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10.1038/srep37885 http://scihub22266oqcxt.onion/10.1038/srep37885 C5121659!5121659 !27883077     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27883077 &cmd=llinks): Failed to open stream: HTTP request failed! 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TGF beta receptor II interacting protein-1, an intracellular protein has an extracellular role as a modulator of matrix mineralization |pdf=|usr=}}{{27883077 }} gab.com Text TGF beta receptor II interacting protein-1, an intracellular protein has an extracellular role as a modulator of matrix mineralization JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27883077 #FOAvip 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 K(D)?=?48??M. 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. Twit Text FOAVip TGF beta receptor II interacting protein-1, an intracellular protein has an extracellular role as a modulator of matrix mineralization ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27883077 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27883077 #FOAvip English Wikipedia <ref>{{Cite pmid|27883077 }}</ref> TGF beta receptor II interacting protein-1, an intracellular protein has an extracellular role as a modulator of matrix mineralization #MMPMID27883077 Ramachandran A ; Ravindran S ; Huang CC ; George A Sci Rep 2016[Nov]; 6 (ä): 37885 PMID27883077 show ga 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 K(D)?=?48??M. 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. |Animals [MESH] |Calcification, Physiologic/*physiology [MESH] |Calcium Phosphates/metabolism [MESH] |Cell Differentiation/genetics [MESH] |Cell Line [MESH] |Collagen Type I/metabolism [MESH] |Eukaryotic Initiation Factor-3/metabolism [MESH] |Eukaryotic Initiation Factors/genetics/*metabolism [MESH] |Exosomes/metabolism [MESH] |Extracellular Matrix/*physiology [MESH] |Humans [MESH] |Intracellular Signaling Peptides and Proteins/genetics/*metabolism [MESH] |Male [MESH] |Mice, Nude [MESH] |Osteoblasts/*metabolism/physiology [MESH] |Osteogenesis/genetics [MESH] |Rats [MESH]TGF beta receptor II interacting protein-1, an intracellular protein h(epmc).pdf DeepDyve Pubget Overpricing