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Journal article

Subcellular localization of the melanoma-associated protein Melan-AMART-1 influences the processing of its HLA-A2-restricted epitope.

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  • 2001-09-12
Published in:
  • The Journal of biological chemistry. - 2001
Amino Acid Sequence
Antigens, Neoplasm
Cell Line
Cell Membrane
Cysteine Endopeptidases
Cytosol
Dose-Response Relationship, Drug
Endoplasmic Reticulum
Epitopes
Exocytosis
Glycoside Hydrolases
Golgi Apparatus
HLA-A2 Antigen
Humans
Kinetics
MART-1 Antigen
Microscopy, Fluorescence
Models, Biological
Molecular Sequence Data
Multienzyme Complexes
Neoplasm Proteins
Peptides
Plasmids
Precipitin Tests
Proteasome Endopeptidase Complex
Protein Binding
Protein Structure, Tertiary
T-Lymphocytes, Cytotoxic
Time Factors
Transfection
English The peptide derived from the melanoma-associated protein Melan-A (Melan-A(26-35)/HLA-A2) is an attractive candidate for tumor immunotherapy but little is known about the intracellular processing of this antigen. Here we show that Melan-A is a single-pass membrane protein with an NH(2) terminus exposed to the lumen of the exocytic compartment. In transfected melanoma cells, Melan-A accumulates in the Golgi region. Inversion of the membrane topology leads to the retention of Melan-A in the endoplasmic reticulum. Most strikingly, melanoma cells expressing this form of Melan-A are more effectively recognized by specific CTL than those expressing either Melan-A in its native membrane orientation or Melan-A artificially localized in the cytosol. Our data are compatible with the notion that proteins retained in the endoplasmic reticulum are more efficiently degraded and produce more antigenic peptides.
Language
  • English
Open access status
bronze
Identifiers
Persistent URL
https://sonar.ch/global/documents/93563
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