Altered surface glycoproteins in melanoma cell variants with reduced metastasizing capacity selected for resistance to wheat germ agglutinin

Jumblatt, James E.; Tao, Tien-Wen; Schlup, Verena; Finne, Jukka; Burger, Max M.

doi:10.1016/0006-291x(80)90711-1

Cited by 20 publications

(3 citation statements)

References 8 publications

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“…The parental and the variant cells presented in this study showed great similarities in some basic characteristics: (1) they remained tumor cells; (2) they remained melanin-producing and releasing cells; (3) their growth rates were similar not only in vitro but also in vivo (Tao and Burger, 1982); (4) the major cellular proteins were similar as analyzed by SDS polyacrylamide slab gel electrophoresis (Jumblatt et al, 1980;Finne et al, 1980). On the other hand, some alterations were displayed by the variant cells as summarized in Table IV. Both lectin-resistant lines which displayed lower metastasis were found to have an approximately 50 % DNA increase which is reflected in an approximately 50 % increase in chromosome numbers, restricted however to mostly five of the 19 autosomal chromo- somes.…”

Section: Discussionmentioning

confidence: 66%

“…The change in a carbohydrate adding enzyme (Finne et al, 1982) and consequently in a specific tetraantennary oligosaccharide seemed to correlate with lymphatic metastasis, but not necessarily with hematogenous metastasis. The possible role that surface sialic acid may play in malignancy has been discussed in other papers (Jumblatt et al, 1980;Finne et al, 1980;Yogeeswaren and Tao, 1980) and is beyond the scope of this report.…”

Section: Discussionmentioning

confidence: 84%

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Lectin‐resistant variants of mouse melanoma cells. II. In vitro characteristics

Tao

Jenkins

Vosbeck

et al. 1983

Intl Journal of Cancer

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Lectin-resistant variants of B-16 melanoma cells were selected with wheat-germ agglutinin, ricin and concanavalin A. They exhibited altered metastasizing capacity and tumorigenicity in C57BL mice. Several in vitro properties were defined and compared including homotypic adhesiveness, microfilament organization, melanin release, activity of tyrosine hydroxylase, DNA content, and karyotypes. The possible relevance of these properties in vitro for the malignant behavior displayed in vivo is discussed. The usefulness of this approach of selecting surface variants to study the problem of metastasis is also discussed.

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Section: Discussionmentioning

confidence: 66%

Section: Discussionmentioning

confidence: 84%

Lectin‐resistant variants of mouse melanoma cells. II. In vitro characteristics

Tao

Jenkins

Vosbeck

et al. 1983

Intl Journal of Cancer

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“…Poorly tumorigenic lectin-resistant variants isolated from highly metastatic tumor cells have been widely used to characterize specific changes in cell-surface glycoproteins which parallel the loss of metastatic potential (Jumblatt et al, 1980;Tao and Burger, 1982;Dennis, 1986;Dennis and Laferte, 1986). Increase of sialic acid content of cell membranes and acquisition of metastatic properties are closely correlated (Yogeeswaran el al., 1979;Yogeeswaran and Tao, 1980;Yogeeswaran and Salk, 1981;Collard et al, 1986;Irimura et al, 1986).…”

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confidence: 99%

Hyposialylation of high‐molecular‐weight membrane glycoproteins parallels the loss of metastatic potential in wheat‐germ agglutinin‐resistant friend leukemia cells

Benedetto¹,

Elia

Sala

et al. 1989

Intl Journal of Cancer

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From the highly metastatic in vivo-passaged Friend leukemia cells (FLC), WGA-resistant (WR) tumor cell variants were selected. These WR FLC had lost their capacity to metastasize when injected i.v. or s.c. into DBA/2 mice. We have characterized the plasma membrane glycoproteins of the different FLC types by: (i) metabolic labelling with (3H)-galactose; (ii) surface labelling with galactose oxidase-borohydride; (iii) direct binding of (125I)-lectins on glycoproteins separated by SDS-PAGE. The ensemble of these approaches showed that the 100- to 200-kDa glycoproteins of in vivo-passaged FLC and WR FLC exhibited a very similar distribution of the terminal galactose in their oligosaccharide moieties. In contrast, the expression of terminal sialic acid was reduced in WR FLC with respect to in vivo-passaged counterparts as appreciated by: (i) binding experiments with (125I)-WGA; (ii) cathodic shift of the 100- to 200-kDa glycoproteins in 2-dimensional electrophoresis studies, and (iii) thiobarbituric acid assay after FLC treatment with neuraminidase. Moreover, binding experiments with (125I)-LPHA, (125I)-ConA and (125I)-WGA (after Smith degradation) indicated that, in the 100- to 200-kDa region, virtually identical asparagine-linked tri- or tetra-antennary complex-type oligosaccharides were expressed in both cell types. We conclude that the sialylation of high-molecular-weight surface glycoproteins (particularly in the 150-kDa region) is strongly associated with the metastatic potential of FLC, especially to the liver.

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The effects of monensin on blood‐borne arrest and glycosylation of BL/VL3 lymphoma cells

Virgilio

Rampelberg

Greimers

et al. 1992

Cell Biochemistry & Function

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We have previously shown that inhibitors of N-glycan processing alter both the cell surface carbohydrates and the homing properties in lymphoid cells. We have now studied the effects of the ionophore monensin (MON) on these parameters. Arrest in the spleen of [111In]-labelled BL/VL3 murine T lymphoma cells, injected intravenously was clearly reduced if the cells had been cultured for 24 h in the presence of monensin (0.1-1.0 microgram ml-1). We have characterized glycopeptides from BL/VL3 murine T lymphoma cells. Following labelling with tritiated precursors (fucose, mannose, galactose, glucosamine), surface glycopeptides from BL/VL3 murine T lymphoma cells, were released by trypsin and separated by gel filtration on Bio-Gel P6 and by affinity chromatography on immobilized lectins. After treatment with MON, a class of high molecular mass glycopeptides was no longer found. There were less complex and more high mannose glycans, as a consequence of a reduction of terminal glycosylation (sialylation, fucosylation or incorporation of N-acetyl-glucosamine). Similar findings were obtained with immunoprecipitated Thy-1 antigen. However, as estimated by flow cytometry analysis, the cell surface expression of Thy-1 was not reduced in MON-treated cells. Taken together our results show that cell surface oligosaccharides are modified dramatically, but that at least, certain cell surface antigens are present in normal amounts. It is tempting to speculate that changes in glycosylation account for the abnormal homing properties of MON-treated cells.

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Altered surface glycoproteins in melanoma cell variants with reduced metastasizing capacity selected for resistance to wheat germ agglutinin

Cited by 20 publications

References 8 publications

Lectin‐resistant variants of mouse melanoma cells. II. In vitro characteristics

Lectin‐resistant variants of mouse melanoma cells. II. In vitro characteristics

Hyposialylation of high‐molecular‐weight membrane glycoproteins parallels the loss of metastatic potential in wheat‐germ agglutinin‐resistant friend leukemia cells

The effects of monensin on blood‐borne arrest and glycosylation of BL/VL3 lymphoma cells

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