Abstract |
The possible degradation of the tumor antigen epitope gp100(280-288) (YLEPGPVTA) in the presence of the monocyte-like line U937, and the effect of degradation on the in vitro-measured immune recognition, were investigated by chromatographic techniques and immunological assays. Results indicate a rapid hydrolysis of the substrate in the presence of the model cells, which is consistent with the hypothesis that degradation of gp100(280-288) is caused by the activity of U937-expressed enzymes, specifically amino- and carboxypeptidases. On the other hand, these results do not support the involvement of other enzymes known to be expressed by U937 cells. From a functional point of view, these data indicate that the degradation of gp100(280-288) severely hampered recognition by specific CTL clones. The results obtained may provide a model for epitope degradation by the antigen-presenting cells found in defined anatomical compartments and may, at least in part, account for the low activity of peptide-based antineoplastic vaccines, as well as for the transience of the effects of subcutaneously administered peptides in general.
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Authors | Federica Albo, Antonella Cavazza, Bruno Giardina, Silvio Lippa, Mario Marini, L Giorgio Roda, Giulio Spagnoli |
Journal | Peptides
(Peptides)
Vol. 24
Issue 3
Pg. 371-8
(Mar 2003)
ISSN: 0196-9781 [Print] United States |
PMID | 12732334
(Publication Type: Journal Article)
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Chemical References |
- Amino Acids
- Antigens, Neoplasm
- Peptide Fragments
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Topics |
- Amino Acids
(metabolism)
- Antigens, Neoplasm
(chemistry, immunology, metabolism)
- Humans
- Hydrolysis
- Kinetics
- Melanoma
(chemistry, immunology)
- Monocytes
(metabolism)
- Peptide Fragments
(chemistry, immunology, metabolism)
- T-Lymphocytes, Cytotoxic
(immunology)
- U937 Cells
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