Cell contact-dependent ganglioside changes in mouse 3T3 fibroblasts and a suppressed sialidase activity on cell contact

Yogeeswaran, Ganesa; Hakomori, Sen‐itiroh

doi:10.1021/bi00681a017

Cited by 100 publications

(28 citation statements)

References 32 publications

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“…The presence of fibronectin on the cell surface is also reduced with transformation (30)(31)(32). On the other hand, GDia synthesis increases in certain cultured cells where their cell-to-cell contacts are increased (33,34), and fibronectin accumulation also increases at high cell density (35). Recently, it has been reported that glycolipids mediate intercellular adhesion (36).…”

Section: Resultsmentioning

confidence: 99%

Ganglioside inhibition of fibronectin-mediated cell adhesion to collagen.

Kleinman¹,

Martin²,

Fishman³

1979

Proc. Natl. Acad. Sci. U.S.A.

239

107

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Fibronectin mediates the adhesion of cells to col1agen by first binding to the collagen substrate, followed by attachment of the cells to the fibronectin-collagen complex. Bovine brain gangliosides were found to block fibronectinmediated cell adhesion to collagen in a concentration-dependent manner. The gangliosides did not block the binding of fibronectin to collagen but did prevent the attachment of the cells to the fibronectin-collagen complex. Of the individual gangliosides tested, GT1 and GDia were the most effective inhibitors followed by GD1b >> GM1 >> GM2; GM3 was not an inhibitor. The inhibition of cell adhesion also was observed with the oligosaccharide portion of the gangliosides, but not with ceramides or with a variety of free sugars or glycosaminoglycans. Mild periodate oxidation of mixed gangliosides or of GDia modified their sialic acid residues and the oxidized gangliosides were no longer inhibitory; subsequent reduction with NaBH4 did not restore the inhibitory activity of the modified gangliosides. These results suggest that specific gangliosides or related sialic acid-containing glycoconjugates on the cell surface may act as the receptors for fibronectin. Most cells require an appropriate substratum for growth in culture. A variety of cells use fibronectin, a large extrinsic matrix protein to adhere either to plastic (1) or to collagen substrates (2). An identical or very similar protein, cold insoluble globulin, is present in serum, and the serum form of fibronectin promotes the attachment of freshly trypsinized cells. Fibronectin prepared from either cells or serum is equally active in promoting cell attachment (3). With collagen substrates, fibronectin binds to the collagen substratum first (2, 4). Then the cells, in the presence of Ca2+ or Mg2+ in an energy-dependent process (5), adhere to the fibronectin-collagen complex. Fibronectin binds to all mammalian collagens that have been tested so far and it also binds to fibrin (6). In the al(I) chain of collagen, it binds to a specific amino acid sequence lacking carbohydrate (7)(8)(9)(10). These interactions are not cation dependent and can be broken by 1 M KBr (11) or 6 M urea (12). Fibrinogen (13) and collagen affinity columns (11, 12) have proved useful in the purification of fibronectin from serum and from conditioned culture medium.Little is known about the interaction of fibronectin with the cell surface or the nature of the membrane component(s) to which fibronectin binds. One approach to their identification is to test various cell surface components for their ability to interact with the fibronectin-collagen complex and thereby prevent cell attachment. Gangliosides are well-defined membrane components, and a specific ganglioside, GM,, functions as the membrane receptor for cholera toxin (14). This role for GM, was elucidated from the original observation that gangliosides block the biological effects of the toxin (15). We now report that certain gangliosides block cell adhesion promoted by the fibronectin in serum.MATERIALS ...

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Section: Resultsmentioning

confidence: 99%

Ganglioside inhibition of fibronectin-mediated cell adhesion to collagen.

Kleinman¹,

Martin²,

Fishman³

1979

Proc. Natl. Acad. Sci. U.S.A.

239

107

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“…The column was washed extensively with CHCl 3 and the glycolipid fraction eluted with CH 3 COCH 3 /CH 3 OH (9:1) (22). Gangliosides were separated from pooled upper and lower phases by DEAE-Sephadex G-25 chromatography and eluted using 0.4 M ammonium acetate in methanol (23).…”

Section: Gsl Extractionmentioning

confidence: 99%

Role of Multiple Drug Resistance Protein 1 in Neutral but Not Acidic Glycosphingolipid Biosynthesis

Rosa

Sillence

Ackerley

et al. 2004

Journal of Biological Chemistry

107

109

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MDR1a, 1b, MRP1) mouse fibroblasts showed the same loss of neutral glycosphingolipid (glucosyl ceramide, lactosyl ceramide) but not ganglioside (GM3) synthesis, confirming the proposed role for MDR1 translocase activity. Cryo-immunoelectron microscopy showed MDR1 was predominantly intracellular, largely in rab6-containing Golgi vesicles and Golgi cisternae, the site of glycosphingolipid synthesis. These studies identify MDR1 as the major glucosyl ceramide flippase required for neutral glycosphingolipid anabolism and demonstrate a previously unappreciated dichotomy between neutral and acid glycosphingolipid synthesis.

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“…Alterations of the levels of ganglioside sialidase expression associated with malignant transformation have been described in 3T3-transformed cells (14) and in BHK-transformed cells. (15) However, little was known about the mechanisms by which sialidase was altered in these systems until ganglioside sialidase clones became available.…”

mentioning

confidence: 99%

Membrane sialidase NEU3 is highly expressed in human melanoma cells promoting cell growth with minimal changes in the composition of gangliosides

Miyata¹,

Kambe²,

Tajima³

et al. 2011

Cancer Science

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NEU3 is a membrane sialidase specific for gangliosides. Its increased expression and implication in some cancers have been reported. Here, we analyzed NEU3 expression in malignant melanoma cell lines and its roles in the cancer phenotypes. Quantitative RT-PCR revealed that high levels of the NEU3 gene were expressed at almost equivalent levels with those in colon cancers. To examine the effects of overexpression of NEU3, NEU3 cDNA-transfectant cells were established using a melanoma cell line SK-MEL-28 and its mutant N1 lacking GD3. SK-MEL-28 sublines overexpressing both the NEU3 gene and NEU3 enzyme activity showed no changes in both cell growth and ganglioside expression, while N1 cells showed a mild increase in cell proliferation with increased phosphorylation of the EGF receptor and neo-synthesis of Gb3 after NEU3 transfection. In contrast, NEU3 silencing resulted in a definite reduction in cell growth in a melanoma line MeWo, while ganglioside patterns underwent minimal changes. Phosphorylation levels of ERK1 ⁄ 2 with serum stimulation decreased in the NEU3-silenced cells. All these results suggest that NEU3 is highly expressed to enhance malignant phenotypes including apoptosis inhibition in malignant melanomas. (Cancer Sci 2011; 102: 2139-2149

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Cell contact-dependent ganglioside changes in mouse 3T3 fibroblasts and a suppressed sialidase activity on cell contact

Cited by 100 publications

References 32 publications

Ganglioside inhibition of fibronectin-mediated cell adhesion to collagen.

Ganglioside inhibition of fibronectin-mediated cell adhesion to collagen.

Role of Multiple Drug Resistance Protein 1 in Neutral but Not Acidic Glycosphingolipid Biosynthesis

Membrane sialidase NEU3 is highly expressed in human melanoma cells promoting cell growth with minimal changes in the composition of gangliosides

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