{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,3]],"date-time":"2026-11-03T00:19:52Z","timestamp":1793665192389,"version":"4.5.1"},"reference-count":35,"publisher":"SAGE Publications","issue":"10","license":[{"start":{"date-parts":[[2022,6,9]],"date-time":"2022-06-09T00:00:00Z","timestamp":1654732800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"funder":[{"DOI":"10.13039\/100000072","name":"National Institute of Dental and Craniofacial Research","doi-asserted-by":"publisher","award":["F30DE030358"],"award-info":[{"award-number":["F30DE030358"]}],"id":[{"id":"10.13039\/100000072","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000072","name":"National Institute of Dental and Craniofacial Research","doi-asserted-by":"publisher","award":["R01DE027639"],"award-info":[{"award-number":["R01DE027639"]}],"id":[{"id":"10.13039\/100000072","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000072","name":"National Institute of Dental and Craniofacial Research","doi-asserted-by":"publisher","award":["T32DE014320"],"award-info":[{"award-number":["T32DE014320"]}],"id":[{"id":"10.13039\/100000072","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JSPS Research Fellowship for Japanese Biomedical"],"award-info":[{"award-number":["JSPS Research Fellowship for Japanese Biomedical"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000069","name":"National Institute of Arthritis and Musculoskeletal and Skin Diseases","doi-asserted-by":"publisher","award":["intramural funding to M.J. Somerman"],"award-info":[{"award-number":["intramural funding to M.J. Somerman"]}],"id":[{"id":"10.13039\/100000069","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["J Dent Res"],"published-print":{"date-parts":[[2022,9]]},"abstract":"<jats:p>\n                    Bone sialoprotein (gene: Ibsp; protein: BSP) is a multifunctional extracellular matrix protein present in bone, cementum, and dentin. Accumulating evidence supports BSP as a key regulator of mineralized tissue formation via evolutionarily conserved functional domains, including a C-terminal integrin-binding Arg-Gly-Asp (RGD) domain implicated in extracellular matrix\u2013cell signaling. Ablation of Ibsp in mice ( Ibsp\n                    <jats:sup>\u2212\/\u2212<\/jats:sup>\n                    ) results in impaired bone growth and mineralization and defective osteoclastogenesis, with effects in the craniofacial region including reduced acellular cementum formation, detachment of the periodontal ligament (PDL), alveolar bone hypomineralization, and severe periodontal breakdown. We hypothesized that BSP-RGD plays an important role in cementum and alveolar bone formation and mineralization, as well as periodontal function. This hypothesis was tested by replacing the RGD motif with a nonfunctional Lys-Ala-Glu (KAE) sequence in ( Ibsp\n                    <jats:sup>KAE\/KAE<\/jats:sup>\n                    ) mice and OCCM.30 murine ( Ibsp\n                    <jats:sup>KAE<\/jats:sup>\n                    ) cementoblasts. The RGD domain was not critical for acellular or cellular cementum formation in Ibsp\n                    <jats:sup>KAE\/KAE<\/jats:sup>\n                    mice. However, PDL volume and thickness were increased, and significantly more tartrate-resistant acid phosphatase\u2013positive osteoclasts were found on alveolar bone surfaces of Ibsp\n                    <jats:sup>KAE\/KAE<\/jats:sup>\n                    mice versus wild type mice. PDL organization was disrupted as indicated by picrosirius red stain, second harmonic generation imaging, dynamic mechanical analysis, and decreased asporin proteoglycan localization. In vitro studies implicated RGD functions in cell migration, adhesion, and mineralization, and this was confirmed by an ossicle implant model where cells lacking BSP-RGD showed substantial defects as compared with controls. In total, the BSP-RGD domain is implicated in periodontal development, though the scale and scope of changes indicated by in vitro studies indicate that other factors may partially compensate for and reduce the phenotypic severity of mice lacking BSP-RGD in vivo.\n                  <\/jats:p>","DOI":"10.1177\/00220345221100794","type":"journal-article","created":{"date-parts":[[2022,6,10]],"date-time":"2022-06-10T02:58:57Z","timestamp":1654829937000},"page":"1238-1247","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":29,"title":["The Bone Sialoprotein RGD Domain Modulates and Maintains Periodontal Development"],"prefix":"10.1177","volume":"101","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0528-4025","authenticated-orcid":false,"given":"K.","family":"Nagasaki","sequence":"first","affiliation":[{"name":"Laboratory of Oral Connective Tissue Biology, National Institute of Arthritis and Musculoskeletal and Skin 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