Leptin receptor (OB-R) oligomerizes with itself but not with its closely related cytokine signal transducer gp130.
FEBS Lett
; 403(1): 79-82, 1997 Feb 10.
Article
en En
| MEDLINE
| ID: mdl-9038364
ABSTRACT
Leptin (OB) exerts weight-reducing effects in mice. The structure of the receptor for this factor, OB-R, is considerably similar to those of gp130, the common signal transducing receptor component for the interleukin-6 (IL-6) family of cytokines, and leukemia inhibitory factor receptor (LIFR). Since the IL-6 family of cytokines signal through gp130 homodimer or gp130/LIFR heterodimer, we have examined in this study the possible involvement of gp130 and LIFR in leptin signaling through OB-R. Leptin stimulation induces tyrosine phosphorylation of neither gp130 nor LIFR, while LIF stimulation does both. As examined by using two differently epitope-tagged OB-R molecules, the spontaneous homo-oligomerization of OB-R has been elucidated. Ba/F3 cells, which do not express gp130, are non-responsive to leptin and exhibit increased DNA synthesis in response to leptin after transfection of OB-R cDNA alone. OB-R appears to transduce the signal via its homo-oligomerization without interaction with gp130 or LIFR.
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Bases de datos:
MEDLINE
Asunto principal:
Glicoproteínas de Membrana
/
Proteínas Portadoras
/
Antígenos CD
/
Linfocinas
/
Interleucina-6
/
Receptores de Citocinas
/
Receptores de Superficie Celular
/
Inhibidores de Crecimiento
Idioma:
En
Revista:
FEBS Lett
Año:
1997
Tipo del documento:
Article
País de afiliación:
Japón