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{"insert":{"user_id":"1000161700","type":"misc"},"similar_merge":{"see_also":[{"@id":"https://tokushima-u.repo.nii.ac.jp/records/2003104","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1050022708923184000/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=327259","label":"url"}],"paper_title":{"en":"The New Insight into Radicular Dentin Formation","ja":"教授就任総説 歯根象牙質形成を再考する"},"authors":{"en":[{"name":"Baba Otto"}],"ja":[{"name":"馬場 麻人"}]},"description":{"en":"Dentin is mineralized connective tissue, which consists of two parts, coronal dentincovered by enamel and radicular dentin by cementum. Although both parts are formed by odontoblasts, biophysical and biochemical properties are indeed different, which evoke the specific system for radicular dentin formation. One of the critical factor of radicular dentin formation is Hertwig's epithelial root sheath (HERS), which leads proliferation and differentiation of odontoblasts under the control of TGF-/BMP signaling, and the ablation or over-expression of constituent molecules showed the specific malformation of radicular dentin. Wnt/-catenin signaling is the other candidate of dentin formation which may regulate differently on crown and root formation. Fibroblast growth factor (FGF) 18 is possible downstream molecule of this signaling. Interestingly, the expression of FGF18 transcripts was detected during root formation, but not crown formation in rat mandibular molar.While possible receptors, FGFR2 and FGFR3, were continuously observed in both crown and root formation, those suggested that coronal and radicular dentin might be formed under the continuous and/or reciprocal control of different FGFs. The clarification of these systems may open new insight into the tissue regeneration and/or engineering of tooth and periodontium.","ja":"Dentin is mineralized connective tissue, which consists of two parts, coronal dentincovered by enamel and radicular dentin by cementum. Although both parts are formed by odontoblasts, biophysical and biochemical properties are indeed different, which evoke the specific system for radicular dentin formation. One of the critical factor of radicular dentin formation is Hertwig's epithelial root sheath (HERS), which leads proliferation and differentiation of odontoblasts under the control of TGF-/BMP signaling, and the ablation or over-expression of constituent molecules showed the specific malformation of radicular dentin. Wnt/-catenin signaling is the other candidate of dentin formation which may regulate differently on crown and root formation. Fibroblast growth factor (FGF) 18 is possible downstream molecule of this signaling. Interestingly, the expression of FGF18 transcripts was detected during root formation, but not crown formation in rat mandibular molar.While possible receptors, FGFR2 and FGFR3, were continuously observed in both crown and root formation, those suggested that coronal and radicular dentin might be formed under the continuous and/or reciprocal control of different FGFs. The clarification of these systems may open new insight into the tissue regeneration and/or engineering of tooth and periodontium."},"publication_date":"2016-06","publication_name":{"en":"Journal of Oral Health and Biosciences","ja":"Journal of Oral Health and Biosciences"},"volume":"29","number":"1","starting_page":"1","ending_page":"6","languages":["jpn"],"identifiers":{"issn":["2188-7888"]},"misc_type":"introduction_scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000161700","type":"misc"},"similar_merge":{"see_also":[{"@id":"https://cir.nii.ac.jp/crid/1570009750246749568/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=315642","label":"url"}],"paper_title":{"en":"硬組織構造生物 : Dentin sialoprotein(DSP)の歯周組織における発現","ja":"硬組織構造生物 : Dentin sialoprotein(DSP)の歯周組織における発現"},"authors":{"en":[{"name":"Baba Otto"}],"ja":[{"name":"馬場 麻人"}]},"publication_date":"2005-03","publication_name":{"en":"The Journal of the Stomatological Society, Japan","ja":"口腔病学会雑誌"},"volume":"71","number":"4","starting_page":"112","ending_page":"112","languages":["jpn"],"identifiers":{"issn":["0300-9149"]},"misc_type":"introduction_scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000161700","type":"misc","id":"49809750"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/15187031","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=308326","label":"url"}],"paper_title":{"en":"Post-translational modifications of sibling proteins and their roles in osteogenesis and dentinogenesis.","ja":"Post-translational modifications of sibling proteins and their roles in osteogenesis and dentinogenesis."},"authors":{"en":[{"name":"Qin C"},{"name":"Baba Otto"},{"name":"Butler W T"}],"ja":[{"name":"Qin C"},{"name":"馬場 麻人"},{"name":"Butler W T"}]},"description":{"en":"The extracellular matrix (ECM) of bone and dentin contains several non-collagenous proteins. One category of non-collagenous protein is termed the SIBLING (Small Integrin-Binding LIgand, N-linked Glycoprotein) family, that includes osteopontin (OPN), bone sialoprotein (BSP), dentin matrix protein 1 (DMP1), dentin sialophosphoprotein (DSPP), and matrix extracellular phosphoglycoprotein (MEPE). These polyanionic SIBLING proteins are believed to play key biological roles in the mineralization of bone and dentin. Although the specific mechanisms involved in controlling bone and dentin formation are still unknown, it is clear that some functions of the SIBLING family members are dependent on the nature and extent of post-translational modifications (PTMs), such as phosphorylation, glycosylation, and proteolytic processing, since these PTMs would have significant effects on their structure. OPN and BSP are present in the ECM of bone and dentin as full-length forms, whereas amino acid sequencing indicates that DMP1 and DSPP exist as proteolytically processed fragments that result from scission of X-Asp bonds. We hypothesized that the processing of DMP1 and DSPP is catalyzed by the PHEX enzyme, since this protein, an endopeptidase that is predominantly expressed in bone and tooth, has a strong preference for cleavage at the NH2-terminus of aspartyl residue. We envision that the proteolytic processing of DMP1 and DSPP may be an activation process that plays a significant, crucial role in osteogenesis and dentinogenesis, and that a failure in this processing would cause defective mineralization in bone and dentin, as observed in X-linked hypophosphatemic rickets.","ja":"The extracellular matrix (ECM) of bone and dentin contains several non-collagenous proteins. One category of non-collagenous protein is termed the SIBLING (Small Integrin-Binding LIgand, N-linked Glycoprotein) family, that includes osteopontin (OPN), bone sialoprotein (BSP), dentin matrix protein 1 (DMP1), dentin sialophosphoprotein (DSPP), and matrix extracellular phosphoglycoprotein (MEPE). These polyanionic SIBLING proteins are believed to play key biological roles in the mineralization of bone and dentin. Although the specific mechanisms involved in controlling bone and dentin formation are still unknown, it is clear that some functions of the SIBLING family members are dependent on the nature and extent of post-translational modifications (PTMs), such as phosphorylation, glycosylation, and proteolytic processing, since these PTMs would have significant effects on their structure. OPN and BSP are present in the ECM of bone and dentin as full-length forms, whereas amino acid sequencing indicates that DMP1 and DSPP exist as proteolytically processed fragments that result from scission of X-Asp bonds. We hypothesized that the processing of DMP1 and DSPP is catalyzed by the PHEX enzyme, since this protein, an endopeptidase that is predominantly expressed in bone and tooth, has a strong preference for cleavage at the NH2-terminus of aspartyl residue. We envision that the proteolytic processing of DMP1 and DSPP may be an activation process that plays a significant, crucial role in osteogenesis and dentinogenesis, and that a failure in this processing would cause defective mineralization in bone and dentin, as observed in X-linked hypophosphatemic rickets."},"publication_date":"2004-06-04","publication_name":{"en":"Critical Reviews in Oral Biology and Medicine","ja":"Critical Reviews in Oral Biology and Medicine"},"volume":"15","number":"3","starting_page":"126","ending_page":"136","languages":["eng"],"identifiers":{"issn":["1544-1113"]},"misc_type":"introduction_scientific_journal"},"priority":"input_data"}