FBJ virus-induced osteosarcoma has type V collagen consisting of A, B and C-like chains in addition to type I collagen

Yamagata, Sadako; Miwa, Mayumi; Tanaka, Kyoko; Yamagata, Toshio

doi:10.1016/0006-291x(82)91097-x

Cited by 13 publications

(5 citation statements)

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“…The capacity for FBJ-LL cells to migrate was ten times that of FBS-S1 cells, but decreased by a half by treatment with GD1a [1]. FBJ-LL cells mestasized into the liver and lung, but FBJ-S1 did not [36]. LA5-22, LA5-30 cells were obtained by transfection of FBJ-LL cells with β1-4GalNAcT-1 (GM2/GD2-synthase), and mock-transfectant M5 cells, as control [3].…”

Section: Cell Lines and Culturementioning

confidence: 92%

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Ganglioside GD1a regulation of caveolin-1 and Stim1 expression in mouse FBJ cells:Augmented expression of caveolin-1 and Stim1 in cells with increased GD1a content

et al. 2006

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GD1a was previously shown responsible for regulating cell motility, cellular adhesiveness to vitronectin, phosphorylation of c-Met and metastatic ability of mouse FBJ osteosarcoma cells. To determine the particular molecules regulated by GD1a, FBJ cells were assessed for tumor-related gene expression by semi-quantitative RT-PCR. Caveolin-1 and stromal interaction molecule 1 (Stim1) expression in FBJ-S1 cells, rich in GD1a, were found to be 6 and 4 times as much, respectively, than in FBJ-LL cells devoid of GD1a. Enhanced production of caveolin-1 in protein was confirmed by Western blotting. A low-metastatic FBJ-LL cell variant, having high GD1a expression through beta1-4GalNAcT-1 (GM2/GD2 synthase) cDNA transfection (Hyuga S, et al, Int J Cancer 83: 685-91, 1999), showed enhanced production of caveolin-1 and Stim1 in mRNA and protein, compared to mock-transfectant M5. Incubation of FBJ-M5 cells with exogenous GD1a augmented the expression of caveolin-1 in mRNA and protein and Stim1 in mRNA as well. Treatment of FBJ-S1 with fumonisin B1, an inhibitor of N-acylsphinganine synthesis, for 15 days caused the complete depletion of gangliosides and suppressed the expression of caveolin-1 and Stim1. St3gal5 siRNA transfected cells showed decreased expression of caveolin-1 and Stim1 mRNA, as well as St3gal5 mRNA. These findings clearly indicate ganglioside GD1a to be involved in the regulation of the transformation suppressor genes, caveolin-1 and Stim1. Moreover, treatment with GD1a of mouse melanoma B16 cells and human hepatoma HepG2 cells brought about elevated expression of caveolin-1 and Stim1.

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Section: Cell Lines and Culturementioning

confidence: 92%

“…The highly metastatic mouse osteosarcoma cell line, FBJ-LL, and poorly metastatic cell line, FBJ-S1, were produced from a FBJ virus-induced osteosarcoma of the BALB/c mouse [36,37]. FBJ-S1 cells expressed GM3 and GD1a, whereas FBJ-LL cells expressed GM3 and slightly expressed GD1a [1].…”

Section: Cell Lines and Culturementioning

confidence: 99%

Ganglioside GD1a regulation of caveolin-1 and Stim1 expression in mouse FBJ cells:Augmented expression of caveolin-1 and Stim1 in cells with increased GD1a content

et al. 2006

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“…The highly metastatic FBJ-LL cells metastasized into the liver and lung, but FBJ-S1 did not (Yamagata et al, 1982). The cells were maintained in medium containing RPMI 1640 (Nissui, Tokyo, Japan) supplemented with 10% FCS (GIBCO BRL, Grand Island, NY) and cultured at 37°C in a humidified atmosphere of 95% air and 5% CO 2 .…”

Section: Cell Lines and Culturementioning

confidence: 99%

Suppression by ganglioside GD1A of migration capability, adhesion to vitronectin and metastatic potential of highly metastatic FBJ-LL cells

et al. 1999

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“…The highly metastatic FBJ-LL cells metastasize into the liver and lung, but FBJ-S1 cells do not metastasize at all. 13 These cells were cultured in medium containing RPMI-640 (Nissui, Tokyo, Japan) supplemented with 10% FCS (GIBCO BRL, Grand Island, NY) at 37°C in a humidified atmosphere of 95% air and 5% CO 2 . GM2/GD2-synthase cDNA transfectants (LA5-7 and LA5-22) and mock-transfectant M-5 cell 7 were cultured in RPMI-1640 supplemented with 10% FCS and 100 g/ml Geneticin (GIBCO BRL).…”

Section: Cell Lines and Culturementioning

confidence: 99%

Ganglioside GD1a inhibits HGF-induced motility and scattering of cancer cells through suppression of tyrosine phosphorylation of c-Met

Hyuga¹,

Kawasaki²,

Hyuga³

et al. 2001

Int. J. Cancer

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We previously reported that ganglioside GD1a, which is highly expressed in poorly metastatic FBJ-S1 cells, inhibits the serum-induced motility of FBJ-LL cells and that the metastatic potential of FBJ-LL cells is completely suppressed by enforced GD1a expression (Hyuga et al., Int J Cancer 1999; 83:685-91). We recently discovered that hepatocyte growth factor (HGF) induces FBJ-LL cell motility. In the present study, the HGF-induced motility of FBJ-S1 cells was found to be one-thirtieth that of FBJ-LL cells. This motility of GD1a-expressing transfectants, which were produced by transfection of FBJ-LL cells with GM2/GD2 synthase cDNA, decreased with increases in their GD1a expression and HGF induced almost no motility in GD1a-pretreated FBJ-LL cells, indicating that GD1a inhibits the HGF-induced motility of GD1a; HGF; motility; scattering Gangliosides are sialylated glycosphingolipids found on the outer layer of the plasma membrane. Changes in ganglioside expression in cancer cells are strongly related to their metastatic potential. 1-5 Although increases in complex ganglioside expression in cancer cells have been considered to be associated with malignancy, in our previous study we found that the poorly metastatic FBJ-S1 cells highly expressed the complex ganglioside GD1a, whereas the highly metastatic FBJ-LL cells only slightly expressed this ganglioside. 6 GD1a inhibited the serum-induced motility of FBJ-LL cells and the metastatic potential of FBJ-LL cells was completely suppressed by enforced GD1a expression. 7 It is possible that GD1a suppresses metastasis of FBJ-LL cells by inhibiting cell migration. The target molecules of GD1a need to be identified to clarify the mechanism of inhibition of metastasis by GD1a. Key words:We recently found that HGF induces FBJ-LL cell motility 8 and that the serum-induced motility of FBJ-LL cells was decreased by treatment of the serum with anti-HGF antibody (unpublished data), suggesting that HGF is a migration-stimulating factor in serum. Since FBJ-LL cells metastasize to the liver and HGF is secreted by nonparenchymal liver cells, HGF may promote liver metastasis of FBJ-LL cells. We suspect that HGF may play a key role in FBJ-LL cell metastasis. HGF is a multipotential modulator of biologic activities in a variety of cell types and it influences the growth, motility, differentiation and morphogenesis of its target cells through the c-Met tyrosine kinase receptor. 9 HGF has been described as a potent chemotactic factor 10 and has been associated with the progression of carcinoma cells. 11 Overexpression of the HGF receptor, c-Met, in malignant cells has been reported in various tissues. 12 Hence HGF may play a crucial role in cancer metastasis.In the present study, we attempted to identify the target molecules of GD1a by analyzing the molecular mechanism of the inhibition of cell migration by GD1a. We found that GD1a inhibited the HGFinduced motility, morphologic change and formation of actin stress fibers in FBJ-LL cells through suppression of tyrosine phosphorylation ...

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FBJ virus-induced osteosarcoma has type V collagen consisting of A, B and C-like chains in addition to type I collagen

Cited by 13 publications

References 14 publications

Ganglioside GD1a regulation of caveolin-1 and Stim1 expression in mouse FBJ cells:Augmented expression of caveolin-1 and Stim1 in cells with increased GD1a content

Ganglioside GD1a regulation of caveolin-1 and Stim1 expression in mouse FBJ cells:Augmented expression of caveolin-1 and Stim1 in cells with increased GD1a content

Suppression by ganglioside GD1A of migration capability, adhesion to vitronectin and metastatic potential of highly metastatic FBJ-LL cells

Ganglioside GD1a inhibits HGF-induced motility and scattering of cancer cells through suppression of tyrosine phosphorylation of c-Met

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