Lectins

Liener, Irvin E.

doi:10.1016/b978-0-12-597183-6.50014-0

Cited by 7 publications

(6 citation statements)

References 110 publications

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“…WGA specifically binds to GlcNAc (1,4) GlcNAc and chitin. 93,96 Expression of GNA in a transgenic tobacco plant resulted in added protection against aphids, which suggested that plant lectins could be useful in the development of crops tolerant to pests. 99 PHAs and GNA bind to midgut epithelia and the binding is supposed to be the cause of toxicity of lectin against insects; however, the detailed mechanisms of toxicities are not clear.…”

Section: 08122(iii) Proteinasementioning

confidence: 99%

“…99 PHAs and GNA bind to midgut epithelia and the binding is supposed to be the cause of toxicity of lectin against insects; however, the detailed mechanisms of toxicities are not clear. 93,95,96 WGA is supposed to exert its toxicity by binding to or by preventing the formation of peritrophic membrane in midgut lumen rich in chitin; 100 however, the detailed mechanism of toxicity is unknown.…”

Section: 08122(iii) Proteinasementioning

confidence: 99%

“…55,[89][90][91][92] 4.08.1.2.2(vi) Lectins Lectins are proteins that bind to specific sugars and are found in a wide variety of plant species, but are abundant in legume seeds. [93][94][95][96] Typical lectins have multiple binding sites in each molecule, and thus they have cell agglutinating property, but some lectins have single binding site. Lectins from kidney bean seeds (Phaseolus hemagglutinin (PHA)), 97 lectin from wheat germ (wheat germ agglutinin (WGA)), 98 Chemical Defence and Toxins of Plants 351 and lectin from snowdrop, Galanthus nivalis (snowdrop lectin, GNA), 92 are the three lectins whose chemical characters and toxicity against insects have been intensively studied.…”

Section: 08122(iii) Proteinasementioning

confidence: 99%

“…Lectins from kidney bean seeds (Phaseolus hemagglutinin (PHA)), 97 lectin from wheat germ (wheat germ agglutinin (WGA)), 98 Chemical Defence and Toxins of Plants 351 and lectin from snowdrop, Galanthus nivalis (snowdrop lectin, GNA), 92 are the three lectins whose chemical characters and toxicity against insects have been intensively studied. 93,95,96 PHAs specifically bind to -GalNAc and GNA specifically binds to mannose. WGA specifically binds to GlcNAc (1,4) GlcNAc and chitin.…”

Section: 08122(iii) Proteinasementioning

confidence: 99%

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Chemical Defence and Toxins of Plants

Yamane

Konno

Sabelis

et al. 2010

Comprehensive Natural Products II

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Section: 08122(iii) Proteinasementioning

confidence: 99%

Section: 08122(iii) Proteinasementioning

confidence: 99%

Section: 08122(iii) Proteinasementioning

confidence: 99%

Section: 08122(iii) Proteinasementioning

confidence: 99%

See 2 more Smart Citations

Chemical Defence and Toxins of Plants

Yamane

Konno

Sabelis

et al. 2010

Comprehensive Natural Products II

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“…The haptenic sugars (Sigma, 0.2M in distilled water)included: N-acetyl-D-glucosamine for Triticum vulgaris agglutinin, D (+)-glucosamine and N-acetyl-D-glucosamine for Phaseolus vulgaris agglutinin and α-methyl mannose for Len culinaris agglutinin. L-fucose served as a non-haptenic sugar for the 3 lectins (Liener, et al, 1986). In the case of PHA, monosaccharides not usually considered effective happen inhibitors.…”

Section: Bead Assaymentioning

confidence: 99%

Analysis of unconventional approaches for the rapid detection of surface lectin binding ligands on human cell lines

et al. 2006

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SummaryThis laboratory has developed and used a novel histochemical assay using derivatized agarose beads for over a decade to examine the surface properties of various cell types. Most recently we have used this assay to examine lectin binding ligands on two human cell types, CCL-220, a colon cancer cell line, and CRL-1459, a non-cancer colon cell line. We found that CCL-220 cells bound specific lectins better than CRL-1459, and this information was used to test for possible differential toxicity of these lectins in culture, as a possible approach in the design of more specific anti-cancer drugs. Although we have examined the validity of the bead-binding assay in sea urchin cell systems, we have not validated this technique for mammalian cells. Here the binding results of the bead assay are compared with conventional fluorescence assays, using lectins from 3 species (Triticum vulgaris, Phaseolus vulgaris, and Lens culinaris) on the 2 colon cell lines. These lectins were chosen because they seemed to interact with the two cell lines differently.Binding results obtained using both assays were compared for frozen, thawed and fixed; cultured and fixed; and live cells. Both qualitative and quantitative fluorescence results generally correlated with those using the bead assay. Similar results were also obtained with all of the 3 different cell preparation protocols. The fluorescence assay was able to detect lower lectin binding ligand levels than the bead assay, while the bead assay, because it can so rapidly detect cells with large numbers of lectin binding ligands, is ideal for initial screening studies that seek to identify cells that are rich in surface binders for specific molecules. The direct use of frozen, thawed, and fixed cells allows rapid mass screening for surface molecules, without the requirement for costly and time consuming cell culture.

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Peptides

Seigler

1998

Plant Secondary Metabolism

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Lectins

Cited by 7 publications

References 110 publications

Chemical Defence and Toxins of Plants

Chemical Defence and Toxins of Plants

Analysis of unconventional approaches for the rapid detection of surface lectin binding ligands on human cell lines

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