Linked Life Data

11751953

Source:http://linkedlifedata.com/resource/pubmed/id/11751953

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-12-25
pubmed:abstractText
A viral oncogene carrying well-defined K(b)/D(b)-restricted epitopes was expressed in a heat shock protein (hsp)-associated or nonassociated form in the murine tumor cells P815 and Meth-A. Wild-type SV40 large T-Ag (wtT-Ag) is expressed without stable hsp association; mutant (cytoplasmic cT-Ag) or chimeric (cT272-green fluorescent fusion protein) T-Ag is expressed in stable association with the constitutively expressed, cytosolic hsp73 (hsc70) protein. In vitro, remnants from apoptotic wtT-Ag- or cT-Ag-expressing tumor cells are taken up and processed by immature dendritic cells (DC), and the K(b)/D(b)-binding epitopes T1, T2/3, and T4 of the T-Ag are cross-presented to CTL in a TAP-independent way. DC pulsed with remnants of transfected, apoptotic tumor cells cross-presented the three T-Ag epitopes more efficiently when they processed ATP-sensitive hsp73/cT-Ag complexes than when they processed hsp-nonassociated (native) T-Ag. In vivo, more IFN-gamma-producing CD8+ T cells were elicited by a DNA vaccine that encoded hsp73-binding mutant T-Ag than by a DNA vaccine that encoded native, non-hsp-binding T-Ag. Three- to 5-fold higher numbers of T-Ag (T1-, T2/3-, or T4-) specific, D(b)/K(b)-restricted IFN-gamma-producing CD8+ T cells were primed during the growth of transfected H-2(d) Meth-A/cT tumors than during the growth of transfected Meth-A/T tumors in F(1)(b x d) hosts. Hence, the association of an oncogene with constitutively expressed, cytosolic hsp73 facilitates cross-priming in vitro and in vivo of CTL by DC that process material from apoptotic cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
168
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
108-17
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:11751953-Animals, pubmed-meshheading:11751953-Antigen Presentation, pubmed-meshheading:11751953-Antigens, Polyomavirus Transforming, pubmed-meshheading:11751953-Cancer Vaccines, pubmed-meshheading:11751953-Carrier Proteins, pubmed-meshheading:11751953-Cells, Cultured, pubmed-meshheading:11751953-Dendritic Cells, pubmed-meshheading:11751953-Endocytosis, pubmed-meshheading:11751953-Epitopes, T-Lymphocyte, pubmed-meshheading:11751953-HSC70 Heat-Shock Proteins, pubmed-meshheading:11751953-HSP70 Heat-Shock Proteins, pubmed-meshheading:11751953-Interferon-gamma, pubmed-meshheading:11751953-Lymphocyte Activation, pubmed-meshheading:11751953-Mice, pubmed-meshheading:11751953-Mice, Inbred BALB C, pubmed-meshheading:11751953-Mice, Inbred C57BL, pubmed-meshheading:11751953-Mutation, pubmed-meshheading:11751953-Neoplasms, pubmed-meshheading:11751953-T-Lymphocytes, Cytotoxic, pubmed-meshheading:11751953-Tumor Cells, Cultured, pubmed-meshheading:11751953-Vaccines, DNA
pubmed:year
2002
pubmed:articleTitle
Noncovalent association with stress protein facilitates cross-priming of CD8+ T cells to tumor cell antigens by dendritic cells.
pubmed:affiliation
Department of Medical Microbiology, University of Ulm, Helmholtzstrasse 8/1, D-89081 Ulm, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't