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Cell Function on Substrates Containing Immobilized Bioactive Peptides

Published online by Cambridge University Press:  15 February 2011

Kay C Dee
Affiliation:
Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, NY, 12180
Thomas T. Andersen
Affiliation:
Department of Biochemistry, Albany Medical College, Albany, NY, 12208
R. Bizios
Affiliation:
Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, NY, 12180
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Abstract

Adhesion, proliferation and motility of bovine pulmonary artery endothelial cells and of rat calvarial osteoblasts were examined in vitro and on glass surfaces modified with immobilized bioactive peptides. The peptides Arginine-Glycine-Aspartic Acid-Serine (RGDS), Arginine-Aspartic Acid-Glycine-Serine (RDGS), and Tyrosine-Isoleucine-Glycine-Serine-Arginine-Glycine (YIGSRG) were covalently bound to aminophase glass. The results of this study showed that modification of the substrate surface with immobilized peptides affected each cell line in different ways. Incorporation of this knowledge in the design of implant materials could result in biomaterials which promote and/or sustain a number of desirable cellular functions at the tissue-implant interface.

Type
Research Article
Copyright
Copyright © Materials Research Society 1994

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References

1. Yamada, K., J. Biol. Chem., 266, 1280912812 (1991).Google Scholar
2. Kojima, N. and Hakamori, S., J. Biol. Chem., 266, 1755217558 (1991).Google Scholar
3. Ruoslahti, E., J. Biol. Chem., 264, 1336913372 (1989).Google Scholar
4. Buck, C.A. and Horwitz, A.F., J. Cell Sci., 8, 231250 (1987).Google Scholar
5. Schwarzbauer, J.E., Curr. Op. in Cell Bio., 3, 786791 (1991).Google Scholar
6. Mercurio, A.M., Curr. Op. in Cell Bio., 2, 845849 (1990).Google Scholar
7. Yamada, K.M., J. Biol. Chem., 266(20), 1280912812 (1991).Google Scholar
8. Massia, S.P. and Hubbell, J.A., Anal. Biochem., 187, 292301 (1990).Google Scholar
9. Massia, S.P. and Hubbell, J.A., J. Biomed. Mater. Res., 25, 223242 (1991).Google Scholar
10. Robinson, P.J., Dunnil, P. and Lilly, M.D., Biochim. Biophys. Acta, 242, 659661 (1971).Google Scholar
11. Akashi, M., Maryuma, I., Fukudome, N. and Yashima, E., Bioconj. Chem. 3(5), 363365 (1992).Google Scholar
12. Bellows, C.G., Aubin, J.E., Heersche, J.N.M., and Antosz, M.E., Caic. Tiss. Int., 38, 143154 (1986).Google Scholar
13. Puleo, D.A., Holleran, L.A., Doremus, R.H. and Bizios, R., J Biomed Mater. Res., 25, 711723 (1991).Google Scholar
14. Puleo, D.A., Preston, K.E., Shaffer, J.B. and Bizios, R., Biomaterials, 14(2), 111116 (1993).Google Scholar
15. Malik, M.A., Puleo, D.A., Bizios, R. and Doremus, R.H., Biomaterials, 25, 123128 (1991).Google Scholar
16. Puleo, D.A. and Bizios, R., Bone, 12, 271276 (1991).Google Scholar
17. Puleo, D.A. and Bizios, R., Bone and Mineral, 18, 215226 (1992).Google Scholar