains of the α-chain of the high-affinity receptor complex for immunoglobulin E in signal transduction

2010 ◽  
Vol 48 (1-3) ◽  
pp. 128-136 ◽  
Author(s):  
Amir Rashid ◽  
Marco W. Iodice ◽  
Kathleen M. Carroll ◽  
Jonathan E.M. Housden ◽  
Michael Hunter ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Immunoglobulin E ◽  
Transmembrane Domains ◽  
Receptor Complex ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Α Chain
Sign in / Sign up

Export Citation Format

Share Document