deoxymannojirimycin/leukemia

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Effect of glycoprotein-processing inhibitors on the mouse IgE binding capacity of rat basophilic leukemia cells.

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The basophile surface high affinity receptors for IgE (Fc epsilon R) are heavily glycosylated glycoproteins like the IgE Fc itself. Their functional expression in their physiological environment can be studied with the help of a recently developed CELISA (ELISA on cell) methodology. The relevance of

Variable transduction efficiency of murine leukemia retroviral vector on mammalian cells: role of cellular glycosylation.

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To elucidate the cellular tropism of Moloney murine leukemia virus (MuLV), we have studied the transduction efficiency of a recombinant MuLV vector carrying the beta-galactosidase reporter gene on a variety of rodent cells. Under optimal conditions for in vitro cell transduction, primary cultures of

The N-linked oligosaccharides of the Fc epsilon receptors of rat basophilic leukemia cells.

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This study was undertaken to investigate the nature and microheterogeneity of the carbohydrate moiety of the Fc epsilon receptors of RBL-CA10 and RBL-CA10.7 cells. Treatment using the glycosylation processing inhibitors, castanospermine (CN), 1-deoxymannojirimycin (DMJ), and swainsonine (SW)

Interferon-gamma increases the expression of glycosylated CD95 in B-leukemic cells: an inducible model to study the role of glycosylation in CD95-signalling and trafficking.

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B-lineage acute leukaemia cells are generally resistant to CD95-mediated apoptosis. In this report, the CD95-resistant B-leukaemia lines SEM, RS4;11, and REH were used to investigate the mechanisms of resistance to CD95-signalling. We found that interferon-gamma (IFN-gamma) treatment increased the

Antiretroviral activity of castanospermine and deoxynojirimycin, specific inhibitors of glycoprotein processing.

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The objective of this study was to investigate the antiretroviral activity of specific inhibitors of glycosidases and mannosidases that are involved in N-linked oligosaccharide processing of glycoproteins. Castanospermine and 1-deoxynojirimycin, potent inhibitors of glucosidases I and II, showed

Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR.

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The C-type lectins DC-SIGN and DC-SIGNR [collectively referred to as DC-SIGN(R)] bind and transmit human immunodeficiency virus (HIV) and simian immunodeficiency virus to T cells via the viral envelope glycoprotein (Env). Other viruses containing heavily glycosylated glycoproteins (GPs) fail to

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