IL-1 and transforming growth factor-beta inhibit platelet-derived growth factor-AA binding to osteoblastic cells by reducing platelet-derived growth factor-alpha receptor expression.
J Immunol
; 150(12): 5625-32, 1993 Jun 15.
Article
en En
| MEDLINE
| ID: mdl-8515080
ABSTRACT
Platelet-derived growth factor (PDGF) is thought to play a significant role in bone repair and regeneration. We previously demonstrated that PDGF-AA-induced chemotaxis and proliferation can be modulated by IL-1. We now report that IL-1 and transforming growth factor-beta (TGF-beta) significantly decrease the number of PDGF-AA binding sites in both normal and tumor-derived human osteoblastic cells, whereas PDGF-BB binding is minimally affected. The affinity of PDGF-AA binding remains unchanged in the presence of IL-1, but is slightly reduced by TGF-beta as demonstrated by Scatchard analysis. We also showed that tyrosyl kinase phosphorylation after PDGF-AA binding is decreased in the presence of both IL-1 and TGF-beta. Northern blot analysis indicates that both IL-1 and TGF-beta decrease the expression of PDGF-alpha receptor mRNA. These results suggest that IL-1 and TGF-beta have the potential to regulate PDGF-AA-induced biologic activity in normal human osteoblastic cells and in human osteoblastic sarcoma cells by decreasing the levels of the PDGF-alpha receptor.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Osteoblastos
/
Factor de Crecimiento Derivado de Plaquetas
/
Factor de Crecimiento Transformador beta
/
Interleucina-1
/
Receptores del Factor de Crecimiento Derivado de Plaquetas
Límite:
Humans
Idioma:
En
Revista:
J Immunol
Año:
1993
Tipo del documento:
Article
País de afiliación:
Marruecos