Characterization of interleukin-13 receptor in carcinoma cell lines and human blood cells and comparison with the interleukin-4 receptor.
J Recept Signal Transduct Res
; 15(7-8): 931-49, 1995.
Article
de En
| MEDLINE
| ID: mdl-8673724
ABSTRACT
The interleukin-13 receptor is characterized by ligand-binding and crosslinking studies and compared with the interleukin-4 receptor. Crosslinking of radio-labeled hIL-4 and hIL-13 to the receptors on human carcinoma and mast cell lines demonstrated a predominant subunit at 130 kDa with two other minor bands of lower molecular mass (75 kDa and 65 kDa) in autoradiography. All binding of 125I-IL-13 was specifically blocked when the carcinoma cell suspensions were incubated with an excess of unlabeled hIL-4. However, unlabeled hIL-13 was unable to completely displace 125I-hIL-4 from the 130 kDa protein. In addition, 125I-hIL-13 showed no binding to mouse fibroblast cells transfected with human 130 kDa hIL-4 receptor c-DNA. Using weighted nonlinear computer modeling of the data from several equilibrium binding studies with human mast cells, a model of two binding sites for IL-4 (Kd = 50 and 190 pmol/L) and one site for IL-13 (Kd = 100 pmol/L) fitted better than a one site model with a very high level of significance (F = 10.66, P < 0.0001). It can be concluded that human IL-4R and hIL-13R are similar but distinct. This conclusion is supported here for the first time by a strong statistical criterion.
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Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Antigènes CD
/
Récepteurs aux interleukines
Type d'étude:
Prognostic_studies
Limites:
Humans
Langue:
En
Journal:
J Recept Signal Transduct Res
Sujet du journal:
BIOQUIMICA
/
FISIOLOGIA
Année:
1995
Type de document:
Article