Cell-binding domain context affects cell behavior on engineered proteins

Biomacromolecules

Volumn 6, Issue 1, 2005, Pages 318-323

  Heilshorn, Sarah C ^a   Liu, Julie ^a   Tirrell, David A ^a  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION; AMINO ACIDS; CARDIOVASCULAR SYSTEM; CELL CULTURE; CELLS; CONFORMATIONS; CROSSLINKING; PROTEINS;

ARTIFICIAL EXTRACELLULAR MATRIX PROTEINS; CELL ADHESION; CELL BINDING; VASCULAR GRAFTS;

GRAFTS;

ALPHA4 INTEGRIN; BETA1 INTEGRIN; ELASTIN; FIBRONECTIN; INTEGRIN RECEPTOR; SCLEROPROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CELL ADHESION; CELL CULTURE; CELL FUNCTION; CONTROLLED STUDY; ENDOTHELIUM CELL; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN CROSS LINKING; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; SCANNING ELECTRON MICROSCOPY;

AMINO ACID SEQUENCE; CELL ADHESION; ELASTIN; ENDOTHELIAL CELLS; EXTRACELLULAR MATRIX; FIBRONECTINS; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; TIME FACTORS;

EID: 14044269989     PISSN: 15257797     EISSN: None     Source Type: Journal    
DOI: 10.1021/bm049627q     Document Type: Article

References (44)

1. Humphries, M. J.; Akiyama, S. K.; Komoriya, A.; Olden, K.; Yamada, K. M. J. Cell Biol. 1986, 103, 2637-2647.
2. Humphries, M. J.; Komoriya, A.; Akiyama, S. K.; Olden, K.; Yamada, K. M. J. Biol. Chem. 1987, 262, 6886-6892.
3. Komoriya, A.; Green, L. J.; Mervic, M.; Yamada, S. S.; Yamada, K. M.; Humphries, M. J. J. Biol. Chem. 1991, 266 15075-15079.
4. Graf, J.; Iwamoto, Y.; Sasaki, M.; Martin, G. R.; Kleinman, H. K.; Robey, F. A.; Yamada, Y. Cell 1987, 48, 989-996.
5. Graf, J.; Ogle, R. C.; Robey, F. A.; Sasaki, M.; Martin, G. R.; Yamada, Y.; Kleinman, H. K. Biochemistry 1987, 26, 6896-6900.
6. Sephel, G. C.; Tashiro, K. I.; Sasaki, M.; Greatorex, D.; Martin, G. R.; Yamada, Y.; Kleinman, H. K. Biochem. Biophys. Res. Commun. 1989, 162, 821-829.
7. Tashiro, K.; Sephel, G. C.; Weeks, B.; Sasaki, M.; Martin, G. R.; Kleinman, H. K.; Yamada, Y. J. Biol. Chem. 1989, 264 16174-16182.
8. Pierschbacher, M.; Hayman, E. G.; Ruoslahti, E. Proc. Natl. Acad. Sci. 1983, 80, 1224-1227.
9. Pierschbacher, M. D.; Ruoslahti, E. Nature 1984, 309, 30-33.
10. Pierschbacher, M. D.; Ruoslahti, E. Proc. Natl. Acad. Sci. 1984, 81, 5985-5988.
11. For review of RGD biomaterials, see: Hersel, U.; Dahmen, C.; Kessler, H. Biomaterials 2003, 24, 4385-4415.
12. Pierschbacher, M. D.; Ruoslahti, E. J. Biol. Chem. 1987, 262, 17294-17298.
13. Koivunen, E.; Wang, B. C.; Ruoslahti, E. Bio-Technology 1995, 13, 265-270.
14. Healy, J. M.; Haruki, M.; Kikuchi, M. Protein Pept. Lett. 1996, 3, 23-30.
15. Richards, J.; Miller, M.; Abend, J.; Koide, A.; Koide, S.; Dewhurst, S. J. Mol. Biol. 2003, 326, 1475-1488.
16. Cheng, S.; Craig, W. S.; Mullen, D.; Tschopp, J. F.; Dixon, D.; Pierschbacher, M. D. J. Med. Chem. 1994, 37, 1-8.
17. Krejchi, M. T.; Atkins, E. D. T.; Waddon, A. J.; Fournier, M. J.; Mason, T. L.; Tirrell, D. A. Science 1994, 265, 1427-1432.
18. Petka, W. A.; Harden, J. L.; McGrath, K. P.; Wirtz, D.; Tirrell, D. A. Science 1998, 281, 389-392.
19. Yu, S. J. M.; Conticello, V. P.; Zhang, G. H.; Kayser, C.; Fournier, M. J.; Mason, T. L.; Tirrell, D. A. Nature 1997, 389, 167-170.
20. Urry, D. W.; Pattanaik, A.; Xu, J.; Woods, T. C.; McPherson, D. T.; Parker, T. M. J. Biomater. Sci.-Polym. Ed. 1998, 9 1015-1048.
21. Panitch, A.; Yamaoka, T.; Fournier, M. J.; Mason, T. L.; Tirrell, D. A. Macromolecules 1999, 32, 1701-1703.
22. Welsh, E. R.; Tirrell, D. A. Biomacromolecules 2000 1, 23-30.
23. Halstenberg, S.; Panitch, A.; Rizzi, S.; Hall, H.; Hubbell, J. A. Biomacromolecules 2002, 3, 710-723.
24. Heilshorn, S. C.; Di Zio, K.; Welsh, E. R.; Tirrell, D. A. Biomaterials 2003, 24, 4245-4252.
25. Nowatzki, P. J.; Tirrell, D. A. Biomaterials 2004 25, 1261-1267.
26. Liu, J. C.; Heilshorn, S. C.; Tirrell, D. A. Biomacromolecules 2004, in press.
27. Nagaoka, M.; Ise, H.; Akaike, T. Biotechnol. Lett. 2002, 24, 1857-1862.
28. Asakura, T.; Tanaka, C.; Yang, M. Y.; Yao, J. M.; Kurokawa, M. Biomaterials 2004, 25, 617-624.
29. Kobatake, E.; Onoda, K.; Yanagida, Y.; Aizawa, M. Biomacromolecules 2000, 1, 382-386.
30. Nicol, A.; Gowda, D. C.; Parker, T. M.; Urry, D. W. In Biotechnology and Bioactive Polymers; Gebelein, C. G., Carraher, C. E., Eds.; Plenum Press: New York, 1994.
31. American Heart Association. Heart Disease and Stroke Statistics - 2003 Update; American Heart Association: Dallas, TX, 2002.
32. Rayner, M.; Petersen, S. European Cardiovascular Disease Statistics; British Heart Foundation: London, 2000.
33. Bos, G. W.; Poor, A. A.; Beugeling, T.; van Aken, W. G.; Feijen, J. Arch. Physiol. Biochem. 1998, 106, 100-115.
34. Salacinski, H. J.; Tiwari, A.; Hamilton, G.; Seifalian, A. M. Med. Biol. Eng. Comput. 2001 , 39, 609-618.
35. Nugent, H. M.; Edelman, E. R. Circ. Res. 2003, 92, 1068-1078.
36. Fung, Y. C. Biomechanics: Mechanical Properties of Living Tissues, 2nd ed.; Springer-Verlag: New York, 1993.
37. Di Zio, K.; Tirrell, D. A. Macromolecules 2003, 36, 1553-1558.
38. Smith, P. K.; Krohn, R. I.; Hermanson, G. T.; Mallia, A. K.; Gartner, F. H.; Provenzano, M. D.; Fujimoto, E. K.; Goeke, N. M.; Olson, B. J.; Klenk, D. C. Anal. Biochem. 1985, 150, 76-85.
39. Wiechelman, K. J.; Braun, R. D.; Fitzpatrick, J. D. Anal. Biochem. 1988, 175, 231-237.
40. Calibration curves were identical when using either protein solutions of known concentrations or known amounts of protein dried down in wells.
41. Channavajjala, L. S.; Eidsath, A.; Saxinger, W. C. J. Cell Sci. 1997, 110, 249-256.
42. Koo, L. Y.; Irvine, D. J.; Mayes, A. M.; Lauffenburger, D. A.; Griffith, L. G. J. Cell Sci. 2002, 115, 1423-1433.
43. Hubbell, J. A.; Massia, S. P.; Desai, N. P.; Drumheller, P. D. BioTechnology 1991, 9, 568-572.
44. One of the referees suggested that the observed differences in Cell spreading and adhesion might be due to the difference in molar mass between Ki and Kt molecular weights 37 and 43 kDa, respectively. We performed experiments using Kt and a similar protein with a molar mass of 70 kDa (instead of three repeats of the CS5 cell-binding domain and elastin cassette: this protein has five repeats) and observed no differences in cellular response. Because a molecular weight difference of 27 kDa does not alter cellular response to the Kt sequence design, we do not expect that a molecular weight difference of 6 kDa contributes to the observed differences in cellular response to Kt and Ki.