Hostname: page-component-78c5997874-8bhkd Total loading time: 0 Render date: 2024-11-19T11:49:38.275Z Has data issue: false hasContentIssue false
  • English
  • Français

Effects of Non-Collagenous Matrix Proteins, Fatty Acid Derivatives, Etc. on the Nucleation and Growth of Calcium Phosphate on Hydroxyapatite

Published online by Cambridge University Press:  15 February 2011

A. T.-C. Wong  and
J. T. Czernuszka
A. T.-C. Wong
Affiliation:
Department of Materials, University of Oxford, Oxford, U.K
J. T. Czernuszka
Affiliation:
Department of Materials, University of Oxford, Oxford, U.K
Get access

Abstract

The effects of various non-collagenous bone matrix bio-chemicals on the deposition of calcium phosphate on hydroxyapatite surfaces have been studied. Guanidine-HCI bone extract, guanidine-EDTA bone extract and phosphatidylserine all showed an overall inhibitory effect on calcification. Phosphoserine promoted secondary nucleation but hindered crystal growth. Serum albumin altered the lattice structure of the crystals, thus inducing a significant calcium deficiency. This structural change also resulted in a different fracture behaviour.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 252: Symposium T – Tissue-Inducing Biomaterials , 1991 , 49
Copyright
Copyright © Materials Research Society 1992

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1. Glimcher, M.J., Phil. Trans. R. Soc. Lond., B304, 479 (1984)Google Scholar
2. Boskey, A.L., J. Phys. Chem., 3, 1628 (1989)Google Scholar
3. Boskey, A.L., Maresca, M., Appel, J., Conn. Tissue Res., 21,171 (1989)CrossRefGoogle Scholar
4. Endo, A., Glimcher, M.J., Conn. Tissue Res., 21,179 (1989)CrossRefGoogle Scholar
5. Fujisawa, R., Kuboki, Y., Sasakl, S., Calcif. Tissue Int., 41, 44 (1987)Google Scholar
6. Hunter, G.K., Allen, B.L., Grynpas, M.D., Cheng, P.-T., Biochem. J., 22M, 463 (1985)Google Scholar
7. van Kemenade, M.J.J.M., de Bruyn, P.L., J. Coil. Interf. Sc., 129, 1 (1989)Google Scholar
8. Dalas, E., Koutsoukos, P.G., J. Chem. Soc. Faraday Trans. 1, 85, 2465 (1989)Google Scholar
9. Aoba, T., Moreno, E.C., J. Interf. Coll. Sc., 106, 110 (1985)Google Scholar
10. Boskey, A.L., Dick, B.L., Calcif. Tissue int., 49, 193 (1991)Google Scholar
11. Boskey, A L., Wians, F.H. Jr., Hauschka, P.V., Calcif. Tissue Int., 37, 57 (1985)Google Scholar
12. Aoba, T., Fukae, M., Tanabe, T., Shimizu, M., Moreno, E.C., Calcif. Tissue Int., 41, 281 (1987)Google Scholar
13. Amjad, Z., Langmuir, 3, 1063 (1987)CrossRefGoogle Scholar
14. Dalas, E., loannou, P.V., Koutsoukas, P.G., Langmulr, 5, 157 (1989)Google Scholar
15. Termine, J.D., Belcourt, A.B., Conn, K.M., Kleinman, H.D., J. Biol. Chem., 256,10403 (1981)Google Scholar
16. Termine, J.D., Eanes, E.D., Conn, K.M., Calcif. Tissue int., 31,247 (1980)Google Scholar
17. Blumenthal, N.C., Clin. Orthop. Relf Res., 24E, 279 (1989)Google Scholar
18. JCPDS X-ray diffraction peak files, 26–1056Google Scholar
19. Nancollas, G.H., LoRe, M., Perez, L., Richardson, C., Zawacki, S.J., The Anat. Rec., 224, 234 (1989)Google Scholar
20. TermIne, J.D., Klelnman, H.K., Whiltson, S.W., Conn, K.M., McGarvey, M.L., Martin, G.R., Cell, 26, 99 (1981)Google Scholar
21. Doi, Y., Okuda, R., Takezama, Y., Shibata, S., Moriwaki, Y., Wakamatsu, N., Shimizu, N., Morlyama, K., Shimokawa, H., Calcif. Tissue Int., 44, 200 (1989)Google Scholar