期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 283, 期 49, 页码 34229-34240出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M803142200
关键词
-
资金
- National Institutes of Health [R01 DE10489, R21 AR052824]
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-beta 1 (TGF-beta 1), a potent growth factor abundant in bone, the effect of LOX on TGF-beta 1 signaling, and its potential mechanism. The specific binding between mature LOX and mature TGF-beta 1 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-beta 1-induced Smad3 phosphorylation likely through its amine oxidase activity. The data indicate that LOX binds to mature TGF-beta 1 and enzymatically regulates its signaling in bone and thus may play an important role in bone maintenance and remodeling.
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