Periodontium consists of gingiva, alveolar mucosa, alveolar bone, cementum and periodontal ligament (PDL). PERIOSTIN, which is expressed in fibroblastic cells in PDL and in osteoblastic cells on the alveolar bone surface, is a key extracellular matrix protein that maintains homeostasis of periodontal tissue. During the process for FAM20C protein purification, we discovered that PERIOSTIN is co-purified with FAM20C. Immunolocalization of both FAM20C and PERIOSTIN were observed in the PDL extracellular matrix of murine periodontal tissues. PERIOSTIN bound with FAM20C in vitro. We further identified the binding domain of FAM20C in PERIOSTIN, which mapped within Fasciclin (FAS) I domain 1-4 (RD 1-4) of PERIOSTIN. PERIOSTIN has four conserved S-X-E motifs in both human and mouse FAS domain, which allowed us to use the murine model determine whether PERIOSTIN is phosphorylated by FAM20C and whether this phosphorylation might contribute to the integrity of periodontium tissues. / 2019-04-12T00:00:00Z
| Identifer | oai:union.ndltd.org:bu.edu/oai:open.bu.edu:2144/21970 |
| Date | 12 April 2017 |
| Creators | Lin, Ju-hsien |
| Source Sets | Boston University |
| Language | en_US |
| Detected Language | English |
| Type | Thesis/Dissertation |
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