Letter | Published:

Evidence for translation of rabbit globin mRNA after liposomemediated insertion into a human cell line

Nature volume 274, pages 921923 (31 August 1978) | Download Citation

Subjects

Abstract

THE ability to insert messenger RNA selectively into large numbers of differentiated eukaryotic cells and thereby alter the expression of the eukaryotic genome would provide a new and direct approach to the study of the molecular mechanisms involved in protein synthesis. Several procedures have been used to facilitate the cellular incorporation of administered RNA, including microinjection of RNA into Xenopus oocytes1–6 and into fully differentiated eukaryotic cells7,8, direct co-cultivation of cells with naked RNA (refs 9–12), and encapsulation of mRNA within erythrocyte ghosts followed by Sendai virus induced fusion of the ghosts to recipient cells in culture13. We describe here the use of liposomes for the selective insertion of functional mRNA into differentiated eukaryotic cells in vitro. We provide evidence which indicates that cultured human epithelial carcinoma cells (HEp-2) treated with liposomally encapsulated rabbit globin mRNA are stimulated to produce a globin-like protein.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1.

    , & J. molec. Biol. 61, 73–91 (1971).

  2. 2.

    , & J. Clin. Invest. 57, 576–585 (1976).

  3. 3.

    , , & Proc. natn. Acad. Sci. U.S.A. 74, 4415–4419 (1977).

  4. 4.

    , & Molec. Biol. Rep. 1, 3–8 (1973).

  5. 5.

    & Proc. natn. Acad. Sci. U.S.A. 74, 4462–4465 (1977).

  6. 6.

    , & Proc. natn. Acad. Sci. U.S.A. 69, 1203–1207 (1972).

  7. 7.

    , & Proc. natn. Acad. Sci. U.S.A. 74, 4831–4834 (1977).

  8. 8.

    & 9, 725–732 (1976).

  9. 9.

    in Immune RNA in Neoplasia, (ed. Fink, M.) 61–73 (Academic, New York, 1976).

  10. 10.

    , & J. Immun. 97, 554–558 (1966).

  11. 11.

    , & Exp. Cell Res. 78, 15–24 (1973).

  12. 12.

    et al. Cell Immun. 11, 389–400 (1974).

  13. 13.

    & J. Cell Biol. 70, 185a (1976).

  14. 14.

    & Biochemistry 8, 3000–3005 (1969).

  15. 15.

    & Proc. natn. Acad. Sci. U.S.A. 69, 1408–1412 (1972).

  16. 16.

    & Biochim. biophys. Acta 443, 629–634 (1976).

  17. 17.

    , & Biochem. biophys. Res. Commun. 76, 836–842 (1977).

  18. 18.

    & J. Immun. 103, 380–382 (1969).

  19. 19.

    & J. biol. Chem. 252, 2684–2690 (1977).

  20. 20.

    , , , & Biochemistry 15, 452–460 (1976).

  21. 21.

    , , & Biochim. biophys. Acta 451, 610–618 (1976).

  22. 22.

    & Biochem. J. 164, 439–445 (1977).

  23. 23.

    & Biochim. biophys. Acta 451, 417–425 (1976).

  24. 24.

    & J. biol. Chem. 244, 4406–4412 (1969).

Download references

Author information

Affiliations

  1. Department of Microbiology and Immunology, University of Illinois at the Medical Center, Chicago, Illinois 60612

    • MARC J. OSTRO
    • , DARIO GIACOMONI
    • , DON LAVELLE
    • , WILLIAM PAXTON
    •  & SHELDON DRAY

Authors

  1. Search for MARC J. OSTRO in:

  2. Search for DARIO GIACOMONI in:

  3. Search for DON LAVELLE in:

  4. Search for WILLIAM PAXTON in:

  5. Search for SHELDON DRAY in:

About this article

Publication history

Received

Accepted

Published

DOI

https://doi.org/10.1038/274921a0

Further reading

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.