Effects of fish collagen peptides on collagen post-translational modifications and mineralization in an osteoblastic cell culture system
Source abstract
Abstract
Collagen is one of the most widely used biomaterials for tissue engineering and regenerative medicine. Fish collagen peptides (FCP) have been used as a dietary supplement, but their effects on the cellular function are still poorly understood. The objective of this study was to investigate the effects of FCP on collagen synthesis, quality and mineralization using an osteoblastic MC3T3-E1 cell culture system. Cells treated with FCP significantly upregulated the gene expression of several collagen modifying enzymes and more collagen was deposited in the cultures. Collagen in the treated group showed a greater extent of lysine hydroxylation, higher levels of hydroxylysine-aldehyde derived cross-links and accelerated cross-link maturation compared with the untreated group. Furthermore, the treated group showed accelerated matrix mineralization. These results indicate that FCP exerts a positive effect on osteoblastic cells in terms of collagen synthesis, quality and mineralization, thereby suggesting the potential utility of FCP for bone tissue engineering.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Collagen: Extraction and Characterization · Protein Hydrolysis and Bioactive Peptides · Silk-based biomaterials and applications
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (25)
Show source-provided references
1. 1) Ber S, Kose GT, Hasirci V. Bone tissue engineering on patterned collagen films: an in vitro study. Biomaterials 2005; 26: 1977-1986.10.1016/j.biomaterials.2004.07.007 ↗
2. 10.1007/s10047-007-0391-210.1007/s10047-007-0391-2 ↗
3. 10.1002/jbm.82027011110.1002/jbm.820270111 ↗
4. 10.1271/bbb.8064910.1271/bbb.80649 ↗
5. 10.1021/jf062834s10.1021/jf062834s ↗
6. 10.1271/bbb.10019310.1271/bbb.100193 ↗
7. 8) Yamauchi M. Collagen Biochemistry: an Overview. In: Phillips GO, editor. Advances in Tissue Banking, vol. 6. Singapore: World Scientific Publishing; 2002. p. 445-500.10.1142/9789812776976_0025 ↗
8. 9) Fernandes RJ, Harkey MA, Weis M, Askew JW, Eyre DR. The post-translational phenotype of collagen synthesized by SAOS-2 osteosarcoma cells. Bone 2007; 40: 1343-1351.10.1016/j.bone.2007.01.011 ↗
9. 10) Turecek C, Fratzl-Zelman N, Rumpler M, Buchinger B, Spitzer S, Zoehrer R, Durchschlag E, Klaushofer K, Paschalis EP, Varga F. Collagen cross-linking influences osteoblastic differentiation. Calcif Tissue Int 2008; 82: 392-400.10.1007/s00223-008-9136-3 ↗
10. 13) Rucker RB, Murray J. Cross-linking amino acids in collagen and elastin. Am J Clin Nutr 1978; 31: 1221-1236.10.1093/ajcn/31.7.1221 ↗
11. 14) Yamauchi M, Shiiba M. Lysine hydroxylation and crosslinking of collagen. Methods Mol Biol 2008; 446: 95-108.10.1007/978-1-60327-084-7_7 ↗
12. 16) Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987; 162: 156-159.10.1016/0003-2697(87)90021-2 ↗
13. 10.1006/meth.2001.126210.1006/meth.2001.1262 ↗
14. 10.1021/bi00365a02710.1021/bi00365a027 ↗
15. 10.1016/j.ab.2004.02.00210.1016/j.ab.2004.02.002 ↗
16. 10.1359/JBMR.05061210.1359/JBMR.050612 ↗
17. 23) Kim MM, Mendis E, Rajapakse N, Lee SH, Kim SK. Effect of spongin derived from Hymeniacidon sinapium on bone mineralization. J Biomed Mater Res Part B Appl Biomater 2009; 90: 540-546.10.1002/jbm.b.31315 ↗
18. 10.1016/S1096-7192(02)00036-710.1016/S1096-7192(02)00036-7 ↗
19. 10.1359/jbmr.1999.14.8.127210.1359/jbmr.1999.14.8.1272 ↗
20. 10.1359/JBMR.04032310.1359/JBMR.040323 ↗
21. 10.1359/JBMR.04102610.1359/JBMR.041026 ↗
22. 10.1016/S0945-053X(02)00071-910.1016/S0945-053X(02)00071-9 ↗
23. 31) Wang C, Kovanen V, Raudasoja P, Eskelinen S, Pospiech H, Myllyla R. The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability. J Cell Mol Med 2009; 13: 508-521.10.1111/j.1582-4934.2008.00286.x ↗
24. 32) Sricholpech M, Perdivara I, Yokoyama M, Nagaoka H, Terajima M, Tomer KB, Yamauchi M. Lysyl Hydroxylase 3-mediated glucosylation in type I collagen. Molecular loci and biological significance. J Biol Chem 2012; 287: 22998-23009.10.1074/jbc.M112.343954 ↗
25. 34) Eriksen HA, Sharp CA, Robins SP, Sassi ML, Risteli L, Risteli J. Differently cross-linked and uncross-linked carboxyterminal telopeptides of type I collagen in human mineralised bone. Bone 2004; 34: 720-727.10.1016/j.bone.2003.12.009 ↗