Metastatic potential of murine fibrosarcoma cells is influenced by cell surface laminin

1984 ◽  
Vol 33 (5) ◽  
pp. 651-655 ◽  
Author(s):  
Herbert L. Malinoff ◽  
J. Philip McCoy ◽  
James Varani ◽  
Max S. Wicha
Keyword(s):  
Cell Surface ◽  
Metastatic Potential ◽  
Fibrosarcoma Cells ◽  
Murine Fibrosarcoma

Cell surface and nuclear changes during TNF-α-induced apoptosis in WEHI 164 murine fibrosarcoma cells

1998 ◽  
Vol 433 (1) ◽  
pp. 75-83 ◽  
Author(s):  
A. D. Katsen ◽  
B. Vollmar ◽  
P. Mestres-Ventura ◽  
M. D. Menger
Keyword(s):  
Cell Surface ◽  
Tnf Α ◽  
Fibrosarcoma Cells ◽  
Nuclear Changes ◽  
Murine Fibrosarcoma ◽  
Induced Apoptosis

Effect of glycosylation inhibitors on N-glycosylpeptides and on invasion of malignant mouse MO4 cells in vitro

1990 ◽  
Vol 95 (2) ◽  
pp. 279-286
Author(s):  
E.A. Bruyneel ◽  
M. De Mets ◽  
C.H. Dragonetti ◽  
R.J. Hooghe ◽  
S. Di Virgilio ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cell Surface ◽  
Apparent Molecular Weight ◽  
Metabolic Labeling ◽  
Intact Cells ◽  
Fibrosarcoma Cells ◽  
Chick Heart ◽  
Embryonic Chick Heart ◽  
Murine Fibrosarcoma

Cell surface glycans are believed to play a role in tumour invasion and metastasis. Yet, we have previously shown that the inhibitors of N-linked glycan processing swainsonine (SW) and 1-deoxynojirimycin (dNM) did not prevent invasion of chick heart fragments by MO4 murine fibrosarcoma cells in organ culture. We now present biochemical evidence that these and other inhibitors of processing were indeed effective in remodeling glycans, including those expressed at the cell surface. After metabolic labeling with tritiated mannose or fucose, glycosylpeptides were obtained by Pronase treatment of material released from intact cells by trypsin. Glycosylpeptides were separated by Biogel P-10 chromatography. With all drugs tested, there was a shift towards lower molecular weight of the glycan chains. There were, however, major quantitative differences between the different drugs and also, for monensin (MON; 0.1 microgram ml-1), between fucose-labeled and mannose-labeled chains. The shift in apparent molecular weight affected mainly fucose-labeled peptides after treatment of MO4 cells with SW (0.4 microgram ml-1). The shift induced by dNM (10 mM) + SW (0.4 microgram ml-1) in both fucosylated and mannosylated chains was much larger than that induced by SW given alone. 1-Deoxymannojirimycin (dMM; 1 mM) had major effects on both mannose and fucose-labeled structures and so did N-methyl-1-deoxynojirimycin (MdNM; 2 mM) and castanospermine (CS; 100 micrograms ml-1). With the latter drugs, incorporation of fucose in complex-type glycosylpeptides was dramatically reduced. The effect of SW on fucose-labeled glycosylpeptides of embryonic chick heart was similar to that observed on MO4 cells.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells.

1983 ◽  
Vol 96 (5) ◽  
pp. 1475-1479 ◽  
Author(s):  
H L Malinoff ◽  
M S Wicha
Keyword(s):  
Molecular Weight ◽  
Cell Surface ◽  
Cell Surface Receptor ◽  
Receptor Protein ◽  
High Affinity ◽  
Fibrosarcoma Cells ◽  
Surface Receptor ◽  
Murine Fibrosarcoma ◽  
Laminin Binding Protein ◽  
Laminin Binding

We used affinity chromatography to isolate a specific laminin-binding protein from murine fibrosarcoma cells. These cells bind exogenous laminin to their surface with high affinity (Kd = 2 X 10(-9)M for laminin) with approximately 5 X 10(4) sites per cell. Laminin affinity chromatography of [35S]methionine-labeled cell extracts produced two distinct proteins. One was identified as Type IV (basement membrane) collagen based on its migration pattern on SDS gels and bacterial collagenase sensitivity. The other protein, which migrates as a single band or closely spaced doublet on reduced SDS gels, has a reduced molecular weight of 69,000. Using a nitrocellulose filter disk assay, we found that the latter protein specifically bound 125I-laminin with the same high affinity (Kd = 2 X 10(-9)M for laminin) as did intact fibrosarcoma cells. By iodinating intact cells, we demonstrated that this laminin-binding protein is on the cell surface. We conclude that this protein with reduced molecular weight of 69,000 is a subunit or component of a larger cell surface receptor protein for laminin in this fibrosarcoma model. This laminin receptor may mediate the interaction of the cell with its extracellular matrix.

Identification of a laminin-like substance on the surface of high-malignant murine fibrosarcoma cells

1984 ◽  
Vol 65 (1) ◽  
pp. 139-151
Author(s):  
J.P. McCoy ◽  
R.V. Lloyd ◽  
M.S. Wicha ◽  
J. Varani
Keyword(s):  
Cell Surface ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Rabbit Serum ◽  
Enzyme Linked Immunosorbent Assay ◽  
Immunoperoxidase Staining ◽  
Normal Rabbit Serum ◽  
Malignant Cells ◽  
Fibrosarcoma Cells ◽  
Murine Fibrosarcoma

High- and low-malignant murine fibrosarcoma cells were stained with anti-laminin antibodies using immunoperoxidase techniques and examined by electron microscopy. With the high-malignant cells, specific staining was observed along the cell surface. Use of normal rabbit serum in place of the rabbit anti-laminin or pretreatment of the anti-laminin with soluble laminin completely eliminated this staining. No immunoperoxidase staining was observed with the low-malignant cells. In additional studies, membrane fractions were prepared from the high- and low-malignant cells and used to immunize rabbits. The animals immunized with the membrane fractions from the high-malignant cells produced antibodies that reacted by enzyme-linked immunosorbent assay (ELISA) with murine laminin obtained from the EHS sarcoma. The animals immunized with membrane fractions from the low-malignant cells did not. These studies provide strong evidence that the high-malignant cells (but not the low) express on their cell surface a substance that is immunologically cross-reactive with laminin. In addition, the high-malignant cells (but not the low) secreted a material into the cell culture fluid that could be specifically immunoprecipitated with antilaminin antibodies. The immunoprecipitated material co-migrated with purified laminin when examined by sodium dodecyl sulphate/polyacrylamide gel electrophoresis under reducing conditions. The existence of this substance associated with the surface of the high-malignant cells and its absence from that of the low-malignant cells may explain the previously noted difference between these cells in their ability to attach to type IV collagen. This difference may also contribute to the dissimilarity between these cells in their metastatic potential.

scholarly journals Enhanced Expression of Type IV Collagen-binding Protein (p29) inFyn-transfected Murine Fibrosarcoma Cells

2002 ◽  
Vol 93 (10) ◽  
pp. 1090-1099 ◽  
Author(s):  
Kazuhiko Koike ◽  
Katsuhisa Kogawa ◽  
Tetsuji Takayama ◽  
Naohito Yoshizaki ◽  
Hirohito Muramatsu ◽  
...  
Keyword(s):  
Type Iv Collagen ◽  
Binding Protein ◽  
Collagen Binding ◽  
Type Iv ◽  
Fibrosarcoma Cells ◽  
Enhanced Expression ◽  
Murine Fibrosarcoma

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

1983 ◽  
Vol 157 (1) ◽  
pp. 371-376 ◽  
Author(s):  
M Fogel ◽  
P Altevogt ◽  
V Schirrmacher
Keyword(s):  
Sialic Acid ◽  
Cell Surface ◽  
Tumor Cell ◽  
Metastatic Potential ◽  
Lectin Receptors ◽  
Lectin Receptor ◽  
Receptor Sites ◽  
Variant Line

A plastic adherent variant line (ESb-M) of a highly invasive and metastatic murine T cell lymphoma (ESb) was found to have lost its metastatic potential while still being tumorigenic in normal syngeneic hosts. The variant retained most of its ESb-derived antigenic and biochemical characteristics but differed at binding sites for certain lectins with specificity for terminal N-acetylgalactosamine residues. Whereas such sites were masked by sialic acid on metastatic ESb cells, they became unmasked on the adherent variant line. Metastatic revertants of ESb-M cells did not express the respective lectin receptor sites because these were again masked by sialic acid. It is suggested that the masking of specific lectin receptors sites on the tumor cell surface is of crucial importance for metastatis. If freely exposed, these sites may change adherence characteristics of the cells possibly not only in vitro (to plastic) but also in vivo.

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