Skip to main content

Expression of Neurotrophic Factors such as GDNF in the E. coli System

  • Protocol
  • 474 Accesses

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 169))

Abstract

Neurotrophic factors play an essential role in the growth, survival, and differentiation of neurons in the nervous system. Several well-characterized neurotrophic factors, such as nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), NT-4/5, glial-cell-line-derived neurotrophic factor (GDNF), ciliary neurotrophic factor (CNTF), insulin-like growth factor-1 (IGF-I), are currently in clinical trials and have potential for the treatment of neurological diseases.

This is a preview of subscription content, log in via an institution.

Buying options

Protocol
USD   49.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   84.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD   109.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Springer Nature is developing a new tool to find and evaluate Protocols. Learn more

References

  1. Blackwell, J. R. and Horgan, R. (1991) A novel stratage for production of a highly expressed recombinant protein in an active form. FEBS Lett. 295, 10–12.

    Article  PubMed  CAS  Google Scholar 

  2. Hoess, A., Arthur, A. K., Wanner, G., and Fanning, E. (1988) Recovery of soluble, biologically active recombinant proteins from total bacterial lysates using ion exchange resin. Bio/Technology 6, 1214–1217.

    Article  CAS  Google Scholar 

  3. Amold, F. H. (1991) Metal-affinity separations: a new dimension in protein processing. Bio/Technology 9, 151–156.

    Article  Google Scholar 

  4. Aukhil, L., Joshi, P., Yan, Y., and Erickson, H. P. (1993) Cell-and heparin-binding domains of the hexabrachionarm indentified by tenascin expression protein. J. Biol. Chem. 268, 2542–2553.

    PubMed  CAS  Google Scholar 

  5. Schein, C. H. and Noteborn, M. H. M. (1989) Production of soluble recombinant protein in Bacteria. Bio/Technology 7, 1141–1148.

    CAS  Google Scholar 

  6. Wickner, W., Driessen, A. J. M., and Hartl, F.-U. (1991) The enzymology of protein translocation across the E. coli plasma membrane. Ann. Rev. Biochem. 60, 101–124.

    Article  PubMed  CAS  Google Scholar 

  7. Sukegawa, J. and Blobel, G. (1993) A nuclear pore complex protein that contains zinc finger motifs, binds DNA and faces the nucleoplasm. Cell 72, 29–38.

    Article  PubMed  CAS  Google Scholar 

  8. Yamane, K. and Mizushima, S. (1988) Introduction of basic amino acid residuess after the signal peptide inhibits protein translocation across the cytoplasmic membrane of E. coli. J. Biol. Chem. 263, 19,690–19,696.

    PubMed  CAS  Google Scholar 

  9. Sambook, J., Fritsch, F. F., and Maniatis, T. (1989) Expression of cloned genes in cultured mammalian cells, in Molecular Cloning: A Laboratory Manual, 16.1–16.81, 2nd ed., Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.

    Google Scholar 

  10. Studier, F. W. and Moffatt, B. A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189, 113–130.

    Article  PubMed  CAS  Google Scholar 

  11. Qin, N., Pittler, S., and Baehr, W. (1992) In vitro isoprenylation and membrane association of mouse rod photoreceptor cGMP phosphodiesterase a and b sub-units expressed in Bacteria. J. Biol. Chem. 267, 8458–8463.

    PubMed  CAS  Google Scholar 

  12. Leady, D. J., Hendrickson, W. A., Aukhil, I., and Erickson, H. P. (1992) Structure of a fibronectin type III domain from transcin phased by MAD analysis. Science 258, 987–991.

    Article  Google Scholar 

  13. Rosenberg, A. H., Lade, B. N., Chui, D., Lin, S., Dunn, J. J., and Studier, F. W. (1987) Vector for selective expression of cloned DNA by T7 RNA polymerase. Gene 56, 125.

    Article  PubMed  CAS  Google Scholar 

  14. Moffatt, B. A. and Pfeffer, D. (1987) T7lysozyme inhibits transcription by T7 RNA polymerase. Cell 49, 221.

    Article  PubMed  CAS  Google Scholar 

  15. Seed, B. (1987) An LFA-3 cDNA encodes a phaspholipid-linked membrane protein homologous to its receptor CD2. Nature 329, 840.

    Article  PubMed  CAS  Google Scholar 

  16. Keyse, S. M. and Emsslie, E. A. (1992) A human gene ecoding a protein-tyrosine phosphatase. Nature 359, 644–647.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2001 Humana Press Inc.

About this protocol

Cite this protocol

Huang, BR., Ma, XM. (2001). Expression of Neurotrophic Factors such as GDNF in the E. coli System. In: Rush, R.A. (eds) Neurotrophin Protocols. Methods in Molecular Biology™, vol 169. Humana Press. https://doi.org/10.1385/1-59259-060-8:101

Download citation

  • DOI: https://doi.org/10.1385/1-59259-060-8:101

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-699-4

  • Online ISBN: 978-1-59259-060-5

  • eBook Packages: Springer Protocols

Publish with us

Policies and ethics