Cargando…
Heat shock protein 70-associated peptides elicit specific cancer immunity
Vaccination of mice with heat shock protein 70 (hsp70) preparations derived from the Meth A sarcoma, but not from normal tissues, renders the mice immune to a substantial challenge with Meth A sarcoma. The immunogenicity is dose dependent and tumor specific. Treatment of an antigenically active hsp7...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1993
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2191193/ https://www.ncbi.nlm.nih.gov/pubmed/8376942 |
_version_ | 1782146947282370560 |
---|---|
collection | PubMed |
description | Vaccination of mice with heat shock protein 70 (hsp70) preparations derived from the Meth A sarcoma, but not from normal tissues, renders the mice immune to a substantial challenge with Meth A sarcoma. The immunogenicity is dose dependent and tumor specific. Treatment of an antigenically active hsp70 preparation with ATP followed by removal of low-molecular weight material leaves hsp70 intact, as judged by SDS- PAGE but results in loss of antigenicity, as judged by tumor rejection assays. Separation of this low-molecular weight material on a C18 reverse-phase column shows a diverse array of peptides with molecular mass between 1,000 and 5,000 daltons. Our data indicate that antigenicity of hsp70 preparations derives, not from hsp70 per se, but from associated peptides. These observations may suggest a novel method of using the peptide-binding property of hsp70 for specific vaccination against cancer and infectious diseases. |
format | Text |
id | pubmed-2191193 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1993 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21911932008-04-16 Heat shock protein 70-associated peptides elicit specific cancer immunity J Exp Med Articles Vaccination of mice with heat shock protein 70 (hsp70) preparations derived from the Meth A sarcoma, but not from normal tissues, renders the mice immune to a substantial challenge with Meth A sarcoma. The immunogenicity is dose dependent and tumor specific. Treatment of an antigenically active hsp70 preparation with ATP followed by removal of low-molecular weight material leaves hsp70 intact, as judged by SDS- PAGE but results in loss of antigenicity, as judged by tumor rejection assays. Separation of this low-molecular weight material on a C18 reverse-phase column shows a diverse array of peptides with molecular mass between 1,000 and 5,000 daltons. Our data indicate that antigenicity of hsp70 preparations derives, not from hsp70 per se, but from associated peptides. These observations may suggest a novel method of using the peptide-binding property of hsp70 for specific vaccination against cancer and infectious diseases. The Rockefeller University Press 1993-10-01 /pmc/articles/PMC2191193/ /pubmed/8376942 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Heat shock protein 70-associated peptides elicit specific cancer immunity |
title | Heat shock protein 70-associated peptides elicit specific cancer immunity |
title_full | Heat shock protein 70-associated peptides elicit specific cancer immunity |
title_fullStr | Heat shock protein 70-associated peptides elicit specific cancer immunity |
title_full_unstemmed | Heat shock protein 70-associated peptides elicit specific cancer immunity |
title_short | Heat shock protein 70-associated peptides elicit specific cancer immunity |
title_sort | heat shock protein 70-associated peptides elicit specific cancer immunity |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2191193/ https://www.ncbi.nlm.nih.gov/pubmed/8376942 |