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
1994 ◽  
Vol 10 (1) ◽  
pp. 17-27 ◽  
Author(s):  
Horst Müther ◽  
Klaus Kühlcke ◽  
André Gessner ◽  
Said Abdallah ◽  
Heinz Lother

2007 ◽  
Vol 322 (2) ◽  
pp. 822-828 ◽  
Author(s):  
Sean D. McKenna ◽  
Georg Feger ◽  
Christie Kelton ◽  
Meijia Yang ◽  
Vittoria Ardissone ◽  
...  

2010 ◽  
Vol 48 (1-3) ◽  
pp. 128-136 ◽  
Author(s):  
Amir Rashid ◽  
Marco W. Iodice ◽  
Kathleen M. Carroll ◽  
Jonathan E.M. Housden ◽  
Michael Hunter ◽  
...  

1988 ◽  
Vol 168 (5) ◽  
pp. 1923-1928 ◽  
Author(s):  
M R Fung ◽  
G Ju ◽  
W C Greene

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.


Sign in / Sign up

Export Citation Format

Share Document