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http://purl.uniprot.org/citations/27883077http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27883077http://www.w3.org/2000/01/rdf-schema#comment"Transforming growth factor beta receptor II interacting protein 1 (TRIP-1), a predominantly intracellular protein is localized in the ECM of bone. TRIP-1 lacks a signal peptide, therefore, in this study, we provide evidence that intracellular TRIP-1 can be packaged and exported to the ECM via exosomes. Overexpression of TRIP-1 in MC3T3-E1 cells resulted in increased matrix mineralization during differentiation and knockdown resulted in reduced effects. In vivo function of TRIP-1 was studied by an implantation assay performed using TRIP-1 overexpressing and knockdown cells cultured in a 3-dimmensional scaffold. After 4 weeks, the subcutaneous tissues from TRIP-1 overexpressing cells showed higher calcium and phosphate deposits, arranged collagen fibrils and increased expression of Runx2 and alkaline phosphatase. Nucleation studies on demineralized and deproteinized dentin wafer is a powerful tool to determine the functional role of noncollagenous proteins in matrix mineralization. Using this system, we provide evidence that TRIP-1 binds to Type-I collagen and can promote mineralization. Surface plasmon resonance analysis demonstrated that TRIP-1 binds to collagen with KD = 48 μM. SEM and TEM analysis showed that TRIP-1 promoted the nucleation and growth of calcium phosphate mineral aggregates. Taken together, we provide mechanistic insights of this intracellular protein in matrix mineralization."xsd:string
http://purl.uniprot.org/citations/27883077http://purl.org/dc/terms/identifier"doi:10.1038/srep37885"xsd:string
http://purl.uniprot.org/citations/27883077http://purl.uniprot.org/core/author"Huang C.C."xsd:string
http://purl.uniprot.org/citations/27883077http://purl.uniprot.org/core/author"Ravindran S."xsd:string
http://purl.uniprot.org/citations/27883077http://purl.uniprot.org/core/author"Ramachandran A."xsd:string
http://purl.uniprot.org/citations/27883077http://purl.uniprot.org/core/author"George A."xsd:string
http://purl.uniprot.org/citations/27883077http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27883077http://purl.uniprot.org/core/name"Sci Rep"xsd:string
http://purl.uniprot.org/citations/27883077http://purl.uniprot.org/core/pages"37885"xsd:string
http://purl.uniprot.org/citations/27883077http://purl.uniprot.org/core/title"TGF beta receptor II interacting protein-1, an intracellular protein has an extracellular role as a modulator of matrix mineralization."xsd:string
http://purl.uniprot.org/citations/27883077http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/27883077http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27883077
http://purl.uniprot.org/citations/27883077http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27883077
http://purl.uniprot.org/uniprot/#_Q8BTM6-mappedCitation-27883077http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27883077
http://purl.uniprot.org/uniprot/#_Q9QZD9-mappedCitation-27883077http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27883077
http://purl.uniprot.org/uniprot/#_Q3T9Y8-mappedCitation-27883077http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27883077
http://purl.uniprot.org/uniprot/Q3T9Y8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/27883077
http://purl.uniprot.org/uniprot/Q9QZD9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/27883077
http://purl.uniprot.org/uniprot/Q8BTM6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/27883077