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Updated: May 25, 2026

Accessing the Cytotoxicity and Cell Response to Biomaterials
Published on: July 8, 2021
Localization of transforming growth factor beta receptor II interacting protein-1 in bone and teeth: implications in
Amsaveni Ramachandran1, Sriram Ravindran, Anne George
1Brodie Tooth Development Genetics & Regenerative Medicine Research Laboratory, Department of Oral Biology, University of Illinois at Chicago, Chicago, Illinois, USA.
Abstract:
Transforming growth factor beta receptor II (TGFβR-II) interacting protein 1 (TRIP-1) is a WD-40 protein that binds to the cytoplasmic domain of the TGF-β 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.
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