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

  title={Hyposialylation of high‐molecular‐weight membrane glycoproteins parallels the loss of metastatic potential in wheat‐germ agglutinin‐resistant friend leukemia cells},
  author={Arrigo Benedetto and Giuliano Elia and A. Sala and F. Belardeli},
  journal={International Journal of Cancer},
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 (125l)‐lectins on glycoproteins separated by SDS‐PAGE. The… 
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The significance of hypersialylation of dipeptidyl peptidase IV (CD26) in the inhibition of its activity by Tat and other cationic peptides. CD26: a subverted adhesion molecule for HIV peptide binding.
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Inhibition of sialic acid incorporation prevents hepatic metastases.
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Oncogenes and expression of endogenous lectins and glycoconjugates
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Biologic and biochemical differences between in vitro and in vivo passaged friend erythroleukemia cells. II. Changes in cell surface glycoproteins associated with a highly malignant phenotype
It is seen that repeated in vivo passages of FLC resulted in the appearance of different patterns of membrane glycoproteins and that these changes appeared to be associated consistently with the capacity of these cells to grow as tumor ascites and to metastasize to the liver and spleen.
Cell surface sialylation of glycoproteins and glycosphingolipids in cultured metastatic variant rna‐virus transformed non‐producer BALB/c 3T3 cell lines
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Carbohydrate changes in glycoproteins of a poorly metastasizing wheat germ agglutinin-resistant melanoma clone.
Binding of 125I-labeled lectins to total cellular proteins on polyacrylamide gels following electrophoresis showed that the major wheat germ agglutinin-binding components of F1 cells were altered in Wa-4 cells, suggesting a possible basis for the glycosylation change.
CO‐reversion of a lectin‐resistant mutation and non‐metastatic phenotype in murine tumor cells
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Sialoglycoproteins of murine RAW117 large cell lymphoma/lymphosarcoma sublines of various metastatic colonization properties.
The results indicated that the in vitro selected high liver-colonizing RAW117 variants possesses high WGA r, which strongly suggests that the oligosaccharide back-bones are highly branched and asparagine-linked.
Lectin‐resistant variants of mouse melanoma cells. I. Altered metastasizing capacity and tumorigenicity
From C57BL mouse melanoma B‐16 cells, variant clones were selected in vitro which were resistant to the lectins wheat‐germ agglutinin and ricin and will be a good model for studies seeking to dissociate these two properties.
Altered surface glycoproteins in melanoma cell variants with reduced metastasizing capacity selected for resistance to wheat germ agglutinin.
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Biologic and biochemical differences between in vitro and in vivo passaged friend erythroleukemia cells. I. Tumorigenicity and capacity to metastasize
The phenotype of sensitivity or resistance to the inhibitory effect of alpha/beta mouse interferon on virus replication and cell multiplication was conserved during serial i.p. passages and maintained in the clones derived from in vivo passaged cells.
Different metastatic phenotypes in two genetic classes of wheat germ agglutinin-resistant tumor cell mutants.
  • J. Dennis
  • Biology, Medicine
    Cancer research
  • 1986
The results demonstrate that the loss of metastatic potential in WGA-resistant mutants of MDAY-D2 depends on the phenotypic class of the isolates and their characteristic changes in glycoconjugate structure.