Advertisement

Effect of Hsp70-peptide complexes generated in vivo on modulation EAE

  • Grazyna Galazka
  • Agata Walczak
  • Tomasz Berkowicz
  • Krzysztof Selmaj
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 495)

Abstract

Heat shock proteins (Hs;ps) are a family of proteins that are constitutively expressed by eukaryotic cells. They act as molecular chaperones, participating in intracellular translocation of proteins and enabling proper folding of polypeptide chains. It is postulated that unique chaperoning properties of Hsps might contribute to generating specific immune responses against peptides bound to theme2. Many studies have demonstrated that Hsps isolated from cancer or viral infected cells elicit antitumor or antiviral immune response. However, Hsps derived from normal cells did not shown such effect3’4.It has been suggested that peptides associated with Hsps are responsible for this specific immunogenecity5.

Keywords

Heat Shock Protein Experimental Autoimmune Encephalomyelitis Healthy Mouse Experimental Autoimmune Encephalomyelitis Mouse Nonobese Diabetic Mouse 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Srivastava, P.K., 1993, Peptide-biding heat shock proteins in the endoplasmic reticulum: role in immune response to cancer and in antigen presentation. Adv. Cancer Res. 62: 153–177.PubMedCrossRefGoogle Scholar
  2. 2.
    Srivastava, P.K., Meoret, A., Basu, S., Binder, R.J., McQuade, K.L., 1998, Heat shock proteins come of age: primitive function acquire new roles in an adaptive world. Immunity. 8: 657–665.PubMedCrossRefGoogle Scholar
  3. 3.
    Udono, H., and Srivastava, P.K., 1994, Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, Hsp90, and Hsp70, J. Immunol. 152: 5398–5403.PubMedGoogle Scholar
  4. 4.
    Suto, R., and Srivastava, P.K., 1995, A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science. 269: 1585–1588.PubMedCrossRefGoogle Scholar
  5. 5.
    Li, Z., and Srivastava, P.K., 1993, Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation. EMBO J. 12: 3143–3151.PubMedGoogle Scholar
  6. 6.
    Peng, P., Menoret, A., Srivastava, P.K., 1997, Purification of immunogenic heat shock protein 70-peptide complexes by ADP-affinity chromatography. J. Immunolgical Methods. 204: 13–21.CrossRefGoogle Scholar
  7. 7.
    van Eden, W., van der Zee, R., Paul, A.G.J., Prakken, B.J., Wendling, U., Anderton, S.M., and Wauben, M.H.M., 1998, Do heat shock proteins control the balance of T-cell regulation in inflammatory diseases?. Immunol. Today. 19: 303–307.Google Scholar
  8. 8.
    Udono, H., and Srivastava P.K., 1993, Heat shock protein 70 — associated peptides elicit specific cancer immunity. J. Exp. Med. 178: 1391–1396. Methods. 204: 13–21.Google Scholar

Copyright information

© Springer Science+Business Media New York 2001

Authors and Affiliations

  • Grazyna Galazka
    • 1
  • Agata Walczak
    • 1
  • Tomasz Berkowicz
    • 1
  • Krzysztof Selmaj
    • 1
  1. 1.Department of Neurology, Laboratory of NeuroimmunologyMedical Academy of LodzPoland

Personalised recommendations