Identification of the effector domain of biglycan that facilitates BMP-2 osteogenic function
Abstract We have reported that recombinant biglycan (BGN) core protein accelerates bone formation in vivo by enhancing bone morphogenetic protein (BMP)-2 function. The purpose of the present study was to identify the specific domain (“effector”) within the BGN core protein that facilitates BMP-2 ost...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2018-05-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-018-25279-x |
| _version_ | 1818423176542027776 |
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| author | Prapaporn Jongwattanapisan Masahiko Terajima Patricia A. Miguez William Querido Hideaki Nagaoka Noriko Sumida Elizabeth Grace Gurysh Kristy M. Ainslie Nancy Pleshko Lalith Perera Mitsuo Yamauchi |
| author_facet | Prapaporn Jongwattanapisan Masahiko Terajima Patricia A. Miguez William Querido Hideaki Nagaoka Noriko Sumida Elizabeth Grace Gurysh Kristy M. Ainslie Nancy Pleshko Lalith Perera Mitsuo Yamauchi |
| author_sort | Prapaporn Jongwattanapisan |
| collection | DOAJ |
| description | Abstract We have reported that recombinant biglycan (BGN) core protein accelerates bone formation in vivo by enhancing bone morphogenetic protein (BMP)-2 function. The purpose of the present study was to identify the specific domain (“effector”) within the BGN core protein that facilitates BMP-2 osteogenic function. Thus, we generated various recombinant and synthetic peptides corresponding to several domains of BGN, and tested their effects on BMP-2 functions in vitro. The results demonstrated that the leucine-rich repeats 2–3 domain (LRR2-3) of BGN significantly enhanced the BMP-2 induced Smad1/5/9 phosphorylation, osteogenic gene expression, and alkaline phosphatase activity in myogenic C2C12 cells. Furthermore, addition of LRR2-3 to osteoblastic MC3T3-E1 cells accelerated in vitro mineralization without compromising the quality of the mineral and matrix. These data indicate that LRR2-3 is, at least in part, responsible for BGN’s ability to enhance BMP-2 osteogenic function, and it could be useful for bone tissue regeneration. |
| first_indexed | 2024-12-14T13:37:59Z |
| format | Article |
| id | doaj.art-86b12ac6f51546d392392532a8bb8bf5 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-14T13:37:59Z |
| publishDate | 2018-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-86b12ac6f51546d392392532a8bb8bf52022-12-21T22:59:31ZengNature PortfolioScientific Reports2045-23222018-05-018111110.1038/s41598-018-25279-xIdentification of the effector domain of biglycan that facilitates BMP-2 osteogenic functionPrapaporn Jongwattanapisan0Masahiko Terajima1Patricia A. Miguez2William Querido3Hideaki Nagaoka4Noriko Sumida5Elizabeth Grace Gurysh6Kristy M. Ainslie7Nancy Pleshko8Lalith Perera9Mitsuo Yamauchi10Department of Veterinary Medicine, Faculty of Veterinary Science, Chulalongkorn UniversityOral and Craniofacial Health Sciences, School of Dentistry, University of North Carolina at Chapel HillDepartment of Operative Dentistry, Oral and Craniofacial Health Sciences, School of Dentistry, University of North Carolina at Chapel HillDepartment of Bioengineering, Temple UniversityOral and Craniofacial Health Sciences, School of Dentistry, University of North Carolina at Chapel HillOral and Craniofacial Health Sciences, School of Dentistry, University of North Carolina at Chapel HillDivision of Pharmacoengineering and Molecular Pharmaceutics, Eshelman School of Pharmacy, University of North Carolina at Chapel HillDivision of Pharmacoengineering and Molecular Pharmaceutics, Eshelman School of Pharmacy, University of North Carolina at Chapel HillDepartment of Bioengineering, Temple UniversityGenome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of HealthOral and Craniofacial Health Sciences, School of Dentistry, University of North Carolina at Chapel HillAbstract We have reported that recombinant biglycan (BGN) core protein accelerates bone formation in vivo by enhancing bone morphogenetic protein (BMP)-2 function. The purpose of the present study was to identify the specific domain (“effector”) within the BGN core protein that facilitates BMP-2 osteogenic function. Thus, we generated various recombinant and synthetic peptides corresponding to several domains of BGN, and tested their effects on BMP-2 functions in vitro. The results demonstrated that the leucine-rich repeats 2–3 domain (LRR2-3) of BGN significantly enhanced the BMP-2 induced Smad1/5/9 phosphorylation, osteogenic gene expression, and alkaline phosphatase activity in myogenic C2C12 cells. Furthermore, addition of LRR2-3 to osteoblastic MC3T3-E1 cells accelerated in vitro mineralization without compromising the quality of the mineral and matrix. These data indicate that LRR2-3 is, at least in part, responsible for BGN’s ability to enhance BMP-2 osteogenic function, and it could be useful for bone tissue regeneration.https://doi.org/10.1038/s41598-018-25279-x |
| spellingShingle | Prapaporn Jongwattanapisan Masahiko Terajima Patricia A. Miguez William Querido Hideaki Nagaoka Noriko Sumida Elizabeth Grace Gurysh Kristy M. Ainslie Nancy Pleshko Lalith Perera Mitsuo Yamauchi Identification of the effector domain of biglycan that facilitates BMP-2 osteogenic function Scientific Reports |
| title | Identification of the effector domain of biglycan that facilitates BMP-2 osteogenic function |
| title_full | Identification of the effector domain of biglycan that facilitates BMP-2 osteogenic function |
| title_fullStr | Identification of the effector domain of biglycan that facilitates BMP-2 osteogenic function |
| title_full_unstemmed | Identification of the effector domain of biglycan that facilitates BMP-2 osteogenic function |
| title_short | Identification of the effector domain of biglycan that facilitates BMP-2 osteogenic function |
| title_sort | identification of the effector domain of biglycan that facilitates bmp 2 osteogenic function |
| url | https://doi.org/10.1038/s41598-018-25279-x |
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