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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1995-7-20
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pubmed:abstractText |
Cytotoxic T cells (CTL) are known to recognize small peptide fragments of cytoplasmic proteins bound to major histocompatibility complex (MHC) class I molecules on cell surfaces. Recent work indicates that tumor antigens are processed and presented in a manner similar to viral antigens. Identification of the peptides recognized by tumor-specific CTL would provide valuable information about their parent proteins, as well as allowing for the development of recombinant antigen-specific tumor vaccines. While highly represented MHC-bound peptides have been routinely purified by reversed-phase HPLC for Edman degradation sequencing, identification and sequencing of infrequent peptides that represent the biologically relevant targets of tumor-specific CTL have proved elusive. We have combined matrix-assisted laser desorption/ionization mass spectrometry with on-slide exopeptidase digestion to successfully identify and directly sequence a model tumor-specific peptide antigen derived from an integrated viral gene. The enhanced sensitivity of this technique (femtomolar range) allows for the sequencing of specific MHC-bound peptides derived from as few as 1 x 10(9) cells.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ammonium Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/Carboxypeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class I,
http://linkedlifedata.com/resource/pubmed/chemical/Leucyl Aminopeptidase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/carboxypeptidase P
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0003-2697
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
226
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15-25
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7785766-Amino Acid Sequence,
pubmed-meshheading:7785766-Ammonium Sulfate,
pubmed-meshheading:7785766-Animals,
pubmed-meshheading:7785766-Antigens, Neoplasm,
pubmed-meshheading:7785766-Carboxypeptidases,
pubmed-meshheading:7785766-Chromatography, High Pressure Liquid,
pubmed-meshheading:7785766-Histocompatibility Antigens Class I,
pubmed-meshheading:7785766-Leucyl Aminopeptidase,
pubmed-meshheading:7785766-Mass Spectrometry,
pubmed-meshheading:7785766-Mice,
pubmed-meshheading:7785766-Molecular Sequence Data,
pubmed-meshheading:7785766-Peptides,
pubmed-meshheading:7785766-Sensitivity and Specificity,
pubmed-meshheading:7785766-Sequence Analysis,
pubmed-meshheading:7785766-T-Lymphocytes, Cytotoxic,
pubmed-meshheading:7785766-Tumor Cells, Cultured
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pubmed:year |
1995
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pubmed:articleTitle |
Simplified high-sensitivity sequencing of a major histocompatibility complex class I-associated immunoreactive peptide using matrix-assisted laser desorption/ionization mass spectrometry.
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pubmed:affiliation |
Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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