Journal
JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY
Volume 60, Issue 4, Pages 323-337Publisher
SAGE PUBLICATIONS LTD
DOI: 10.1369/0022155412436879
Keywords
bone histology; cellular localization; chondrocyte; dental tissues; extracellular matrix
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Funding
- National Institutes of Health [DE 11657]
- Brodie Endowment Fund
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Transforming growth factor beta receptor II (TGF beta R-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. (J Histochem Cytochem 60:323-337,2012)
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