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Page 1 de 81 résultats
Inhibition of mannose incorporation into glycoproteins and dolichol-linked intermediates of Sarcoma 180 cells by 6-methylmercaptopurine ribonucleoside.
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6-Methylmercaptopurine ribonucleoside (6-MMPR), an inhibitor of purine nucleotide biosynthesis de novo, was used as a model compound to evaluate the relationship between the levels of intracellular guanosine triphosphate (GTP) and the formation of cellular glycoproteins and their
Kaposi's sarcoma cells express the macrophage-associated antigen mannose receptor and develop in peripheral blood cultures of Kaposi's sarcoma patients.
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The mannose receptor (MR) is a surface 175-kd C-type lectin expressed by macrophages and dendritic cells. MR is involved in removal of effete cells, phagocytosis of mannose-coated particles, pinocytosis, and antigen presentation. Expression of MR was investigated in 17 biopsies of Kaposi's sarcoma
Reduction in cell surface concanavalin A binding and mannose incorporation into glycoproteins of sarcoma 180 by 6-thioguanine.
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Metabolic pathway of 2-deoxy-2-fluoro-D-glucose and 2-deoxy-2-fluoro-D-mannose in mice bearing sarcoma 180 studied by fluorin-19 nuclear magnetic resonance.
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[An evaluation of endogenous lectins in the intrapulmonary metastases of osteogenic sarcoma].
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Assessment is made of the presence or absence of specific sugar receptors (lectins) in patients operated for intrapulmonary metastases of osteogenic sarcoma. Investigations were carried out on histochemically stained paraffin sections for the separate types of sugars. Highest was the presence of
D-galactosyltransferase and its endogenous substrates in chick embryo fibroblasts transformed by Rous sarcoma virus.
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UDP-D-galactose: 2-acetamido-2-deoxy-beta-D-glucopyranosyl 4-beta-D-galactosyltransferase (GalTase) activity was purified, from primary chick embryo fibroblast (CEF) transformed by a temperature-sensitive, Rous sarcoma virus mutant (CEF-RSV), by chromatography on an affinity resin prepared with
Basis for low affinity binding of a lysosomal cysteine protease to the cation-independent mannose 6-phosphate receptor.
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In cultured mouse fibroblasts, secretion of the lysosomal cysteine protease, MEP (major excreted protein) is regulated by growth factors and viral transformation. The ability of this protein to be regulated has been attributed to its intrinsic low affinity for the cation-independent mannose
Sugar effects on murine sarcoma virus transformation.
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Transformation of NIH Swiss mouse fibroblasts by a murine sarcoma virus was influenced by the type of carbohydrate in the culture medium. Exposure to D-mannose and 2-deoxy-D-glucose caused a reduction in the number of transformed colonies in vitro and tumor formation in vivo. This is a new type of
Differences in targeting and secretion of cathepsins B and L by BALB/3T3 fibroblasts and Moloney murine sarcoma virus-transformed BALB/3T3 fibroblasts.
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BALB/3T3 fibroblasts (3T3) were observed to secrete latent, pepsin-activatable forms of cathepsin B and cathepsin L as well as an active form of beta-glucuronidase when cultured in the absence of serum. The secretion of these proteins was stimulated by the cation ionophore monensin: cathepsin B,
Insulin-like growth factor II receptor-mediated intracellular retention of cathepsin B is essential for transformation of endothelial cells by Kaposi's sarcoma-associated herpesvirus.
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Kaposi's sarcoma-associated herpesvirus (KSHV) is the pathological agent of Kaposi's sarcoma (KS), a tumor characterized by aberrant proliferation of endothelial-cell-derived spindle cells. Since in many cancers tumorigenesis is associated with an increase in the activity of the cathepsin family, we
Isolation and analysis of lectin-reactive sarcoma-associated membrane glycoproteins.
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Sarcoma and normal tissue plasma membrane lectin-reactive glycoproteins were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Two peanut agglutinin-reactive N-acetylgalactosamine-containing glycoproteins of 1.05 x 10(6) and 1.25 x 10(5) Da and one lentil agglutinin-reactive
Biosynthesis of an unglycosylated envelope glycoprotein of Rous sarcoma virus in the presence of tunicamycin.
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Cells stably infected with Rous sarcoma virus were treated with tunicamycin to prevent the glycosylation of the precursor (pr92gp) to the two viral envelope glycoproteins gp85 and gp35. Pretreatment of the cells for 4 h with the antibiotic resulted in a 90% reduction in [3H]mannose incorporation
Rous sarcoma virus glycoproteins contain hybrid-type oligosaccharides.
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Examination of [3H]mannose-labeled glycopeptides from Prague C Rous sarcoma virus gp85 with gel filtration and sequential glycosidase digestions demonstrated the presence of hybrid-type asparaginyl-oligosaccharides. The major hybrid species had an oligomannosyl core (Man5GlcNAc2-ASN) characteristic
Processing of gPr92env, the precursor to the glycoproteins of Rous sarcoma virus: use of inhibitors of oligosaccharide trimming and glycoprotein transport.
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A number of aspects of the processing of gPr92env, the precursor to the viral glycoproteins gp85 and gp35 of Rous sarcoma virus (RSV), have been studied. First, the kinetics of gPr92env processing have been examined, revealing that the precursor is overproduced in the infected cell and only a small
Both acidic-type and neutral-type asparaginyl-oligosaccharides of host-cell glycoproteins are altered in Rous-sarcoma-virus-transformed chick-embryo fibroblasts.
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In comparisons of [3H]mannose-labelled glycopeptides from chick-embryo fibroblasts infected and transformed with non-defective Prague C Rous-sarcoma virus and from untransformed fibroblasts infected with a transformation-defective derivative of Prague C Rous-sarcoma virus, we have detected
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