<i>In vivo</i> and <i>in vitro</i> reactivity of rat spleen cells against regressor and progressor colon‐cancer cell variants

Reisser, D; Olsson, Nils‐Olivier; Martin, François

doi:10.1002/ijc.2910530421

Cited by 18 publications

(17 citation statements)

References 25 publications

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“…We showed previously that P R O b cells share the sameTAA as R E G b cells, which is a clone of the same cancer giving rise to regressive tumors [9, 10,241. A tumor-specific, T cell-dependent immune response induces R E G b tumor regression in naive syngeneic rats and prevents P R O b tumor growth in rats immunized against R E G b cells [24].…”

Section: Discussionmentioning

confidence: 99%

Surface phenotype and functions of tumor‐infiltrating dendritic cells: CD8 expression by a cell subpopulation

et al. 1993

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Although the function and significance of tumor-infiltrating dendritic cells (TIDC) in the immune response to tumor have never been clearly demonstrated, their location suggests that they play a critical role in the presentation of tumor antigen to specific T cells. We studied the morphological and functional characteristics of interstitial dendritic cells (DC) located inside tumors obtained by injection of cancer cells into syngeneic rats. Single and double immunostaining of tumor sections revealed a dense network of cells which expressed class II major histocompatibility complex (MHC II) molecules. Cell morphology and surface markers were characteristic of DC populations in other tissues. These DC were in close contact with tumor cells and increased in number as the tumor grew larger. Unexpectedly, a subpopulation of morphologically characteristic TIDC expressed both CD8 and MHC II molecules. TIDC were purified from tumors by gradient centrifugation and immunobeads and characterized by morphology, ultrastructural study and surface markers studied by flow cytometry. TIDC were negative for the CD5 molecule (a pan T cell marker), and were not labeled with 3.2.3 monoclonal antibody (mAb) (an NK cell marker) or with Ki-M2R mAb (a macrophage marker). A subpopulation of TIDC expressed the CD8 molecule, confirming the in situ results. TIDC expressed high levels of class I and class II MHC molecules and the adhesion molecule ICAM-1. This expression is compatible with effective antigen presenting function. Purified TIDC triggered rapid and high levels of proliferation of tumor-immune T cells in vitro, demonstrating the potential of these cells to constitutively process and present tumor-associated antigens.

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Section: Discussionmentioning

confidence: 99%

Surface phenotype and functions of tumor‐infiltrating dendritic cells: CD8 expression by a cell subpopulation

et al. 1993

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“…The pancreatic adenocarcinoma lines BSp73ASML (metastasizing) and BSp73AS (low metastasizing) are sublines from a tumor spontaneously arising in the BDX rat strain (Matzku et al, 1983). Regressor and Progressor are two related colon carcinoma lines, which metastasize via the lymphatic system (Reisser et al, 1993). The bladder carcinoma line 804G was a kind gift from Dr J. Jones, Northwestern University Medical School Chicago, IL, USA (Riddelle et al, 1991).…”

Section: Methodsmentioning

confidence: 99%

The association of the tetraspanin D6.1A with the α6β4 integrin supports cell motility and liver metastasis formation

Herlevsen

Schmidt

Miyazaki

et al. 2003

Journal of Cell Science

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The metastatic subline of a rat pancreatic adenocarcinoma differs from the non-metastasizing subline by overexpression of 5 membrane molecules: CD44 variant isoforms, EpCAM, the tetraspanin D6.1A, an uPAR-related molecule and, as described here, the α6β4 integrin.An antibody-defined molecule was identified by mass spectrometry and cloning as α6β4 integrin. Transfectioninduced expression of α6β4 in the non-metastasizing subline did not support migration on laminin 5 or tumor progression. However, when the non-metastasizing subline was doubly transfected to express α6β4 and the D6.1A tetraspanin, intraperitoneally injected tumor cells frequently formed liver metastasis. For the following reasons we assume that metastasis formation is supported by an interaction between α6β4 and D6.1A. (i) The 2 molecules can associate and co-localize. (ii) Co-localization is strengthened by PKC stimulation. (iii) PKC stimulation, which induces a migratory phenotype, leads to a redistribution of α6β4/D6.1A complexes. In resting cells, the molecules co-localize at the trail of the cell; during PKC stimulation they become transiently internalized and are (re-)expressed in the leading lamella. Thus, in the appropriate milieu, i.e. intraperitoneally, α6β4 changes from an adhesion-supporting towards a migrationsupporting molecule by its association with a tetraspanin. The findings provide a convincing experimental explanation for the repeatedly described involvement of α6β4 in tumor progression.Key words: α6β4 integrin, Tetraspanin, Metastasis, Adhesion, Motility SummaryThe association of the tetraspanin D6.1A with the α6β4 integrin supports cell motility and liver metastasis formation

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“…Informed consent for tissue collection was obtained from each patient and tissue collection was approved by the University Ethics Review Board. The rat cell lines BSp73ASML (ASML) (Zöller et al, 1978), Progressor (Reisser et al, 1993) and 804G (Izumi et al, 1981) were grown in RPMI medium supplemented with 10% FCS. The embryonic kidney cell line HEK-293 was grown in Iscove's medium supplemented with 10% FCS.…”

Section: Tissues and Tumour Linesmentioning

confidence: 99%

C4.4A as a candidate marker in the diagnosis of colorectal cancer

et al. 2007

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C4.4A is a member of the Ly-6 family with restricted expression in non-transformed tissues. C4.4A expression in human cancer has rarely been evaluated. Thus, it became important to explore C4.4A protein expression in human tumour tissue to obtain an estimate on the frequency of expression and the correlation with tumour progression, the study focusing on colorectal cancer. The analysis of C4.4A in human tumour lines by western blot and immunoprecipitation using polyclonal rabbit antibodies that recognize different C4.4A epitopes revealed C4.4A oligomer and heavily glycosylated C4.4A isoform expression that, in some instances, inhibited antibody binding and interaction with the C4.4A ligand galectin-3. In addition, tumour cell lines released C4.4A by vesicle shedding and proteolytic cleavage. C4.4A was expressed in over 80% of primary colorectal cancer and liver metastasis with negligible expression in adjacent colonic mucosa, inflamed colonic tissue and liver. This compares well with EpCAM and CO-029 expression in over 90% of colorectal cancer. C4.4A expression was only observed in about 50% of pancreatic cancer and renal cell carcinoma. By de novo expression in colonic cancer tissue, we consider C4.4A as a candidate diagnostic marker in colorectal cancer, which possibly can be detected in body fluids.

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In vivo and in vitro reactivity of rat spleen cells against regressor and progressor colon‐cancer cell variants

Cited by 18 publications

References 25 publications

Surface phenotype and functions of tumor‐infiltrating dendritic cells: CD8 expression by a cell subpopulation

Surface phenotype and functions of tumor‐infiltrating dendritic cells: CD8 expression by a cell subpopulation

The association of the tetraspanin D6.1A with the α6β4 integrin supports cell motility and liver metastasis formation

C4.4A as a candidate marker in the diagnosis of colorectal cancer

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