Cutting edge: induction of the antigen-processing enzyme IFN-gamma-inducible lysosomal thiol reductase in melanoma cells Is STAT1-dependent but CIITA-independent

J Immunol. 2004 Jul 15;173(2):731-5. doi: 10.4049/jimmunol.173.2.731.

Abstract

Presentation and CD4(+) T cell responses to Ag in the context of MHC class II molecules require processing of native proteins into short peptide fragments. Within this pathway, IFN-gamma-inducible lysosomal thiol reductase (GILT) functions to catalyze thiol bond reduction, thus unfolding native protein Ag and facilitating further processing via cellular proteases. In contrast with professional APCs such as B cells, class II-positive human melanomas expressed relatively little to no GILT protein or mRNA. Tumor cell GILT expression was partially restored with IFN-gamma treatment but unlike other genes required for class II Ag presentation, GILT was not regulated by CIITA. Rather, studies revealed STAT1 plays a direct role in IFN-gamma-inducible GILT expression. These results define a molecular mechanism for the uncoupled regulation of MHC class II genes and the processing enzyme GILT in human melanomas.

Publication types

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

MeSH terms

  • Antigen Presentation* / genetics
  • DNA-Binding Proteins / metabolism*
  • Gene Expression Regulation / physiology
  • Gene Expression Regulation, Enzymologic
  • Gene Expression Regulation, Neoplastic
  • Genes, MHC Class II
  • Humans
  • Melanoma / enzymology*
  • Melanoma / genetics
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Oxidoreductases / genetics
  • Oxidoreductases / metabolism*
  • Oxidoreductases Acting on Sulfur Group Donors
  • STAT1 Transcription Factor
  • Trans-Activators / genetics
  • Trans-Activators / metabolism*

Substances

  • DNA-Binding Proteins
  • MHC class II transactivator protein
  • Nuclear Proteins
  • STAT1 Transcription Factor
  • STAT1 protein, human
  • Trans-Activators
  • Oxidoreductases
  • IFI30 protein, human
  • Oxidoreductases Acting on Sulfur Group Donors