Interleukin 2 high-affinity receptor expression requires two distinct binding proteins.
نویسندگان
چکیده
منابع مشابه
Interleukin 2 high-affinity receptor expression requires two distinct binding proteins
A cell line established from a patient with acute lymphoblastic leukemia was found to express IL-2 binding sites with a novel, intermediate affinity compared with the characteristic high-affinity IL-2-receptors and low-affinity IL-2 binding sites described previously. Clones were isolated from this cell line that displayed solely this new IL-2-binding protein, and were found to be unreactive wi...
متن کاملCharacterization of the Interleukin (IL)-6 Inhibitor IL-6-RFP: fused receptor domains act as high affinity cytokine-binding proteins.
Although fusion proteins of the extracellular parts of receptor subunits termed cytokine traps turned out to be promising cytokine inhibitors for anti-cytokine therapies, their mode of action has not been analyzed. We developed a fusion protein consisting of the ligand binding domains of the IL-6 receptor subunits IL-6Ralpha and gp130 that acts as a highly potent IL-6 inhibitor. Gp130 is a shar...
متن کاملHuman gastrin-releasing peptide receptor gene regulation requires transcription factor binding at two distinct CRE sites.
Ectopic expression of the gastrin-releasing peptide (GRP) receptor (GRP-R) occurs frequently in human malignancies of the gastrointestinal tract. Owing to paracrine and autocrine interaction with its specific high-affinity ligand GRP, tumor cell proliferation, migration, and invasion might ensue. Here we provide the first insights regarding molecular mechanisms of GRP-R regulation in gastrointe...
متن کاملPDGF-AB requires PDGF receptor alpha-subunits for high-affinity, but not for low-affinity, binding and signal transduction.
There are two PDGF receptor proteins (PDGFR alpha and PDGFR beta) which are proposed to function as subunits to form a high-affinity dimeric PDGF receptor. One aspect of this model about which there is still disagreement is whether PDGF-AB can bind to cells that express only PDGFR beta and, if so, whether PDGF-AB can act as an agonist or an antagonist. To address this question, we derived 3T3 c...
متن کاملInterleukin 2-induced activation of Ras requires two domains of interleukin 2 receptor beta subunit, the essential region for growth stimulation and Lck-binding domain.
Interleukin 2 (IL-2) can stimulate the proliferation of various kinds of T-cell lines. The receptor for IL-2 is composed of at least two subunits (alpha and beta), of which beta subunit plays the major role in transducing growth signals into the cells. A nonreceptor-type tyrosine kinase, Lck, is associated with IL-2 receptor beta subunit, and the binding of IL-2 to its receptor induces the acti...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Experimental Medicine
سال: 1987
ISSN: 0022-1007,1540-9538
DOI: 10.1084/jem.165.1.223