Antigenic variation in cancer metastasis: immune escape versus immune control

Schirrmacher, Volker; Fogel, Mina; Russmann, E.; Bosslet, Klaus; Altevogt, Peter; Beck, Liliana

doi:10.1007/bf00046830

Cited by 78 publications

(50 citation statements)

References 91 publications

(102 reference statements)

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“…The murine bend3 endothelioma cell line was kindly provided by Dr. W. Risau (Bad Nauheim, FRG) and was maintained in DMEM with high glucose (Life Technologies, Eggenstein, FRG) containing 10% low endotoxin fetal bovine serum (FBS) (Life Technologies). Cells were activated with LPS from Salmonella enteritidis (Sigma, Deisenhofen, FRG) at a dose of 1 #g/ml for 4 h at 37~ The T cell lymphoma line TK-1 (13,27), the lymphoma cell lines ESb 289 and Eb (28), and the B lymphoma line L1-2 were maintained in RPMI 1640 medium supplemented with 10% FBS, 2 mM L-glutamine, 10 mM Hepes, and 50 mM 2-ME (culture medium). The T cell hybridoma cell line BI 141 (29) was kindly provided by A. Reske-Kunz (University of Mainz, Mainz, FRG) and was maintained in Iscove's medium supplemented with 5% FBS, sodium pyruvate, and 50 mM 2-ME.…”

Section: Methodsmentioning

confidence: 99%

The alpha 4 integrin chain is a ligand for alpha 4 beta 7 and alpha 4 beta 1.

Altevogt

Hubbe

Ruppert

et al. 1995

The Journal of Experimental Medicine

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SummaryThe heterodimeric ol4 integrins c~4~7 lymphocyte Peyer's patch adhesion molecule ([LPAM]-I) and ol431 (very late antigen-4) are cell surface adhesion molecules involved in lymphocyte trafficking and lymphocyte-cell and matrix interactions. Known cellular ligands include vascular cell adhesion molecule (VCAM)-I, which binds to ~431 and ol437, and the mucosal addressin cell adhesion molecule (MAdCAM)-I, which binds to ol437. Here we show that the o~4 chain of these integrins can itself serve as a ligand. The c~4 chain, immunoaffinity purified and immobilized on glass slides, binds thymocytes and T lymphocytes. Binding exhibits divalent cation requirements and temperature sensitivity which are characteristic of integrin-mediated interactions, and is specifically inhibited by anti-cx4 integrin antibodies, which exert their effect at the cell surface. Cells expressing exclusively c~4/~7 (TK-1) or c~431 (L1-2) both bound avidly, whereas ol4-negative cells did not. A soluble 34-kD ol4 chain fragment retained binding activity, and it inhibited lymphocyte adhesion to ~4 ligands. It has been shown that c~4 integrin binding to fibronectin involves an leucine-aspartic acid-valine (LDV) motif in the HeplI/IIICS region of fibronectin (CS-1 peptide), and homologous sequences are important in binding to VCAM-1 and MAdCAM-1. Three conserved LDV motifs occur in the extracellular sequence of c~4. A synthetic LDV-containing c~4-derived oligopeptide supports c~4-integrin-dependent lymphocyte adhesion and blocks binding to the 34-kD ol4 chain fragment. Our results suggest that r and r integrins may be able to bind to the ol4 subunit on adjacent cells, providing a novel mechanism for ol4 integrin-mediated and activation-regulated lymphocyte interactions during immune responses.

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Section: Methodsmentioning

confidence: 99%

The alpha 4 integrin chain is a ligand for alpha 4 beta 7 and alpha 4 beta 1.

Altevogt

Hubbe

Ruppert

et al. 1995

The Journal of Experimental Medicine

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“…This surprising in vivo finding raised the question as to whether ESb-M cells were still ESb-type cells. We therefore examined ESb-M cells for the expression of cell-surface markers that can discriminate between Eb and ESb type cells (4,5,7). ESb-M cells were found to be Thy-l-, Lyt-1 +, Lyt-2-, Fc receptor-positive and possessed the ESbtype tumor antigen (TATAEsb) ( Table I) thus showing a similar phenotype as ESb cells.…”

Section: Methodsmentioning

confidence: 99%

Metastatic potential severely altered by changes in tumor cell adhesiveness and cell-surface sialylation.

Fogel¹,

Altevogt²,

Schirrmacher³

1983

The Journal of Experimental Medicine

130

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It has been shown recently that high metastatic tumor lines can be converted to low metastatic ones by mutagenization and selection for resistance to toxic concentrations of the lectin wheat germ agglutinin (1-3). Lectin-resistant variants were found to differ from the parental lines and respective revertants in terminal cell-surface carbohydrates. Here we describe for the first time a drug-independent selection procedure for the isolation of a low metastatic variant type cell from a high metastatic tumor line. The method is based on the selection of plastic-adherent cells from a suspension culture of highly malignant cells. Similar to the above situation, plasticadherent low-metastatic variant cells were found to differ from the parental cells and from metastatic revertants in terminal cell surface carbohydrates. The importance of terminal carbohydrates, in particular of sialic acid, for cell-surface adhesiveness and metastatic potential will be discussed. Materials and MethodsTumor Lines. Eb is the Heidelberg subline of the methylcholanthrene A-induced T cell lymphoma L5178Y of DBA/2 mice and ESb is a spontaneous high metastatic variant thereof (4). Details of these cells have been described elsewhere (for a review see ref. 5).Selection of a Plastic-adherent Variant. Both tumor lines Eb and ESb grow in suspension culture (6). A strongly plastic-adherent variant (ESb-M) was isolated from the ESb cells by continuously selecting the adherent subpopulation from the suspension cultures over a period of 2 mo and >20 selection steps. ESb-M cells which were released into suspension from monolayer cultures grown to confluency were taken for analysis.Flow Cytofluorography. Immunofluorescent staining was carried out by incubating 2 × 106 cells with appropriately diluted fluorescein isothiocyanate-(FITC) conjugated lectins for 45 rain on ice. The reaction was carried out in saline containing 1 mM Mg and Ca salts. Flow cytofluorographic analysis was performed on an Ortho H-50 cell sorter (Ortho Instruments, Westwood, MA). Fluorescence gains were kept at constant setting for each lectin analyzed. Cell surface differentiation antigens were determined by indirect immunofluorescenceand cytofluorography as described (7).Isolation of Tumor Cells from Organs. Spleen and brain of ESb-M tumor bearing mice were removed 40 d after tumor cell inoculation and pressed through a fine nylon mesh. The cells were suspended and cultured in the appropriate tissue culture medium (4). ResultsWhen inoculated into syngeneic DBA/2 mice, the plastic-adherent ESb-M variant type cells were found to be tumorigenic but not metastatic. The survival curves of * Supported as a guest by the Deutsches Krebsforschungszentrum.Supported by a grant from the Stiftung Meyenburg.J. Exe. MED.

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“…It is easily accessible without the need for pre-treatments such as shaving, and has been demonstrated to be a privileged organ for the induction of protective antitumor immune responses. 19,20,26 An interesting point is the detection of ␤-gal expressing cells in the draining lymph node after i.e. injection of lacZ.…”

Section: -Induced Immune Responses To Different Lacz Plasmid Expressimentioning

confidence: 99%

“…In previous studies with the ESb tumor system it was shown that the ear pinna is a privileged site for the induction of antitumor immunity, 19 preventing the outgrowth of an otherwise lethal dose of tumor cells. Thus it was reasonable to test the ear pinna also as a putative site for DNA vaccination and to compare the strength of the immune response to that induced by ␤-gal expressing tumor cells.…”

Section: Introductionmentioning

confidence: 99%

Superiority of the ear pinna over muscle tissue as site for DNA vaccination

Förg

Hoegen

Dalemans³

et al. 1998

Gene Ther

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Three different vaccination sites were compared for expression vector used. The cytomegalus virus promoter efficiency of immunization with naked DNA. Using the bacdriven pCMV␤ vector was superior to the Moloney murine terial lacZ gene as a model, all three sites of the mouse leukemia virus LTR driven BAG vector. LacZ DNA immuni-(skeletal muscle, dermis of abdominal skin or of the ear zation was also compared with cell-based vaccination with pinna) could express the gene product ␤-gal but varied in lacZ-transfected tumor cells, in which case again the pinna expression time with muscle tissue showing the longest was the best site for inducing strong immune responses. expression. Expression time, however, did not correlateTumor-specific T cell responses could also be well induced with immune response intensity. The ear pinna was by far in the pinna, leading to cytotoxic T lymphocyte induction the most effective and muscle the least effective priming and protective antitumor immunity. Thus, the pinna was site for specific humoral and cytotoxic T cell-mediated found to be a privileged site for induction of antitumor immune responses. Following intra-pinna DNA inoculation, responses and for genetic immunization, an important find-␤-gal expressing cells were detectable around the injection ing of immediate practical and potential future clinical site and in the major draining lymph node. Efficiency of implications. immunization was also dependent on the promoter and

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Antigenic variation in cancer metastasis: immune escape versus immune control

Cited by 78 publications

References 91 publications

The alpha 4 integrin chain is a ligand for alpha 4 beta 7 and alpha 4 beta 1.

The alpha 4 integrin chain is a ligand for alpha 4 beta 7 and alpha 4 beta 1.

Metastatic potential severely altered by changes in tumor cell adhesiveness and cell-surface sialylation.

Superiority of the ear pinna over muscle tissue as site for DNA vaccination

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