Analysis of cellular expression of gangliosides by gene transfection II: rat 3Y1 cells transformed with several DNAs containing oncogenes ( ,  ,   &amp; ) invariably express sialosylparagloboside

Nakaishi, Hitoshi; Sanai, Yutaka; Shibuya, Masabumi; Nagai, Yoshitaka

doi:10.1016/0006-291x(88)90457-3

Cited by 18 publications

(5 citation statements)

References 23 publications

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“…GD3 has been known to be a unique antigen found in extremely proliferating cells such as fetal brain tissues at earlier stages of development [7], and mitogen-activated T lymphocytes [8,9]. It was also induced in a fibroblast cell line after the introduction of an activated intranuclear type oncogenes [10]. Thus, it has been long suggested that GD3 expression reflects the cell nature having extremely proliferating/activating characteristics.…”

Section: Ganglioside Expression In Human Melanomasmentioning

confidence: 99%

Molecules in the signaling pathway activated by gangliosides can be targets of therapeutics for malignant melanomas

Hamamura¹,

Nakashima²,

Furukawa³

2008

Proteomics

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There have been a number of studies on tumor-specific glycolipid antigens. In particular, neuroectoderm-derived cancers express characteristic ganglioside antigens, some of them have been used as tumor markers and/or target of immunotherapy. Molecules in the signaling pathway activated by gangliosides have been analyzed. Here, we reported results on the functions of molecules involved in the signaling pathway to enhance malignant properties of human melanomas under GD3 expression, and emphasized that those molecules including tumor-associated antigens can be targets of therapeutics for malignant melanomas.

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Section: Ganglioside Expression In Human Melanomasmentioning

confidence: 99%

Molecules in the signaling pathway activated by gangliosides can be targets of therapeutics for malignant melanomas

Hamamura¹,

Nakashima²,

Furukawa³

2008

Proteomics

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“…Although the relative activities of the glycosyltransferases may )nfirmed by other account for some of the inter-and intra-site heterogeneity in uizen et al [17] glycoproteins [50][51][52][53][54][55], the recognition of other influential factors ain one and two has led to the development of two principal models. The )f the percentage 'accessibility' model [27][28][29] proposes that the extent of process-I in these species.…”

Section: The Ur-fractionmentioning

confidence: 99%

Analysis of the five glycosylation sites of human α1-acid glycoprotein

Treuheit

Costello

Halsall

1992

Biochemical Journal

162

113

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Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains. Subfractionation of OMD into three molecular variants using concanavalin A lectin chromatography is based on variations in these complex structures. Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants. The ability to quantify the glycoforms present at each site allows us to extend the earlier results of others and resolve the remaining questions concerning the glycan structures of these variants. Most significantly, the proportions of bi-, tri- and tetra-antennary chains differ at each site for the three molecular variants. The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains. Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants. In addition, the two gene products of OMD were differentially glycosylated. Molecular masses of the glycoforms were verified by matrix-assisted u.v. laser desorption mass spectrometry. On the basis of the site distribution of oligosaccharides in the variants, efforts were made to understand the factors that control the processing of the carbohydrate chains in OMD. The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.

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“…It can be induced in human T lymphocytes by stimulating with Concanavalin A or interleukin 2 ( Yamashiro et al 1995 ). It is also induced in fibroblasts introduced with oncogenic ras gene ( Nakaishi et al 1988 ). GD3 has been considered to be a melanoma-associated tumor antigen ( Furukawa and Lloyd 1990 ), and been used as a target of antibody therapy in melanoma patients ( Houghton et al 1985 ).…”

mentioning

confidence: 99%

Disruption of GM2/GD2 synthase gene resulted in overt expression of 9‐O‐acetyl GD3 irrespective of Tis21¹

Furukawa

Aixinjueluo

Kasama

et al. 2008

Journal of Neurochemistry

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GM2/GD2 synthase gene knockout mice lack all complex gangliosides, which are abundantly expressed in the nervous systems of vertebrates. In turn, they have increased precursor structures GM3 and GD3, probably replacing the roles of the depleted complex gangliosides. In this study, we found that 9‐O‐acetyl GD3 is also highly expressed as one of the major glycosphingolipids accumulating in the nervous tissues of the mutant mice. The identity of the novel component was confirmed by neuraminidase treatment, thin layer chromatography‐immunostaining, two‐dimensional thin layer chromatography with base treatment, and mass spectrometry. All candidate factors reported to be possible inducer of 9‐O‐ acetylation, such as bitamine D binding protein, acetyl CoA transporter, or O‐acetyl ganglioside synthase were not up‐regulated. Tis21 which had been reported to be a 9‐O‐acetylation inducer was partially down‐regulated in the null mutants, suggesting that Tis21 is not involved in the induction of 9‐O‐acetyl‐GD3 and that accumulated high amount of GD3 might be the main factor for the dramatic increase of 9‐O‐acetyl GD3. The ability to acetylate exogenously added GD3 in the normal mouse astrocytes was examined, showing that the wild‐type brain might be able to synthesize very low levels of 9‐O‐acetyl GD3. Increased 9‐O‐acetyl GD3, in addition to GM3 and GD3, may play an important role in the compensation for deleted complex gangliosides in the mutant mice.

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Analysis of cellular expression of gangliosides by gene transfection II: rat 3Y1 cells transformed with several DNAs containing oncogenes ( , , & ) invariably express sialosylparagloboside

Cited by 18 publications

References 23 publications

Molecules in the signaling pathway activated by gangliosides can be targets of therapeutics for malignant melanomas

Molecules in the signaling pathway activated by gangliosides can be targets of therapeutics for malignant melanomas

Analysis of the five glycosylation sites of human α1-acid glycoprotein

Disruption of GM2/GD2 synthase gene resulted in overt expression of 9‐O‐acetyl GD3 irrespective of Tis21¹

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Analysis of cellular expression of gangliosides by gene transfection II: rat 3Y1 cells transformed with several DNAs containing oncogenes ( , , & ) invariably express sialosylparagloboside

Cited by 18 publications

References 23 publications

Molecules in the signaling pathway activated by gangliosides can be targets of therapeutics for malignant melanomas

Molecules in the signaling pathway activated by gangliosides can be targets of therapeutics for malignant melanomas

Analysis of the five glycosylation sites of human α1-acid glycoprotein

Disruption of GM2/GD2 synthase gene resulted in overt expression of 9‐O‐acetyl GD3 irrespective of Tis211

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Disruption of GM2/GD2 synthase gene resulted in overt expression of 9‐O‐acetyl GD3 irrespective of Tis21¹