Lysyl oxidase binds transforming growth factor-beta and regulates its signaling via amine oxidase activity.
J Biol Chem
; 283(49): 34229-40, 2008 Dec 05.
Article
em En
| MEDLINE
| ID: mdl-18835815
ABSTRACT
Lysyl oxidase (LOX), an amine oxidase critical for the initiation of collagen and elastin cross-linking, has recently been shown to regulate cellular activities possibly by modulating the functions of growth factors. In this study, we investigated the interaction between LOX and transforming growth factor-beta1 (TGF-beta1), a potent growth factor abundant in bone, the effect of LOX on TGF-beta1 signaling, and its potential mechanism. The specific binding between mature LOX and mature TGF-beta1 was demonstrated by immunoprecipitation and glutathione S-transferase pulldown assay in vitro. Both proteins were colocalized in the extracellular matrix in an osteoblastic cell culture system, and the binding complex was identified in the mineral-associated fraction of bone matrix. Furthermore, LOX suppressed TGF-beta1-induced Smad3 phosphorylation likely through its amine oxidase activity. The data indicate that LOX binds to mature TGF-beta1 and enzymatically regulates its signaling in bone and thus may play an important role in bone maintenance and remodeling.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Regulação Enzimológica da Expressão Gênica
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Fator de Crescimento Transformador beta
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Amina Oxidase (contendo Cobre)
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Proteína-Lisina 6-Oxidase
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article