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Disease relevance of Maackia


High impact information on Maackia

  • On the contrary, labeling by Maackia amurensis lectin, which recognizes the Neu5Ac alpha 2-3Gal beta 1-4GlcNAc sequence, was intense on all three Ehrlich cell variants; it was 20-60 times greater than alpha-2,6-linked sialic acid-containing glycoconjugates [3].
  • Lectin blot assay showed that Maackia amurensis mitogen, a plant lectin specific for the trisaccharide sequence Sia(alpha)2-3Galbeta1-4GlcNAc of N-linked oligosaccharides, has strong affinity for GP-2 [4].
  • By contrast, expression of the H epitope was increased 5-8-fold in transfected cells with a 40% reduction in the expression of alpha-galactose epitope and a 50% decrease in sialylation, as measured by binding of Maackia amurensis and Sambuccus nigra agglutinins [5].
  • Moreover, the overall extent of sialylation was not affected based on the reactivity of cells to fluorescein isothiocyanate-conjugated Maackia amurensis lectin [6].
  • A stable subunit of Maackia amurensis leukoagglutinin (MMAL) was prepared by the selective reduction of disulfide bridges between the subunits followed by alkylation with 4-vinylpyridine [7].

Biological context of Maackia

  • The in situ labelling patterns of two sialic acid-specific lectins, Maackia amurensis (MAA) and Sambucus nigra (SNA) agglutinins, both showed that the helically coiled substructure of chromatids is also enriched in sialylated proteins [8].
  • That apoptosis is associated with a marked decrease in cell surface sialylation was confirmed by using the sialic acid-specific lectins Maackia amurensis agglutinin and Sambucus nigra agglutinin [9].

Anatomical context of Maackia

  • Expression of alpha 2,6-linked sialic acid residues in neoplastic but not in normal human colonic mucosa. A lectin-gold cytochemical study with Sambucus nigra and Maackia amurensis lectins [10].
  • Pretreatment of human brain endothelial cells with wheatgerm agglutinin, sialic acid, alpha(2,3)-neuraminidase or Maackia amurensis agglutinin that recognizes alpha(2,3)-, but not with Sambucus nigra agglutinin that recognizes alpha(2,6) sialylgalactosyl residues, significantly reduced FC5 transcytosis [11].
  • 125I-ASD derivatives of two sialic acid-specific plant lectins, Maackia amurensis leukoagglutinin and Sambucus nigra agglutinin, with oligosaccharide binding specificities similar to those of PT also labeled a 70-kDa protein in Jurkat cells [12].
  • The binding to normal and sialidase-treated human erythrocytes and lymphocytes of four 125I-labeled lectins [Maackia amurensis hemagglutinins (MAM and MAH), Ricinus communis hemagglutinin (RCH), and Bauhinia purpurea hemagglutinin (BPH)] was studied in detail [13].
  • Enhanced 3-O-sulfation of galactose in Asn-linked glycans and Maackia amurensis lectin binding in a new Chinese hamster ovary cell line [14].

Associations of Maackia with chemical compounds

  • Transfected cells expressed twofold-higher amounts of 6-linked sialic acids and twofold-lower amounts of 3-linked sialic acids than parent MDCK cells as judged by staining with Sambucus nigra agglutinin and Maackia amurensis agglutinin, respectively [15].
  • Previous work has shown that both types of EAT cells express Neu5Ac alpha 2,3 Gal-beta 1, 4 GlcNAc residues on their cell surface and that they both react with Maackia amurensis lectin which specifically recognizes this carbohydrate structure [16].
  • Only roots of control species that nodulate, Maackia amurensis Rupr. & Maxim. and alfalfa (Medicago sativa), produced pseudonodules after treatment with zeatin or 2,3,5-triiodobenzoic acid, an auxin transport inhibitor [17].
  • Using such cultures the suppressing activity of the Datura stramonium, Viscum album, Bauhinia purpurea, Triticum aestivum and Maackia amurensis lectins on gelatinase B induction were demonstrated [18].
  • Substitution or insertion that yielded a partial sequence similar to those of L-fucose-specific lectins and hemagglutinin from Maackia amurensis resulted in a complete loss of the hemagglutinating activity of rRBL [19].

Gene context of Maackia

  • In addition, gp300 showed complex changes during postnatal development in reactivity with the galactose binding lectin peanut agglutinin (PNA) and the sialic acid binding lectin Maackia amuresis (MAA) [20].
  • In addition, N-cadherin from WM9 (lymphomodus metastatic site) and A375 (solid tumor metastatic site) contained complex type chains with alpha2-3 sialic acid (positive reaction with Maackia amurensis agglutinin--MAA) [21].
  • Extracts of B16-F10 treated with neuraminidase showed only the basic beta-1 isoform, suggesting that terminal sialic acid residues may be responsible for this acidic pattern, an interpretation supported by the fact that MAA (Maackia ammurensis agglutinin) reacts only with the acidic isoform [22].
  • Ecgp was partially purified by wheat germ agglutinin and Maackia amurensis lectin (MAL) affinity chromatography [23].
  • The glycoconjugate expressions were demonstrated for 5 lectins, namely, Arachis hypogaea (PNA), Dolichos biflorus (DBA), Amaranthus caudatus (ACA), Maackia amurensis (MAA) and Sambucus nigra (SNA) [24].

Analytical, diagnostic and therapeutic context of Maackia

  • Loss of terminally alpha (2-->3) bound sialic acids of the oligosaccharides of rhAT III was analyzed in lectin-based Western blot and enzyme-linked lectin assays, using Maackia amurensis and Datura stramonium agglutinins for specific determination of Neu5Ac alpha (2-->3)Gal- and Gal beta (1-->4)-GlcNAc-terminated glycoproteins, respectively [25].
  • The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA) [26].


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  2. Comparison of the lectin-like activity of pertussis toxin with two plant lectins that have differential specificities for alpha (2-6) and alpha (2-3)-linked sialic acid. Heerze, L.D., Armstrong, G.D. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  3. Differential expression of cell surface sialoglycoconjugates on wild-type and cultured Ehrlich tumor cells as revealed by quantitative lectin-gold ultrastructural cytochemistry. Roth, J., Li, W.P., Knibbs, R.N., MacCallum, D.K., Song, Z., Goldstein, I.J. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  4. A potential endogenous ligand of annexin IV in the exocrine pancreas. Carbohydrate structure of GP-2, a glycosylphosphatidylinositol-anchored glycoprotein of zymogen granule membranes. Tsujii-Hayashi, Y., Kitahara, M., Yamagaki, T., Kojima-Aikawa, K., Matsumoto, I. J. Biol. Chem. (2002) [Pubmed]
  5. Expression of alpha-1,3-galactose and other type 2 oligosaccharide structures in a porcine endothelial cell line transfected with human alpha-1,2-fucosyltransferase cDNA. Sepp, A., Skacel, P., Lindstedt, R., Lechler, R.I. J. Biol. Chem. (1997) [Pubmed]
  6. Fucosylation of disaccharide precursors of sialyl LewisX inhibit selectin-mediated cell adhesion. Sarkar, A.K., Rostand, K.S., Jain, R.K., Matta, K.L., Esko, J.D. J. Biol. Chem. (1997) [Pubmed]
  7. Monomeric, monovalent derivative of Maackia amurensis leukoagglutinin. Preparation and application to the study of cell surface glycoconjugates by flow cytometry. Kaku, H., Mori, Y., Goldstein, I.J., Shibuya, N. J. Biol. Chem. (1993) [Pubmed]
  8. Localization and identification of galactose/N-acetylgalactosamine and sialic acid-containing proteins in Chinese hamster metaphase chromosomes. Myllyharju, J., Nokkala, S. Cell Biol. Int. (1998) [Pubmed]
  9. Lectin-based three-color flow cytometric approach for studying cell surface glycosylation changes that occur during apoptosis. Batisse, C., Marquet, J., Greffard, A., Fleury-Feith, J., Jaurand, M.C., Pilatte, Y. Cytometry. Part A : the journal of the International Society for Analytical Cytology. (2004) [Pubmed]
  10. Expression of alpha 2,6-linked sialic acid residues in neoplastic but not in normal human colonic mucosa. A lectin-gold cytochemical study with Sambucus nigra and Maackia amurensis lectins. Sata, T., Roth, J., Zuber, C., Stamm, B., Heitz, P.U. Am. J. Pathol. (1991) [Pubmed]
  11. The blood-brain barrier transmigrating single domain antibody: mechanisms of transport and antigenic epitopes in human brain endothelial cells. Abulrob, A., Sprong, H., Van Bergen en Henegouwen, P., Stanimirovic, D. J. Neurochem. (2005) [Pubmed]
  12. The 70-kilodalton pertussis toxin-binding protein in Jurkat cells. Armstrong, G.D., Clark, C.G., Heerze, L.D. Infect. Immun. (1994) [Pubmed]
  13. Elucidation of lectin receptors by quantitative inhibition of lectin binding to human erythrocytes and lymphocytes. Kawaguchi, T., Osawa, T. Biochemistry (1976) [Pubmed]
  14. Enhanced 3-O-sulfation of galactose in Asn-linked glycans and Maackia amurensis lectin binding in a new Chinese hamster ovary cell line. Bai, X., Brown, J.R., Varki, A., Esko, J.D. Glycobiology (2001) [Pubmed]
  15. Overexpression of the alpha-2,6-sialyltransferase in MDCK cells increases influenza virus sensitivity to neuraminidase inhibitors. Matrosovich, M., Matrosovich, T., Carr, J., Roberts, N.A., Klenk, H.D. J. Virol. (2003) [Pubmed]
  16. Expression and function of beta 1 integrins on adherent and nonadherent Ehrlich ascites tumor cells. Song, Z., Varani, J., Goldstein, I.J. Exp. Cell Res. (1995) [Pubmed]
  17. Accumulation of ENOD2-like transcripts in non-nodulating woody papilionoid legumes. Foster, C.M., Horner, H.T., Graves, W.R. Plant Physiol. (2000) [Pubmed]
  18. Regulation of gelatinase B (MMP-9) in leukocytes by plant lectins. Dubois, B., Peumans, W.J., Van Damme, E.J., Van Damme, J., Opdenakker, G. FEBS Lett. (1998) [Pubmed]
  19. Studies by site-directed mutagenesis of the carbohydrate-binding properties of a bark lectin from Robinia pseudoacacia. Nishiguchi, M., Yoshida, K., Sumizono, T., Tazaki, K. FEBS Lett. (1997) [Pubmed]
  20. Expression of sulfated gp300 and changes in glycosylation during pancreatic development. De Lisle, R.C., Isom, K.S. J. Histochem. Cytochem. (1996) [Pubmed]
  21. Carbohydrate moieties of N-cadherin from human melanoma cell lines. Ciołczyk-Wierzbicka, D., Gil, D., Hoja-Łukowicz, D., Lityńska, A., Laidler, P. Acta Biochim. Pol. (2002) [Pubmed]
  22. Glycosylation of beta-1 integrins in B16-F10 mouse melanoma cells as determinant of differential binding and acquisition of biological activity. Veiga, S.S., Chammas, R., Cella, N., Brentani, R.R. Int. J. Cancer (1995) [Pubmed]
  23. Identification of Escherichia coli outer membrane protein A receptor on human brain microvascular endothelial cells. Prasadarao, N.V. Infect. Immun. (2002) [Pubmed]
  24. Grading dysplasia in colorectal adenomas by means of the quantitative binding pattern determination of Arachis hypogaea, Dolichos biflorus, Amaranthus caudatus, Maackia amurensis, and Sambucus nigra agglutinins. Bronckart, Y., Nagy, N., Decaestecker, C., Bouckaert, Y., Remmelink, M., Gielen, I., Hittelet, A., Darro, F., Pector, J.C., Yeaton, P., Danguy, A., Kiss, R., Salmon, I. Hum. Pathol. (1999) [Pubmed]
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  26. Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins. Mrkoci, K., Kelm, S., Crocker, P.R., Schauer, R., Berger, E.G. Glycoconj. J. (1996) [Pubmed]
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