Identification of the effector domain of biglycan that facilitates BMP-2 osteogenic function
| dc.creator | Jongwattanapisan, P | |
| dc.creator | Terajima, M | |
| dc.creator | Miguez, PA | |
| dc.creator | Querido, W | |
| dc.creator | Nagaoka, H | |
| dc.creator | Sumida, N | |
| dc.creator | Gurysh, EG | |
| dc.creator | Ainslie, KM | |
| dc.creator | Pleshko, N | |
| dc.creator | Perera, L | |
| dc.creator | Yamauchi, M | |
| dc.date.accessioned | 2021-01-14T17:16:29Z | |
| dc.date.available | 2021-01-14T17:16:29Z | |
| dc.date.issued | 2018-12-01 | |
| dc.identifier.issn | 2045-2322 | |
| dc.identifier.issn | 2045-2322 | |
| dc.identifier.doi | http://dx.doi.org/10.34944/dspace/4652 | |
| dc.identifier.other | 29728612 (pubmed) | |
| dc.identifier.uri | http://hdl.handle.net/20.500.12613/4670 | |
| dc.description.abstract | © 2018 The Author(s). 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. | |
| dc.format.extent | 7022- | |
| dc.language.iso | en | |
| dc.relation.haspart | Scientific Reports | |
| dc.relation.isreferencedby | Springer Science and Business Media LLC | |
| dc.rights | CC BY | |
| dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
| dc.subject | Animals | |
| dc.subject | Biglycan | |
| dc.subject | Bone Morphogenetic Protein 2 | |
| dc.subject | Calcification, Physiologic | |
| dc.subject | Cell Line | |
| dc.subject | Cells, Cultured | |
| dc.subject | Mice | |
| dc.subject | Models, Molecular | |
| dc.subject | Osteogenesis | |
| dc.subject | Peptides | |
| dc.subject | Protein Binding | |
| dc.subject | Protein Conformation | |
| dc.subject | Protein Interaction Domains and Motifs | |
| dc.subject | Rats | |
| dc.subject | Recombinant Fusion Proteins | |
| dc.subject | Signal Transduction | |
| dc.subject | Spectroscopy, Fourier Transform Infrared | |
| dc.subject | Structure-Activity Relationship | |
| dc.title | Identification of the effector domain of biglycan that facilitates BMP-2 osteogenic function | |
| dc.type | Article | |
| dc.type.genre | Journal Article | |
| dc.relation.doi | 10.1038/s41598-018-25279-x | |
| dc.ada.note | For Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu | |
| dc.creator.orcid | Pleshko, Nancy|0000-0001-8656-3936 | |
| dc.date.updated | 2021-01-14T17:16:25Z | |
| refterms.dateFOA | 2021-01-14T17:16:30Z |
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