The Fifth CORD Conference

Woodruff, Dianne L.

doi:10.1017/s0149767700011177

Cited by 2 publications

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“…When infused into syngeneic recipients, influenza-virus-treated rat thoracic duct lymphocytes accumulated in the liver and their recovery in the lymph nodes and spleen was severely reduced (287). The same pattern of lymphocyte migration was obtained after treatment of these cells with purified V .…”

Section: Sequestration Of Cellsmentioning

confidence: 59%

Glycosidases—Properties and Application to the Study of Complex Carbohydrates and Cell Surfaces

Flowers¹,

Sharon²

1979

Advances in Enzymology - And Related Areas of Molecular Biology

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Section: Sequestration Of Cellsmentioning

confidence: 59%

Glycosidases—Properties and Application to the Study of Complex Carbohydrates and Cell Surfaces

Flowers¹,

Sharon²

1979

Advances in Enzymology - And Related Areas of Molecular Biology

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“…Of more immediate pertinence, however, are the very recent studies of Woodruff and Woodruff (18,19) on the interaction of influenza virus and lymphocytes. After brief incubation of thoracic duct lymphocytes with influenza virus at 370, sialic acid was liberated from the cell surface as a consequence of the viral neuraminidase.…”

mentioning

confidence: 99%

Lymphocyte mitogenesis induced by a mammalian liver protein that specifically binds desialylated glycoproteins.

Novogrodsky¹,

Ashwell²

1977

Proc. Natl. Acad. Sci. U.S.A.

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ABSTRACr A purified rabbit liver membrane protein that binds desialylated yeoproteins has been shown to be a mitogen for human peripheral Iymphocytes. The mitogenic activity is specific for desialylated thymus-derived (T-cells. The loss of mitogenicity upon exposure of the binding protein to neuraminidase and the inhibitory potency of asialo-orosomucoid support-the conclusion that the site involved in the binding of asialoglycoproteins is also responsible for the mitogenic effect on desialylated lymphocytes. The potential relevance of this phenomenon to the etiology of hepatocellular necrosis is considered.Mitogens induce lymphocyte transformation by reacting with specific carbohydrate residues on the surface membrane of the cell (1, 2). The target sites for mitogens such as phytohemagglutinin (PHA), concanavalin A (Con A), or periodate are fully exposed on the cell surface, whereas the sites for soybean agglutinin (SBA), peanut agglutinin (PNA), and galactose oxidase are masked by sialic acid residues and require treatment with neuraminidase prior to activation. The penultimate galactose residues, exposed by the enzymatic release of sialic acid, are presumed to be the target site for the latter mitogens (3-5).The isolation and characterization of a rabbit liver binding protein specific for galactose-terminated glycoproteins has been described (6, 7) and the protein has been shown to possess the lectin-like ability to agglutinate erythrocytes (8). In some species, agglutination was made manifest only after neuraminidase treatment of the cells.The present report extends these findings with the demonstration that this hepatic binding protein (HBP) t To whom reprint requests should be addressed. and desialylated as described previously (11). The hepatic protein, purified to homogeneity from whole rabbit liver by affinity chromatography (7)

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The Fifth CORD Conference

Cited by 2 publications

References 0 publications

Glycosidases—Properties and Application to the Study of Complex Carbohydrates and Cell Surfaces

Glycosidases—Properties and Application to the Study of Complex Carbohydrates and Cell Surfaces

Lymphocyte mitogenesis induced by a mammalian liver protein that specifically binds desialylated glycoproteins.

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