Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Selvamurugan N,Shimizu E,Lee M,Liu T,Li H,Partridge NCdoi
10.1016/j.febslet.2009.02.040subject
Has Abstractpub_date
2009-04-02 00:00:00pages
1141-6issue
7eissn
0014-5793issn
1873-3468pii
S0014-5793(09)00154-9journal_volume
583pub_type
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