Association of peptides with heat shock protein gp96 occurs in vivo and not after cell lysis

Biochem Biophys Res Commun. 1999 Sep 7;262(3):813-8. doi: 10.1006/bbrc.1999.1306.

Abstract

Immunization of mice and rats with gp96 preparations isolated from syngeneic cancers has been shown to elicit protective immunity to a number of cancers. The specific immunogenicity of gp96 preparations derives from the antigenic peptides chaperoned by the gp96 molecule and not from gp96 molecules per se. Studies reported here demonstrate that the association of peptides with gp96 occurs in vivo and is not a procedural artifact which occurs in vitro after cell lysis. This demonstration has a bearing on the proposed functional role of HSP peptide association in antigen processing and presentation by MHC I molecules.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antigens, Neoplasm / chemistry*
  • Antigens, Neoplasm / immunology
  • Antigens, Neoplasm / metabolism*
  • Artifacts
  • Female
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / metabolism
  • Histocompatibility Antigens Class I / chemistry
  • Histocompatibility Antigens Class I / metabolism
  • Mice
  • Mice, Inbred BALB C
  • Peptides / chemistry*
  • Peptides / metabolism*
  • Protein Binding
  • Rats
  • Tumor Cells, Cultured

Substances

  • Antigens, Neoplasm
  • Heat-Shock Proteins
  • Histocompatibility Antigens Class I
  • Peptides
  • sarcoma glycoprotein gp96 rejection antigens