Osteocalcin/fibronectin‐functionalized collagen matrices for bone tissue engineering
Source abstract
Abstract
Abstract Collagen is the most abundant protein found in the extracellular matrix and is widely used to build scaffolds for biomedical applications which are the result of its biocompatibility and biodegradability. In the present study, we constructed a rhOCN/FNIII9‐10 fusion protein and rhOCN/FNIII9‐10‐functionalized collagen matrices and investigated the potential value for bone tissue engineering. In vitro studies carried out with preosteoblastic MC3T3‐E1 cells showed that rhOCN/FNIII9‐10 fusion protein promoted cell adhesion and the mRNA levels of osteogenic markers including osteocalcin, runt‐related transcription factor 2, alkaline phosphatase (ALP), and collagen type I. In addition, rhOCN/FNIII9‐10‐functionalized collagen matrices showed significant induction of the ALP activity more than rhFNIII9‐10‐functionalized collagen matrices or collagen matrices alone. These results suggested that rhOCN/FNIII9‐10‐functionalized collagen matrices have potential for bone tissue engineering. © 2014 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 103A: 2133–2140, 2015.
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Research context
OpenAlex topics: Cellular Mechanics and Interactions · Bone Tissue Engineering Materials · 3D Printing in Biomedical Research
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Biochemistry Inha University School of Medicine Incheon 400‐712 Republic of Korea
Funding
National Research Foundation Korea
References (49)
Show source-provided references
1. 10.1074/jbc.271.43.2688410.1074/jbc.271.43.26884 ↗
2. 10.1083/jcb.54.3.62610.1083/jcb.54.3.626 ↗
3. 10.1073/pnas.76.3.127410.1073/pnas.76.3.1274 ↗
4. 10.1083/jcb.124.4.40110.1083/jcb.124.4.401 ↗
5. 10.1016/j.cell.2007.08.00610.1016/j.cell.2007.08.006 ↗
6. 10.1097/MOH.0b013e3282fcc32110.1097/MOH.0b013e3282fcc321 ↗
7. 10.1016/j.yexcr.2009.09.02110.1016/j.yexcr.2009.09.021 ↗
8. 10.1089/ten.tea.2010.031610.1089/ten.tea.2010.0316 ↗
9. 10.1016/j.yexcr.2012.10.00510.1016/j.yexcr.2012.10.005 ↗
10. 10.1002/jbm.a.3468910.1002/jbm.a.34689 ↗
11. 10.1073/pnas.81.19.598510.1073/pnas.81.19.5985 ↗
12. 10.1016/j.biomaterials.2012.06.09510.1016/j.biomaterials.2012.06.095 ↗
13. 10.1242/dev.08905210.1242/dev.089052 ↗
14. 10.1242/jcs.0005910.1242/jcs.00059 ↗
15. 10.3748/wjg.v17.i20.248210.3748/wjg.v17.i20.2482 ↗
16. 10.1016/j.matbio.2005.06.00810.1016/j.matbio.2005.06.008 ↗
17. 10.1016/0092-8674(92)90600-H10.1016/0092-8674(92)90600-H ↗
18. Characterization of regions of fibronectin besides the arginine‐glycine‐aspartic acid sequence required for adhesive function of the cell‐binding domain using site‐directed mutagenesis10.1016/S0021-9258(18)98498-X ↗
19. 10.1007/s10529-009-0111-510.1007/s10529-009-0111-5 ↗
20. 10.1023/B:BILE.0000004393.02839.d810.1023/B:BILE.0000004393.02839.d8 ↗
21. Collagenous and non‐collagenous biochemical markers of bone metastases from prostate cancer
22. 10.1073/pnas.73.5.144710.1073/pnas.73.5.1447 ↗
23. 10.1002/j.1460-2075.1986.tb04440.x10.1002/j.1460-2075.1986.tb04440.x ↗
24. 10.1016/S8756-3282(98)00092-110.1016/S8756-3282(98)00092-1 ↗
25. 10.1038/382448a010.1038/382448a0 ↗
26. 10.1002/jbmr.565005010410.1002/jbmr.5650050104 ↗
27. 10.1038/ncomms272010.1038/ncomms2720 ↗
28. 10.1038/nrm185810.1038/nrm1858 ↗
29. 10.1038/nrm259210.1038/nrm2592 ↗
30. 10.1146/annurev.cellbio.042308.11331810.1146/annurev.cellbio.042308.113318 ↗
31. 10.1038/nbt105510.1038/nbt1055 ↗
32. 10.1126/science.117164310.1126/science.1171643 ↗
33. 10.1038/nmat273210.1038/nmat2732 ↗
34. 10.1038/eye.1988.2810.1038/eye.1988.28 ↗
35. 10.1097/MOH.0b013e3282fcc32110.1097/MOH.0b013e3282fcc321 ↗
36. 10.1007/s10555-008-9178-z10.1007/s10555-008-9178-z ↗
37. 10.1023/A:102342702681810.1023/A:1023427026818 ↗
38. 10.1096/fasebj.3.9.266358110.1096/fasebj.3.9.2663581 ↗
39. 10.1016/j.pep.2012.10.00410.1016/j.pep.2012.10.004 ↗
40. 10.1016/j.pep.2011.02.01310.1016/j.pep.2011.02.013 ↗
41. 10.1128/AEM.00119-1110.1128/AEM.00119-11 ↗
42. 10.1007/s10529-011-0812-410.1007/s10529-011-0812-4 ↗
43. 10.1016/j.pep.2012.03.00510.1016/j.pep.2012.03.005 ↗
44. 10.1002/jbm.a.3165010.1002/jbm.a.31650 ↗
45. 10.1016/B978-012470862-4/50005-210.1016/B978-012470862-4/50005-2 ↗
46. 10.1002/jbmr.565008131210.1002/jbmr.5650081312 ↗
47. 10.3109/0300820010901424610.3109/03008200109014246 ↗
48. 10.1359/jbmr.1998.13.5.82810.1359/jbmr.1998.13.5.828 ↗
49. 10.1002/jbmr.50910.1002/jbmr.509 ↗