Refine
Has Fulltext
- yes (23)
Is part of the Bibliography
- yes (23)
Year of publication
Document Type
- Journal article (23)
Language
- English (23)
Keywords
- cancer (3)
- CML (2)
- association (2)
- management (2)
- 316L stainless-steel (1)
- BCR‐ABL (1)
- BRAF(V600E) mutation (1)
- Biochemie (1)
- Bullous pemphigoid (1)
- CD74 (1)
Institute
- Theodor-Boveri-Institut für Biowissenschaften (4)
- Abteilung für Funktionswerkstoffe der Medizin und der Zahnheilkunde (2)
- Klinik und Poliklinik für Allgemein-, Viszeral-, Gefäß- und Kinderchirurgie (Chirurgische Klinik I) (2)
- Klinik und Poliklinik für Anästhesiologie (ab 2004) (2)
- Klinik und Poliklinik für Dermatologie, Venerologie und Allergologie (2)
- Medizinische Klinik und Poliklinik I (2)
- Deutsches Zentrum für Herzinsuffizienz (DZHI) (1)
- Frauenklinik und Poliklinik (1)
- Institut für Anorganische Chemie (1)
- Institut für Experimentelle Biomedizin (1)
- Institut für Geographie (1)
- Institut für Klinische Transfusionsmedizin und Hämotherapie (1)
- Institut für Theoretische Physik und Astrophysik (1)
- Institut für Virologie und Immunbiologie (1)
- Institut für diagnostische und interventionelle Neuroradiologie (ehem. Abteilung für Neuroradiologie) (1)
- Klinik und Poliklinik für Hals-, Nasen- und Ohrenkrankheiten, plastische und ästhetische Operationen (1)
- Klinik und Poliklinik für Kinder- und Jugendpsychiatrie, Psychosomatik und Psychotherapie (1)
- Klinik und Poliklinik für Mund-, Kiefer- und Plastische Gesichtschirurgie (1)
- Klinik und Poliklinik für Nuklearmedizin (1)
- Klinik und Poliklinik für Psychiatrie, Psychosomatik und Psychotherapie (1)
- Pathologisches Institut (1)
- Rudolf-Virchow-Zentrum (1)
Interleukin 4 (IL-4) exerts a decisive role in the coord.ination of proteelive immune responses against parasites, particularly helminths. A disregulation of ll.r4 function is possibly involved in the genesis of allergic disease states. The search for important amino acid residues in human ll.r4 by mutational analysis of charged invariant amino acid positions identified two distinct functional sites in the 4-helix-bundle protein. Site 1 was marked by amino acid substitutions of the glutamic acid at position 9 in helix A and arginine at position 88 in helix C. Exchanges at both positions led to IL-4 variants deficient in binding to the extracellular domain of the ll.r4 receptor (IL-4ReJ. In parallel, up to 1000-fold increased concentrations of this type of variant were required to induce T -cell proliferation and B-eeil CD23 expression. Site 2 was marked by amino acid exchanges in helix D at positions 121, 124 and 125 (arginine, tyrosine and serine respectively in the wild-type).ß.A variants affected at site 2 exhibited partial agonist activity during T -cell proliferation; however, they still bound with high affinity to IL-4Rex. [The generation of an IL-4 antagonist by replacing tyrosine 124 with aspartic acid has been described before by Kruse et al. (1992) (EMBO }., 11, 3237-3244)]. These findings indicate that IL-4 functions by bind.ing IL-4Rex via site 1 which is constituted by residues on helices A and C. They further suggest that the association of a second, still undetined receptor protein with site 2 in helix D activates the receptor system and generates a transmembrane signal.