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Macromolecular Nutriend Limitations of Encapsulated Cells

Published online by Cambridge University Press:  15 February 2011

Erik Einar Hancock  and
Linda Griffith Cima
Erik Einar Hancock
Affiliation:
Department of Chemical Engineering, Massachusetts Institute of Technology
Linda Griffith Cima
Affiliation:
Department of Chemical Engineering, Massachusetts Institute of Technology
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Abstract

Encapsulated cells are likely to encounter transport limitations of trace nutrients carried by macromolecules due to a high diffusion resistance in the encapsulating membrane. We modeled the transport of transferrin to encapsulated cells and found that the transport limitation of transferrin is potentially significant in comparison to oxygen, which is limiting in unencapsulated tissue. Since transferrin is the primary biological iron carrier, deprivation of transferrin to encapsulated cells may limit long term function and viability in vivo.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 331: Symposium T – Biomaterials for Drug and Cell Delivery , 1993 , 171
Copyright
Copyright © Materials Research Society 1994

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References

1. Sullivan, S.J., et al., Science, 252 (May 3), 718–721 (1991).Google Scholar
2. Christenson, L., Lysaght, M.J., and Dionne, K.E., in Fundamentals of Animal Cell Encapsulation and Immobilization, (CRC Press, 1993), p. 8–26.Google Scholar
3. Lanza, R.P., et al., Proceedings of the National Academy of Sciences, USA, 88, 11100–11104 (1991).Google Scholar
4. Dionne, K., PhD thesis, MIT, 1989.Google Scholar
5. Barnes, D. and Sato, G., Analytical Biochemistry, 102, 255–270 (1980).Google Scholar
6. Aisen, P., in Iron in Biochemistry and Medicine.I, (Eds, Jacobs, A and Worwood, M.,) Academic Press, New York, 1980, pp 87–123.Google Scholar
7. Lacy, P.E., et al., Science, 254, 1782–4, (1991).Google Scholar
8. McEvoy, R.C. and Leung, P.E., Endocrinology, 111 (5), 1568–1575 (1982).Google Scholar
9. Vaupel, P., Pfluger Archives, 361 , 201–204 (1976).Google Scholar
10. Swabb, E.A., Wei, J., and Gullino, P.M., Cancer Research, 34, 2814–2822 (1974).Google Scholar
11. Opong, W.S. and Zydney, A.L., AIChE Journal, 37 (10), 1497–1510 (1991).Google Scholar
12. Dionne, K.E., Colton, C.K., and Yarmush, M.L., Diabetes, 42,12–21 (1993).Google Scholar
13. Alper, C.A., Hematology. Second ed. (M.I.T., Cambridge,MA, 1977), p. 466.Google Scholar
14. Octave, J.N., et al., Trends in Biochemical Science, 8, 217–220 (1983).Google Scholar
15. Slordahl, S., Romslo, I., and Lamvik, J., Scand. J. Clin. Lab. Invest., 44, 549-533 (1984).Google Scholar
16. Young, S.P. and Garner, C., Biochem. Journal, 265, 587–591 (1990).Google Scholar
17. McArdle, H.J., Douglas, A.J., and Morgan, E.H., Journal of Cellular Physiology, 122, 405–409 (1985).Google Scholar
18. Chan, R.Y., Ponka, P. and Schulman, H. M., Experimental Cell Research, 202, 326–336 (1992).Google Scholar
19. Richardson, D. and Baker, E., Biochimica et Biophysica Acta., 1093 , 20–28 (1991).Google Scholar