Reactions of Normal and Tumor Cell Surfaces to Enzymes, I. Wheat-Germ Lipase and Associated Mucopolysaccharides

Aub, Joseph C.; Tieslau, Carol; Lankester, A

doi:10.1073/pnas.50.4.613

Cited by 224 publications

(57 citation statements)

References 12 publications

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“…Wheat germ agglutinin (WGA) is a plant lectin which can agglutinate various animal cells, particularly malignant cells and normal protease treated cells [1][2][3]. Agglutination is inhibited by N-acetyl-glucosamine and its/3-1--4-1inked oligomers [2--4].…”

Section: Introductionmentioning

confidence: 99%

Protein—sugar interactions A nuclear magnetic resonance investigation of the binding of O‐methyl‐di‐N‐acetyl‐β‐chitobioside to wheat germ agglutinin (lectin)

Grivet¹,

Delmotte²,

Monsigny³

1978

FEBS Letters

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Section: Introductionmentioning

confidence: 99%

Protein—sugar interactions A nuclear magnetic resonance investigation of the binding of O‐methyl‐di‐N‐acetyl‐β‐chitobioside to wheat germ agglutinin (lectin)

Grivet¹,

Delmotte²,

Monsigny³

1978

FEBS Letters

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“…More recently, it has been demonstrated that similar glycoproteins agglutinate transformed animal cells (4,5). The plant agglutinins appear to function by recognizing glycosides present in cell-surface polymers of the animal cells.…”

mentioning

confidence: 99%

Proteins from Plant Cell Walls Inhibit Polygalacturonases Secreted by Plant Pathogens

Albersheim

Anderson

1971

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

202

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Proteins extracted from the cell walls of Red Kidney bean hypocotyls, tomato stems, and suspension-cultured sycamore cells can completely inhibit the activity of the polygalacturonases (polygalaicturonide hydrolases, EC 3.2.1.15) secreted by the fungal plant pathogens Colletotrichum lindemuthianum, Fusarium oxysporum, and Sclerotium rolfsii. The inhibitor of the C. lindemuthianum polygalacturonase, purified 560-fold from bean hypocotyl extracts, is 40 times as effective an inhibitor of the C. lindemuthianum polygalacturonase as of the F. oxysporum polygalacturonase, and does not demonstrably inhibit the S. rolfsii polygalacturonase. A crude hypocotyl extract that completely inhibits the three polygalacturonases does not inhibit C. lindemuthianum-secreted cellulase, xylanase, a-galactosidase, aarabinofuranosidase, or a-galacturonosidase. The purified bean hypocotyl protein combines with the C. lindemuthianum polygalacturonase to form a complex with a dissociation constant of 2 X 10-9 M or less. The physical properties of these inhibitors are similar to those of phytohemagglutinins and of the plant glycoproteins capable of agglutinating transformed animal cells.

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“…In addition to differences in the agglutinability of cells by plant lectins (24)(25)(26), transformed cells exhibit incomplete synthesis of carbohydrate chains in membrane glycoproteins (27)(28)(29) and glycolipids (30)(31)(32)(33), and increased synthesis of a sialofucopeptide (34,35).…”

mentioning

confidence: 99%

Cholera Toxin and Cell Growth: Role of Membrane Gangliosides

Hollenberg

Fishman

Bennett

et al. 1974

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

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The bindikg of cholera toxin to three transformed mouse cell lines derived from the same parent strain, and the effects of the toxin on DNA synthesis and adenylate cyclase activity, vary in parallel with the ganglioside composition of the cells. TAL/N cells of early passage, which contain large quantities of gangliosides Gm3, GM2, G11, and GDWa, as well as the glycosyltransferases necessary for the synthesis of these gangliosides, bind the most cholera toxin and are the most sensitive to its action.TAL/N cells of later passage, which lack chemically detectable GM, and GD1a and which have no UDP-Gal:GM2 Cholera toxin (choleragen), the principal exoenterotoxin of Vibrio cholerae, is an oligomeric protein (molecular weight, approx. 100,000) (2, 7) which acts at the plasma membrane to exert its biological effect (3-7). The diverse actions of the toxin (2, 8-13) can be attributed to its ability to stimulate specifically the membrane-localized enzyme, adenylate cyclase (EC 4.6.1.1), thereby raising intracellular levels of cAMP. It is presumably by this mechanism that choleragen acts as a potent inhibitor of mitogen-induced DNA synthesis in human fibroblasts (14). Also, stimulation of adenylate cyclase probably explains the toxin's ability to inhibit mitogenic transformation of lymphocytes (15), to stimulate steroidogenesis in adrenal cells (16,17), and to induce differentiation in melanoma cells (18). In all cells so far studied, choleragen is nontoxic by several criteria (14-17) and the action of choleragen is observed to persist for at least two weeks in culture (18).It has been observed that gangliosides can interact specifically with choleragen so as to block the binding of the toxin to cell membranes (3)(4)(5)(6)(7)(19)(20)(21)(22)(23). In particular, GM1 is a highly potent inhibitor of choleragen binding; GD1a and GM2 are at least 50-fold, and GM3 at least 250-fold less effective than

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Reactions of Normal and Tumor Cell Surfaces to Enzymes, I. Wheat-Germ Lipase and Associated Mucopolysaccharides

Cited by 224 publications

References 12 publications

Protein—sugar interactions A nuclear magnetic resonance investigation of the binding of O‐methyl‐di‐N‐acetyl‐β‐chitobioside to wheat germ agglutinin (lectin)

Protein—sugar interactions A nuclear magnetic resonance investigation of the binding of O‐methyl‐di‐N‐acetyl‐β‐chitobioside to wheat germ agglutinin (lectin)

Proteins from Plant Cell Walls Inhibit Polygalacturonases Secreted by Plant Pathogens

Cholera Toxin and Cell Growth: Role of Membrane Gangliosides

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