Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1999-8-12
pubmed:abstractText
Tumors evade host immunity at both the induction and effector phases Most studies have focused on tumor evasion at the induction phase, and, due in part to poor antitumor CTL responses to most tumors, the mechanism for evasion of CTL effector function is less clear. Here we have taken advantage of the strong CTL responses to a costimulator B7-1-transfected tumor to study the mechanism for tumor evasion of preexisting host immunity. We have investigated six independent recurrent tumors isolated from mice that were challenged with and had rejected B7-1-transfected J558 (J558-B7) tumors. Because the mice had developed strong antitumor CTL responses, these recurrent tumors must have evaded preexisting antitumor CTLs. Indeed, whereas the parental J558-B7 cell line is efficiently lysed by the ex vivo tumor-infiltrating lymphocytes, all of the recurrent tumors are resistant to such lysis. Interestingly, the recurrent tumors can be divided into two groups. The group 1 tumors have vastly reduced levels of cell surface MHC class I with a concurrent reduction in the expression of multiple genes devoted to MHC class I antigen presentation. In contrast, the group 2 tumors have lost the expression of costimulatory molecule B7-1 while retaining cell surface MHC class I and expression of all antigen presentation genes studied. These results demonstrate that tumors can evade preexisting CTLs either by avoiding presentation of the tumor antigen or, surprisingly, by down-regulation of costimulatory molecules. The paradoxical requirements of both antigen and costimulatory molecules at the effector phase raised an interesting question on the nature of antitumor immunity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD80, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Matrix Proteins, http://linkedlifedata.com/resource/pubmed/chemical/H-2 Antigens, http://linkedlifedata.com/resource/pubmed/chemical/LMP-2 protein, http://linkedlifedata.com/resource/pubmed/chemical/LMP7 protein, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Neoplasm, http://linkedlifedata.com/resource/pubmed/chemical/Tap2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/beta 2-Microglobulin
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0008-5472
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3461-7
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:10416611-ATP-Binding Cassette Transporters, pubmed-meshheading:10416611-Animals, pubmed-meshheading:10416611-Antigen Presentation, pubmed-meshheading:10416611-Antigens, CD80, pubmed-meshheading:10416611-Cysteine Endopeptidases, pubmed-meshheading:10416611-Extracellular Matrix Proteins, pubmed-meshheading:10416611-H-2 Antigens, pubmed-meshheading:10416611-Major Histocompatibility Complex, pubmed-meshheading:10416611-Mice, pubmed-meshheading:10416611-Mice, Inbred BALB C, pubmed-meshheading:10416611-Multienzyme Complexes, pubmed-meshheading:10416611-Neoplasm Metastasis, pubmed-meshheading:10416611-Neoplasm Proteins, pubmed-meshheading:10416611-Neoplasm Recurrence, Local, pubmed-meshheading:10416611-Nerve Tissue Proteins, pubmed-meshheading:10416611-Proteasome Endopeptidase Complex, pubmed-meshheading:10416611-Proteins, pubmed-meshheading:10416611-RNA, Messenger, pubmed-meshheading:10416611-RNA, Neoplasm, pubmed-meshheading:10416611-T-Lymphocytes, Cytotoxic, pubmed-meshheading:10416611-Transfection, pubmed-meshheading:10416611-beta 2-Microglobulin
pubmed:year
1999
pubmed:articleTitle
Two mechanisms for tumor evasion of preexisting cytotoxic T-cell responses: lessons from recurrent tumors.
pubmed:affiliation
Department of Pathology and Comprehensive Cancer Center, Ohio State University Medical Center, Columbus 43210, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't