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(searched for: doi:10.1002/jsscb.380170404)
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Leonard Weiss, F. William Orr
Published: 1 January 1992
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Jack A. Alhadeff, Mary Catherine Glick
Critical Reviews in Oncology/Hematology, Volume 9, pp 37-107; https://doi.org/10.1016/s1040-8428(89)80014-9

Abstract:
The cell surface is involved in cell growth and division, cell-cell interaction, communication, differentiation and migration, and other processes likely to be involved in malignant transformation and/or the metastatic spread of cancer. Although there are many alterations of glycoproteins and glycolipids on the malignant cell surface, it is unclear whether these alterations are epiphenomena or an integral part of the malignancy process. This article reviews the recent literature and some earlier studies relevant for understanding emerging concepts and trends with respect to malignant cell glycoconjugates. Emphasis is on structural alterations of the carbohydrate portions of malignant cell glycoproteins and glycolipids and on the enzymes (glycosyltransferases and glycosidases) involved in their metabolism. Practical applications derived from malignant cell glycoconjugate studies are discussed briefly with respect to the diagnosis, staging, monitoring, and treatment of malignant disease. The review concludes by indicating which research areas on malignant cell glycoconjugates are likely to be fruitful in increasing our basic understanding of, and ability to deal effectively with, malignant disease.
Peter A. Netland, Bruce R. Zetter
Published: 1 January 1989
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Garth L. Nicolson
Published: 1 January 1989
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Tatsuro Irimura, Motowo Nakajima, Takao Yamori, David M. Ota, Karen F. Cleary, Garth L. Nicolson
Published: 1 January 1988
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R.J. Wieser, F. Oesch
Journal of Biochemical and Biophysical Methods, Volume 15, pp 13-21; https://doi.org/10.1016/0165-022x(87)90058-3

Abstract:
In previous studies, we have shown that plasma membrane glycoproteins are of major importance in the density-dependent regulation of growth of normal diploid fibroblasts. Due to the hydrophobic portions of these molecules, functional studies in cell culture are often diffucult to perform and to interpret. Specially, the addition of these molecules in soluble form to cell culture, after depletion of detergents needed for their solubilization, leads to aggregation and internalization. Therefore, we developed a method for the covalent immobilization of the solubilized plasma membrane proteins to derivatized silica beads for further investigations on the molecular nature of the active molecules. The addition of immobilized plasma membrane glycoproteins to spasely seeded human fibroblasts resulted in cellular reactions similar to those found in confluent cell cultures (strongly reduced cell proliferation; high collagen type III synthesis). The method consists in the derivatization of silica beads (Lichrosphere Si 500, 10 μm) with isothiocyanatopropyltreithoxysilane. Amino-groups react with the SCN group under physiological conditions, resulting in a stable linkage of amino-group bearing molecules with the silica beads. Due to the easy handling of the silica beads (e.g. washing by short centrifugation steps), the mild coupling conditions, and the stable bondings this system is highly suited for functional studies of molecules involved in cell-cell interactions.
, K Matsumoto, S L White, K Olden
Journal of the National Medical Association, Volume 79, pp 411-9

Abstract:
In this overview the authors describe their recent attempts to specifically interfere with the metastatic spread of B16-F10 melanoma cells. Using the experimental metastasis model system, inhibitory effects of (1) coinjection of cells with synthetic peptides derived from the glycoprotein fibronectin, which possess the ability to disrupt cell adhesion, and (2) treatment of cells with inhibitors of protein glycosylation and oligosaccharide processing have been examined.
, K Matsumoto, S L White, K Olden
Proceedings of the National Academy of Sciences, Volume 83, pp 1752-1756; https://doi.org/10.1073/pnas.83.6.1752

Abstract:
Oligosaccharide moieties of cell-surface glycoconjugates are thought to be involved in recognition events associated with tumor metastasis and invasion. Using swainsonine (SW), an inhibitor of Golgi alpha-mannosidase II that results in the formation of hybrid-type oligosaccharides on N-linked glycoproteins, we have tested the hypothesis that specific glycan structures are required for pulmonary colonization by tumor cells. B16-F10 murine melanoma cells were treated with SW in growth medium and then injected intravenously into syngeneic C57BL/6 mice. This treatment resulted in dramatic inhibition of colonization, but it had no effect on B16-F10 viability or on cellular tumorigenicity after subcutaneous implantation. SW-treated radiolabeled B16-F10 cells were cleared from the lungs at a greater rate than control cells, suggesting that one effect of treatment is to alter tumor cell retention in the target organ. Our results implicate specific glycan structures in pulmonary colonization and offer a potential approach for identification of specific macromolecules involved in tumor cell-organ recognition during metastasis.
Garth L. Nicolson, Motowo Nakajima, Tatsuro Irimura
Published: 1 January 1986
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Tatsuro Irimura, David M. Ota, Karen R. Cleary, Garth L. Nicolson
Published: 1 January 1986
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I. Virtanen, E. Lehtonen, O. Närvänen, I. Leivo, V.-P. Lehto
Published: 30 November 1985
Experimental Cell Research, Volume 161, pp 53-62; https://doi.org/10.1016/0014-4827(85)90489-6

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Lance A. Liotta, Ronald H. Goldfarb
Published: 1 January 1984
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Garth L. Nicolson, Tatsuro Irimura, Motowo Nakajima, Timothy V. Updyke, George Poste
Published: 1 January 1984
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Kenneth V. Honn, James M. Onoda, David G. Menter, John D. Taylor, Bonnie F. Sloane
Published: 1 January 1984
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John G. Steele, Charles Rowlatt, , L. M. Franks
Published: 15 December 1983
International Journal of Cancer, Volume 32, pp 769-779; https://doi.org/10.1002/ijc.2910320619

Abstract:
The surface oligosaccharide residues, glycoproteins and sialyl components of CMT64 lung carcinoma cells and high‐metastatic sublines CMT167 and CMT181 have been studied in culture. (I) The total cellular sialic acid content did not differ appreciably between the three lines. However, the accessibility of surface sialyl groups, measured by metabolic incorporation of [3H]NAcmannosamine followed by neuraminidase hydrolysis, was decreased from 42% in CMT64 to 25% hydrolyzed in CMT181. (2) The major plasma membrane glycoproteins of the lines were radiolabelled by lactoperoxidase iodination, metabolic incorporation of [3H]fucose or labelling in the terminal sialyl residues by the NalO4‐NaB[3H]4 method and the labelled glycoproteins were analyzed by two‐dimensional gel electrophoresis. Each labelling technique identified a complex pattern of glycoproteins including a prominently labelled group of high‐molecular‐weight acidic sialoglycoproteins: GP200/4.9–5.1 (apparent molecular weight ×10−3/pI of iodoprotein); GP150/5.1–5.6; GP130/5.0–5.6; GP110/5.0; GP100/4.8 and GP100/5.0–5.4. (3) The neuraminidase‐susceptible glycoproteins on CMT64 and CMT181 were identified in the isoelectric focusing separation of the two‐dimensional gel separation by the charge difference caused by desialylation. The glycoproteins most susceptible to neuraminidase were the high‐molecular‐weight acidic glycoproteins which showed marked charge heterogeneity: GP150/5.1–5.6, GP130/5.0–5.6; GP100/5.0–5.4 and GP100/4.8. (4) Using these procedures we did not detect modifications between CMT181 and CMT64 and we conclude that the cultured cells of the sublines do not display marked surface glycoprotein alterations that reflect their enhanced spontaneous metastatic potential.
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