First Author | Ramachandran A | Year | 2012 |
Journal | J Histochem Cytochem | Volume | 60 |
Issue | 4 | Pages | 323-37 |
PubMed ID | 22260994 | Mgi Jnum | J:196769 |
Mgi Id | MGI:5489865 | Doi | 10.1369/0022155412436879 |
Citation | Ramachandran A, et al. (2012) Localization of transforming growth factor beta receptor II interacting protein-1 in bone and teeth: implications in matrix mineralization. J Histochem Cytochem 60(4):323-37 |
abstractText | Transforming growth factor beta receptor II (TGFbetaR-II) interacting protein 1 (TRIP-1) is a WD-40 protein that binds to the cytoplasmic domain of the TGF-beta type II receptor in a kinase-dependent manner. To investigate the role of TRIP-1 in mineralized tissues, we examined its pattern of expression in cartilage, bone, and teeth and analyzed the relationship between TRIP-1 overexpression and mineralized matrix formation. Results demonstrate that TRIP-1 was predominantly expressed by osteoblasts, odontoblasts, and chondrocytes in these tissues. Interestingly, TRIP-1 was also localized in the extracellular matrix of bone and at the mineralization front in dentin, suggesting that TRIP-1 is secreted by nonclassical secretory mechanisms, as it is devoid of a signal peptide. In vitro nucleation studies demonstrate a role for TRIP-1 in nucleating calcium phosphate polymorphs. Overexpression of TRIP-1 favored osteoblast differentiation of undifferentiated mesenchymal cells with an increase in mineralized matrix formation. These data indicate an unexpected role for TRIP-1 during development of bone, teeth, and cartilage. |