Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96

Curr Opin Immunol. 1998 Feb;10(1):103-9. doi: 10.1016/s0952-7915(98)80039-3.

Abstract

The past year has born witness to compelling demonstrations of the utility of peptide complexes with glucose regulated protein 94 (GRP94, also known as gp96) in cancer immunotherapy. Insights into the structural basis of peptide binding to GRP94 have been obtained and the role of the transporter for antigen presentation in defining the GRP94-bound peptide composition has been determined.

Publication types

  • Review

MeSH terms

  • Animals
  • Antigens, Neoplasm / chemistry
  • Antigens, Neoplasm / immunology
  • Endoplasmic Reticulum / metabolism
  • HSP70 Heat-Shock Proteins* / chemistry
  • HSP70 Heat-Shock Proteins* / immunology
  • HSP70 Heat-Shock Proteins* / metabolism
  • Humans
  • Membrane Proteins* / chemistry
  • Membrane Proteins* / immunology
  • Membrane Proteins* / metabolism
  • Molecular Chaperones* / chemistry
  • Molecular Chaperones* / immunology
  • Molecular Chaperones* / metabolism
  • Peptides / metabolism
  • Phylogeny
  • Subcellular Fractions

Substances

  • Antigens, Neoplasm
  • HSP70 Heat-Shock Proteins
  • Membrane Proteins
  • Molecular Chaperones
  • Peptides
  • glucose-regulated proteins