scholarly journals Solution assembly of the pseudo-high affinity and intermediate affinity interleukin-2 receptor complexes

2008 ◽  
Vol 8 (3) ◽  
pp. 482-489 ◽  
Author(s):  
Zining Wu ◽  
Byron Goldstein ◽  
Thomas M. Laue ◽  
Stefano F. Liparoto ◽  
Michael J. Nemeth ◽  
...  
Keyword(s):  
Interleukin 2 ◽  
Receptor Complexes ◽  
High Affinity ◽  
Interleukin 2 Receptor

scholarly journals Interleukin 2 receptor-targeted cytotoxicity. Interleukin 2 receptor-mediated action of a diphtheria toxin-related interleukin 2 fusion protein.

1988 ◽  
Vol 167 (2) ◽  
pp. 612-622 ◽  
Author(s):  
P Bacha ◽  
D P Williams ◽  
C Waters ◽  
J M Williams ◽  
J R Murphy ◽  
...  
Keyword(s):  
T Cells ◽  
Protein Synthesis ◽  
T Cell ◽  
Diphtheria Toxin ◽  
Interleukin 2 ◽  
Elongation Factor ◽  
High Affinity ◽  
Interleukin 2 Receptor ◽  
Human T Cell ◽  
Inhibition Of Protein Synthesis

The IL-2 toxin-mediated inhibition of protein synthesis in high affinity IL-2-R-positive murine and human T cell lines has been examined. Both excess free IL-2 and mAb to the Tac epitope of the p55 subunit of IL-2-R are shown to block the action of IL-2 toxin; whereas, agents that interact with other receptors or antigens on the T cell surface have no effect. We show that IL-2 toxin, like diphtheria toxin, must pass through an acidic vesicle in order to intoxicate target T cells. Finally, we demonstrate that the IL-2 toxin-mediated inhibition of protein synthesis in both human and murine T cells that bear the high affinity IL-2-R is due to the classic diphtheria toxin fragment A-catalyzed ADP ribosylation of elongation factor 2.

Stepwise formation of the high-affinity complex of the interleukin 2 receptor

1990 ◽  
Vol 2 (12) ◽  
pp. 1167-1177 ◽  
Author(s):  
Yuji Saito ◽  
Toshihiko Ogura ◽  
Masanori Kamio ◽  
Hisataka Sabe ◽  
Takashi Uchiyama ◽  
...  
Keyword(s):  
Interleukin 2 ◽  
High Affinity ◽  
Interleukin 2 Receptor ◽  
Stepwise Formation

Kinetic study of interleukin-2 binding on the reconstituted interleukin-2 receptor complexes including the human γ chain

1993 ◽  
Vol 23 (10) ◽  
pp. 2472-2476 ◽  
Author(s):  
Mitsuo Matsuoka ◽  
Toshikazu Takeshita ◽  
Naoto Ishii ◽  
Masataka Nakamura ◽  
Takao Ohkubo ◽  
...  
Keyword(s):  
Kinetic Study ◽  
Interleukin 2 ◽  
Receptor Complexes ◽  
Interleukin 2 Receptor

scholarly journals An α-Helical Signal in the Cytosolic Domain of the Interleukin 2 Receptor β Chain Mediates Sorting Towards Degradation after Endocytosis

1997 ◽  
Vol 136 (3) ◽  
pp. 583-595 ◽  
Author(s):  
Agathe Subtil ◽  
Muriel Delepierre ◽  
Alice Dautry-Varsat
Keyword(s):  
Amino Acid ◽  
Interleukin 2 ◽  
Sorting Signal ◽  
Receptor Complexes ◽  
High Affinity ◽  
Cytosolic Domain ◽  
Α Helix ◽  
Endocytic Compartments ◽  
Β Chain ◽  
Amino Acid Segment

High-affinity IL2 receptors consist of three components, the α, β, and γ chains that are associated in a noncovalent manner. Both the β and γ chains belong to the cytokine receptor superfamily. Interleukin 2 (IL2) binds to high-affinity receptors on the cell surface and IL2-receptor complexes are internalized. After endocytosis, the components of this multimolecular receptor have different intracellular fates: one of the chains, α, recycles to the plasma membrane, while the others, β and γ, are routed towards late endocytic compartments and are degraded. We show here that the cytosolic domain of the β chain contains a 10–amino acid sequence which codes for a sorting signal. When transferred to a normally recycling receptor, this sequence diverts it from recycling. The structure of a 17–amino acid segment of the β chain including this sequence has been studied by nuclear magnetic resonance and circular dichroism spectroscopy, which revealed that the 10 amino acids corresponding to the sorting signal form an amphipathic α helix. This work thus describes a novel, highly structured signal, which is sufficient for sorting towards degradation compartments after endocytosis.

Novel interleukin-2 receptor subunit detected by cross-linking under high-affinity conditions

Science ◽  
1986 ◽  
Vol 234 (4778) ◽  
pp. 859-863 ◽  
Author(s):  
M Sharon ◽  
R. Klausner ◽  
B. Cullen ◽  
R Chizzonite ◽  
W. Leonard
Keyword(s):  
Interleukin 2 ◽  
Cross Linking ◽  
Receptor Subunit ◽  
High Affinity ◽  
Interleukin 2 Receptor

scholarly journals A Chimera of Interleukin 2 and a Binding Variant of Aerolysin Is Selectively Toxic to Cells Displaying the Interleukin 2 Receptor

2007 ◽  
Vol 283 (3) ◽  
pp. 1572-1579 ◽  
Author(s):  
Milan Osusky ◽  
Lisa Teschke ◽  
Xiaoying Wang ◽  
Kevin Wong ◽  
J. Thomas Buckley
Keyword(s):  
Cell Death ◽  
Mammalian Cells ◽  
Therapeutic Agent ◽  
Interleukin 2 ◽  
Bacterial Toxin ◽  
Hybrid Protein ◽  
High Affinity ◽  
Interleukin 2 Receptor ◽  
Hybrid Molecules ◽  
N Terminus

Aerolysin is a bacterial toxin that binds to glycosylphosphatidylinositol-anchored proteins (GPI-AP) on mammalian cells and oligomerizes, inserting into the target membranes and forming channels that cause cell death. We have made a variant of aerolysin, R336A, that has greatly reduced the ability to bind to GPI-AP, and as a result it is only very weakly active. Fusion of interleukin 2 (IL2) to the N terminus of R336A-aerolysin results in a hybrid that has little or no activity against cells that do not have an IL2 receptor because it cannot bind to the GPI-AP on the cells. Strikingly, the presence of the IL2 moiety allows this hybrid to bind to cells displaying high affinity IL2 receptors. Once bound, the hybrid molecules form insertion-competent oligomers. Cell death occurs at picomolar concentrations of the hybrid, whereas the same cells are insensitive to much higher concentrations of R336A-aerolysin lacking the IL2 domain. The targeted channel-forming hybrid protein may have important advantages as a therapeutic agent.

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