fucose/sarcoma

The incorporation of isotopically labeled fucose into the lipids of normal and murine sarcoma virus-transformed rat cells as a function of cell population density was examined. When normal cells were seeded at low cell density, the levels of the major fucolipids, i.e., fucolipids III and IV, were

Adhesion and inhibition experiments with pulmonary cells of BALB/c-mouse origin and syngeneic sarcoma L-1 cells indicated that L-fucose specific lectin-like adhesion molecules, presumably situated on pulmonary cell surfaces are (at least partly) responsible for the specificity of this cell-cell

Kirsten murine sarcoma virus (Ki-MSV) transformed Balb/eT3 mouse cells (K-Balb) were found to have altered membrane glycoconjugates compared to normal Balb/3T3 cells. There were reduced amounts of mono- and disialogangliosides, GM1 and GD1a, and activity of the specific galactosyltransferase

Normal rat kidney (NRK) cells infected with a temperature-sensitive (ts) mutant of mouse sarcoma virus (NRK [MSV-1b]) express the transformed phenotype when grown under permissive conditions, but acquire the normal phenotype when grown under restrictive conditions. Addition of 3', 5' cyclic

Two alpha-fucose-binding lectins, Ulex europaeus agglutinin I (UEA I) and Lotus tetragonolobus agglutinin, were employed to compare and contrast the distribution of fucosubstance in normal human kidneys and a variety of renal tumors. The study employed a total of 31 kidneys surgically removed for

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

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

The temporal relationship between butyrate-induced cellular flattening of murine sarcoma virus-transformed rat cells (MSV-NRK) and alterations in certain surface-associated biochemical markers of transformation, e.g., surface glycopeptides, glycolipids, fibronectin, hexose uptake, and cell-substrate

The viral proteins of Moloney murine sarcoma virus-transformed mouse cells (G8-124), that overproduce the sarcoma virus relative to helper leukemia virus, were examined by immunoprecipitation, sizing by gel electrophoresis and peptide mapping. Using antisera to the viral core proteins, a

In the present work we show that sarcoma and normal hamster tissues contain a protein which agglutinates normal and transformed cells. The inhibition of agglutination by galacturonic acid and occasionally by fucose suggests a resemblance of this protein with vegetal lectins. When added 5 h after

Glycopeptides and endogly cosidase-digested oligosaccharides from [3H]mannose-labeled Rous sarcoma virus and Sinbis virus have been fractionated by lentil lectin-Sepharose and concanavalin A-agarose affinity chromatography and subsequently analyzed by BioGel P-4 gel filtration. Only a specific

Immune precipitation with a monospecific antiserum was employed to study the synthesis of the major viral glycoprotein gp85. Labeled gp85 was detectable by polyacrylamide gel electrophoresis of immune precipitates prepared from lysates of transformed cells which had been labeled for long term with

Three clones of myeloproliferative virus (MPV)-transformed rat fibroblasts (NRK) with different growth properties and morphology were transplanted to athymic nude mice. Presence of carbohydrate-binding proteins was inferred by fluorescence microscopy using fluorescent, glycosylated markers. Salt and