Interleukin high-affinity receptor

C2. Caligiuri, M. A., Zmuidzinas, A., Manley, T. J., Levine, H., Smith, K. A., and Ritz, J. Functional consequences of interleukin-2 receptor expression on resting human lymphocytes. Identification of a novel natural killer cell subset with high affinity receptors. J. Exp. Med. 171, 1509-1526 (1990). 

M38. Mita, S., Tominaga, A., Hitoshi, Y., Sakamoto, K., Honjo, T., Akagi, M., Kikuchi, Y., Ya-maguchi, N., and Takatsu, K. Characterization of high-affinity receptors for interleukin-5 on interleukin-5-dependent cell lines. Proc. Nail. Acad. Sci. U.SA. 86, 2311-2315 (1989). 

Walter, M. R., Windsor, W. T., Nagabhushan, T. L., Lundell, D. J., Lunn, C. A., Zauodny, P. J., and Narula, S. K. (1995). Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor. Nature 376, 230-235. Wang, Y., Shen, B. J., and Sebald, W. (1997). A mixedhuman interleukin 4 dominates high-affinity interaction with the receptor alpha chain. fVoc. Natl. Acad. Sci. USA 94(5), 1657-1662. 

Teshigawara K, Wang HM, Kato K, Smith KA Interleukin 2 high-affinity receptor expression requires two distinct binding proteins. J Exp Med 1997 165 223-238. 

Denileukin diftitox is a combination of the active sections of interleukin 2 and diphtheria toxin. It binds to high-affinity interleukin 2 receptors on the cancer cell (and other cells), and the toxin portion of the molecule inhibits protein synthesis to result in cell death. The pharmacokinetics of denileukin diftitox are best described by a two-compartment model, with an a half-life of 2 to 5 minutes and a terminal half-life of 70 to 80 minutes. Denileukin diftitox is used for the treatment of persistent or recurrent cutaneous T-cell lymphoma whose cells express the CD25 receptor. Side effects include vascular leak syndrome, fevers/chills, hypersensitivity reactions, hypotension, anorexia, diarrhea, and nausea and vomiting. 

Suzuki H, Prado GN, Wilkinson N, Navarro J. The N terminus of interleukin-8 (IL-8) receptor confers high affinity binding to human IL-8. J Biol Chem 1994 269(28) 18263-18266. 

Lee J, Horuk R, Rice GC, Bennett GL, Camerato T, Wood WI. Characterization of two high affinity human interleukin-8 receptors. J Biol Chem 1992 267(23) 16283-16287. 

Pharmacology Daclizumab is an immunosuppressive, humanized IgGI monoclonal antibody produced by recombinant DNA technology that binds specifically to the alpha subunit (Tac subunit) of the human high-affinity interleukin-2 (IL-2) receptor that is expressed on the surface of activated lymphocytes. Daclizumab is a composite of human (90%) and murine (10%) antibody sequences. 

Clinical pharmacology Denileukin diftitox is a fusion protein designed to direct the cytocidal action of diphtheria toxin to cells that express the IL-2 receptor. It binds avidly to the high-affinity interleukin-2 receptor on target-cell surfaces, where it is... 

Hacein-Bey, H., M. Cavazzana-Calvo, F. Le Deist, A. Dautry-Varsat, C. Hivroz, I. Riviere, O. Danes, J.M. Heard, K. Sugamura, A. Fischer, and G. De Saint Basile, gamma-c gene transfer into SCID XI patients B-cell lines restores normal high-affinity interleukin-2 receptor expression and function. Blood, 1996. 87(8) 3108-16. 

Tavernier J, Devos R, Comelis S, Tuypens T, et al. 1991. A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CSF. Cell. 66 1175-1184. 

Denileukin Diftitox. Denileukin Diftitox (Ontak) is formulated by combining interleukin-2 with diphtheria toxin.11 Certain leukemia and lymphoma cells have a surface receptor that has a high affinity for interleukin-2, thus attracting this drug directly to these cells. Upon binding with tbe receptor, the diphtheria toxin component of the drug inhibits cellular protein synthesis, which ultimately results in cell death. This... 

Charge Pair in Human Interleukin 4 Dominates High-Affinity Interaction with the Receptor Alpha Chain. 

Yanofsky SD, Baldwin DN, Butler JH, et al., High affinity type I interleukin 1 receptor antagonists discovered by screening recombinant peptide libraries, Proc. Natl. Acad. Sci. USA, 93 7381-7386, 1996. 

Wang, Y., Shen, B. J., and Sebald, W. (1997). A mixed-charge pair in human interleukin 4 dominates high-affinity interaction with the receptor alpha chain. Proc. Natl. Acad. Sci. USA 94(5), 1657-1662. 

Ahuja, S. K., Lee, J. C., and Murphy, P. M. (1996). CXC chemokines bind to unique sets of selectivity determinants that can function independently and are broadly distributed on multiple domains of human interleukin-8 receptor B. Determinants of high affinity binding and receptor activation are distinct. J. Biol. Chem. 271, 225-232. 

The crystal structure of human interleukin-4 (IL-4) bound to the ectodomain of the a-chain of the IL-4 receptor has been solved.34 The IL-4 receptor is a t5y)e I receptor. The ligand, IL-4, binds first with high affinity to the receptor a-chain and then the inter-... 

---