期刊
FEBS LETTERS
卷 583, 期 7, 页码 1141-1146出版社
WILEY
DOI: 10.1016/j.febslet.2009.02.040
关键词
Runx2; Matrix metalloproteinase-13; Collagenase-3; Cyclic adenosine mono phosphate; Parathyroid hormone
资金
- National Institutes of Health [DK 47420]
Matrix metalloproteinase-13 (MMP-13) plays a critical role in parathyroid hormone (PTH)-induced bone resorption. PTH acts via protein kinase A (PKA) to phosphorylate and stimulate the transactivation of Runx2 for MMP-13 promoter activation. We show here that PTH stimulated Runx2 phosphorylation in rat osteoblastic cells. Runx2 was phosphorylated on serine 28 and threonine 340 after 8-bromo cyclic adenosine mono phosphate (8-Br-cAMP) treatment. We further demonstrate that in the presence of 8-Br-cAMP, the wild-type Runx2 construct stimulated MMP-13 promoter activity, while the Runx2 construct having mutations at three phosphorylation sites (S28, S347 and T340) was unable to stimulate MMP-13 promoter activity. Thus, we have identified the Runx2 phosphorylation sites necessary for PKA stimulated MMP-13 promoter activation and this event may be critical for bone remodeling. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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