Research Project
Grant-in-Aid for Research Activity Start-up
We fractionated DPP and DSP along with TGF-b-like activity by ion exchange (IE) chromatography from developing pig molars and measured their alkaline phosphatase (ALP) stimulating activity in human periodontal (HPDL) cells with or without TGF-b receptor inhibitor. We then purified TGF-b-unbound or -bound DPP and DSP by reverse phase high performance liquid chromatography (RP-HPLC) using ALP-HPDL system. The TGF-b isoform bound to DPP and DSP was identified as being TGF-b1 by ELISA and LC-MS/MS analysis. We incubated carrier-free human recombinant TGF-b1 (CF-hTGF-b1) with TGF-b-unbound DPP or DSP and characterized the binding on IE-HPLC using the ALP-HPDL system. DPP and DSP rescued the loss of TGF-b1 activity. Approximately 19% and 10% of the ALP stimulating activities were retained by the binding of TGF-b1 to DPP and DSP, respectively. The type I collagen infrequently bound to CF-hTGFb1. We conclude that both DPP and DSP help retain TGF-b1 activity in porcine dentin.
All 2014 2013 Other
All Journal Article (4 results) (of which Peer Reviewed: 4 results) Presentation (7 results) (of which Invited: 1 results) Book (1 results)
Journal of Dental Research
Volume: 93巻 Pages: 671-677
Volume: -
Archives of Oral Biology
Volume: 58巻 Pages: 1569-1577
Volume: 58 Issue: 11 Pages: 1569-1577
10.1016/j.archoralbio.2013.08.005
