Abstract
A plastic-adherent variant of human myelomonocytic leukaemia cells (U937) is highly susceptible to direct TNF cytolysis in vitro. Previously, we found that a subline selected for resistance to TNF cytolysis (U937/R) was much less motile and more plastic-adherent than the parental line. In the present study we show that U937 and U937/R cells have different glycoforms of a 105-kDa cell-surface glycoprotein. This protein is predominantly N-glycosylated and has the physicochemical properties of the LAMP-I glycoprotein. In nude mice, U937 cells are highly malignant whereas U937/R cells form a benign, encapsulated tumour. Therefore, possession of a different glycoform of the 105-kDa glycoprotein by U937/R cells correlates not only with loss of TNF susceptibility but also with reduced invasiveness and metastasis.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Cell Line / analysis
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Cell Line / drug effects
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Cell Line / pathology
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Drug Resistance
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Glycoproteins / analysis
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Glycoproteins / drug effects*
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Humans
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Leukemia, Myelomonocytic, Chronic / metabolism
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Leukemia, Myelomonocytic, Chronic / pathology*
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Molecular Weight
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Neoplasm Invasiveness
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Neoplasm Metastasis
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Neoplasm Proteins / analysis
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Neoplasm Proteins / drug effects*
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Receptors, Cell Surface / analysis
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Receptors, Cell Surface / drug effects
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Receptors, Tumor Necrosis Factor
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Structure-Activity Relationship
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Tumor Cells, Cultured / analysis
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Tumor Cells, Cultured / drug effects
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Tumor Cells, Cultured / pathology
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Tumor Necrosis Factor-alpha / antagonists & inhibitors*
Substances
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Glycoproteins
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Neoplasm Proteins
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Receptors, Cell Surface
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Receptors, Tumor Necrosis Factor
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Tumor Necrosis Factor-alpha