HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Dental Medicine / Faculty of Dental Medicine >
Peer-reviewed Journal Articles, etc >

Biochemical Mechanism of Titanium Fixation into Living Bone: Acid Soluble Phosphoproteins in Bone Binds with Titanium and Induced Endochondral Ossification in vivo

Files in This Item:
15_15_109.pdf871.95 kBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/79047

Title: Biochemical Mechanism of Titanium Fixation into Living Bone: Acid Soluble Phosphoproteins in Bone Binds with Titanium and Induced Endochondral Ossification in vivo
Authors: KUBOKI, Yoshinori Browse this author →KAKEN DB
YAGAMI, Kimitoshi Browse this author
TERADA-NAKAISHI, Michiko Browse this author
FURUSAWA, Toshitake Browse this author
NAKAOKI, Yasuko Browse this author
KURASAKI, Masaaki Browse this author →KAKEN DB
Keywords: Titanium implants
titanium-binding proteins
titanium- chromatography
phosphoproteins
phosvitin
bone phosphoproteins
Issue Date: 2017
Publisher: 日本再生歯科医学会
Journal Title: Journal of Oral Tissue Engineering
Volume: 15
Issue: 2
Start Page: 109
End Page: 118
Publisher DOI: 10.11223/jarde.15.109
Abstract: In 2014, we discovered that bone phosphoproteins, which are collectively called SIBULING family of proteins, are equipped with titanium-binding ability. Furthermore, the titanium implant devices which were coated with titanium-bound SIBLING induced more than 100 times faster bone formation of early stage when implanted into rat calvaria. These findings led us to an explanation why titanium implants could be fixed into living bone. Several other phosphoproteins including, phosvitin, caseins and phosphophoryn (a dentin phosphoprotein) were also found to bind with titanium by use of a chromatographic column packed with titanium beads. In this study we demonstrated that a typical phosphoprotein, phosvitin lost its titanium-binding ability in a time-dependent manner by the reaction with λ-protein phosphatase. The fact confirmed that certain specific phosphoserines λresidues in this protein were responsible for the titanium-protein interaction. For an additional confirmation of SIBLING-titanium interaction, we extracted bone and dentin proteins with a new and simple method of acidic condition and applied them to the chromatographic column packed with titanium beads. The results showed that definite portions of the acid soluble proteins from both bone and dentin were retained in the column. Electrophoretic analysis showed the retained fractions were Stains-all positive, indicating that both bone and dentin contain multiple phosphoproteins which have affinity with titanium. The titanium-bound fraction of acid extract was again coated on the titanium device and implanted into rat calvaria. After one week, histology showed that in addition to definite pattern of bone formation, process of endochondral ossification was clearly observed. In the control implant of uncoated titanium device, only collagenous tissues were observed, without any cartilage nor bone formation. Based upon these findings we reconfirmed that the core biochemical mechanisms underlying the strong bond between the titanium and living bone is based upon the interaction between the implanted titanium and multiple bone phosphoproteins in the host tissue.
Rights: 利用は著作権の範囲内に限られます
Type: article
URI: http://hdl.handle.net/2115/79047
Appears in Collections:環境科学院・地球環境科学研究院 (Graduate School of Environmental Science / Faculty of Environmental Earth Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
歯学院・歯学研究院 (Graduate School of Dental Medicine / Faculty of Dental Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 久保木 芳徳

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 

 - Hokkaido University