Resolution and partial characterization of the major plasma membrane sialoglycoproteins of Novikoff tumor cells.

Glenney, John R.; Allison, James P.; Hixson, Douglas C.; Walborg, Earl F.

doi:10.1016/s0021-9258(19)86837-0

Cited by 11 publications

References 31 publications

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Surface membrane glycoproteins of cultured human pancreatic cancer cells

Kim¹,

Tsao²,

Hicks³

et al. 1981

Cancer

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The cell-surface glycoproteins and proteins of four human pancreatic cell lines (MIA PaCa-2, PANC-1, HS766T, and CAPAN-1) were separately tritiated using galactose oxidase/NaB(3H)4 and iodinated using lactoperoxidase/125I. Gel electrophoresis showed that the cell lines had very different surface components. All four cell lines were tested for cell-surface antigens that cross-reacted with antisera raised against carcinoembryonic antigen and against the membrane fractions of MIA Pa Ca-2 and CAPAN-1 cells. CAPAN-1 cells reacted most strongly with all three antisera. Seventeen cell-surface proteins can be detected when CAPAN-1 cells are labeled using lactoperoxidase. The labeled membranes were solubilized in detergent and subjected to affinity chromatography on Sepharose-conjugated lectins. The bound proteins were eluted and analyzed on gel electrophoresis . All 17 proteins capable of being labeled by lactoperoxidase bound to at least one lectin column, indicating they are all glycoproteins.

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Surface membrane glycoproteins of cultured human pancreatic cancer cells

Kim¹,

Tsao²,

Hicks³

et al. 1981

Cancer

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Lectin affinity chromatography of cell surface proteins of novikoff tumor cells

Glenney

Walborg

1979

J Supramol Struct

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Novikoff hepatocellular carcinoma cells were radioiodinated by a cell surface-specific method using lactoperoxidase/125I. The iodinated proteins were solubilized in 0.5% Nonidet P-40 and subjected to affinity chromatography on Sepharose-conjugated lectins (Ricinus communis agglutinins I or II, soybean agglutinin, concanavalin A, or wheat germ agglutinin) and analyzed by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Almost all the iodinated proteins bound to one or more of the Sepharose-conjugated lectins, presumptive evidence that these peptides are glycosylated. Lectin affinity chromatography resolved defined subsets of iodinated glycoproteins and suggested that certain glycoproteins could be fractionated on the basis of heterogeneity of their heterosaccharide moieties. Incubation of the iodinated cells with neuraminidase resulted in increased binding of iodinated proteins to Sepharose-conjugated Ricinus communis agglutinins I and II and soybean agglutinin and decreased binding to Sepharose-conjugated wheat germ agglutinin. Binding of iodinated proteins to concanavalin A was unaffected by neuraminidase treatment of the cells. These studies demonstrate the utility of lectins for the multicomponent analysis of plasma membrane proteins.

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