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Disease relevance of Sambucus

  • Colon cancer tissues display an increased activity of beta-galactoside alpha2,6 sialyltransferase (ST6Gal.I) and an increased reactivity with the lectin from Sambucus nigra (SNA), specific for alpha2,6-sialyl-linkages [1].
  • The 35 Streptococcus suis capsular-type reference strains as well as 45 field strains of type 2 were tested with sialic acid-binding lectins from Sambucus nigra (SNA I), Triticum vulgaris, Maackia amurensis, Homarus americanus, and Limax flavus [2].
  • The hemagglutinin from elderberry bark (Sambucus nigra) has a binding specificity for terminal Neu5Ac alpha (2-6) Gal sequences and was found to bind a series of glycoconjugates with a similar specificity as Pertussis toxin [3].
  • Toxicity and cytotoxicity of nigrin b, a two-chain ribosome-inactivating protein from Sambucus nigra: comparison with ricin [4].
  • Sambucus nigra agglutinin (SNA), which recognizes terminal sialic acids, strongly stained the glandular mucous cells of normal subjects, but not those of patients with chronic sinusitis [5].

High impact information on Sambucus

  • Analysis of site-directed mutants showed that alanine or serine mutants of invariant Cys(181) or Cys(332) exhibit no detectable activity, either by direct assay or by staining of the transfected cells with Sambucus nigra agglutinin, which recognizes the product NeuAcalpha2,6Galbeta1,4GlcNAc on glycoproteins [6].
  • The patterns of mRNA expression were compared with the pattern of binding of two sialic acid-specific plant lectins, Sambucus nigra agglutinin and Maackia amurensis agglutinin, which preferentially recognize alpha 2,6- and alpha 2,3-linked sialic acids, respectively, on N-glycans [7].
  • This coincided with increased expression of endothelial glycoproteins bearing N-linked glycans with alpha 2,6-linked sialic acid detected by the lectin Sambucus nigra agglutinin [8].
  • We utilized lectin binding and glycosidase treatment to investigate the functional role of carbohydrates on the activation peptide of factor X. Sambucus nigra agglutinin, a lectin that binds to sialic acid terminally linked alpha(2-6) to galactose or N-acetyl-galactosamine inhibits activation of human factor X in a dose-dependent manner [9].
  • This finding, as well as the ability of the solubilized receptor to interact with a Sambucus nigra L. lectin affinity column suggested that sialic acid residues are associated with SRIF receptors [10].

Biological context of Sambucus


Anatomical context of Sambucus

  • The binding of the agglutinins from Limax flavus (binds unselectively to sialic acid) and Sambucus nigra (binds to sialic acid attached through alpha-2,6 bonds) to the basement membrane displayed a large increase at the corneal side of limbo-corneal demarcation [16].
  • These two cell lines had consistent, significantly reduced binding of elderberry bark lectin, which recognizes terminal sialic acid in the alpha-2,6 configuration [17].
  • Changes in the distribution of sialylglycoconjugates on the surface of uncapacitated and in-vitro capacitated human spermatozoa were studied by means of two sialic acid specific lectins (Maackia amurensis agglutinin and Sambucus nigra agglutinin) [18].
  • The distribution pattern of sialylated glycoproteins in the hippocampal formation of 9-week-old and 29-month-old rats was examined using Maackia amurensis lectin, specific for Sia alpha2-3Gal, and Sambucus sieboldiana agglutinin specific for Sia alpha2-6Gal(GalNAc), and a monoclonal antibody for a linear homopolymer of alpha2-8-linked sialic acid [19].
  • In contrast, a significant increase in the staining with the Sambucus nigra lectin (SNA I), which binds to alpha(2,6)-linked sialic acid residues, was detected in the epithelial cells as well as in the mucins from tumors [20].

Associations of Sambucus with chemical compounds

  • In contrast, alpha 2,6-linked sialic acid as visualized with Sambucus nigra I lectin was found only in severe dysplasia and carcinoma [21].
  • Annexin V was used for the detection of PS at the cell surface, and Sambucus nigra lectin was used to reveal terminal sialic acid in a (alpha2,6) linkage to galactose units [22].
  • The enrichment of EC with elderberry anthocyanins conferred significant protective effects in EC against the following oxidative stressors: hydrogen peroxide (H(2)O(2)); 2, 2'-azobis(2-amidinopropane) dihydrochloride (AAPH); and FeSO(4)/ascorbic acid (AA) [23].
  • Binding was significantly inhibited by N-acetylneuraminic acid and alpha2,6-linked sialic acid-specific lectin derived from Sambucus sieboldiana in a dose-dependent manner [24].
  • Those derived from SW 948 xenografts showed an enrichment of round, non-adherent cells, strongly reactive with the NeuAc alpha 2,6 Gal/GalNAc-specific lectin from Sambucus nigra (SNA), thus indicating that a selection of these cells has occurred [25].

Gene context of Sambucus

  • Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc [26].
  • Carbohydrate binding properties of a new plant lectin isolated from elderberry (Sambucus nigra L.) (SNA) bark were studied using the techniques of quantitative precipitation, hapten inhibition, and equilibrium dialysis [27].
  • The alpha2,6-linkage was confirmed by the increase of Sambucus nigra agglutinin-lectin binding to the cell surface of CHO transfected with the cDNA encoding ST6Gal II and by specific sialidases treatment [28].
  • Reactivity of mucin-specific lectin from Sambucus sieboldiana with simple sugars, normal mucins and tumor-associated mucins. Comparison with other lectins [29].
  • Sense transfectants showed an enhanced ST6Gal-I mRNA expression and enzyme activity and an increased binding of the lectin Sambucus nigra agglutinin (SNA), specific for alpha 2,6-linked sialic acid [30].

Analytical, diagnostic and therapeutic context of Sambucus


  1. Beta-galactoside alpha2,6 sialyltransferase in human colon cancer: contribution of multiple transcripts to regulation of enzyme activity and reactivity with Sambucus nigra agglutinin. Dall'Olio, F., Chiricolo, M., Ceccarelli, C., Minni, F., Marrano, D., Santini, D. Int. J. Cancer (2000) [Pubmed]
  2. Agglutination of Streptococcus suis by sialic acid-binding lectins. Charland, N., Kellens, J.T., Caya, F., Gottschalk, M. J. Clin. Microbiol. (1995) [Pubmed]
  3. 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]
  4. Toxicity and cytotoxicity of nigrin b, a two-chain ribosome-inactivating protein from Sambucus nigra: comparison with ricin. Battelli, M.G., Citores, L., Buonamici, L., Ferreras, J.M., de Benito, F.M., Stirpe, F., Girbés, T. Arch. Toxicol. (1997) [Pubmed]
  5. Reduced sialylation of glycoproteins in nasal glands of patients with chronic sinusitis. Ueno, K., Wang, Z.H., Hanamure, Y., Yoshitsugu, M., Fukuda, K., Furuta, S., Uehara, F., Ohyama, M. Acta Otolaryngol. (1997) [Pubmed]
  6. Conserved cysteines in the sialyltransferase sialylmotifs form an essential disulfide bond. Datta, A.K., Chammas, R., Paulson, J.C. J. Biol. Chem. (2001) [Pubmed]
  7. Characterization of terminal sialic acid linkages on human thymocytes. Correlation between lectin-binding phenotype and sialyltransferase expression. Baum, L.G., Derbin, K., Perillo, N.L., Wu, T., Pang, M., Uittenbogaart, C. J. Biol. Chem. (1996) [Pubmed]
  8. Cytokine-induced beta-galactoside alpha-2,6-sialyltransferase in human endothelial cells mediates alpha 2,6-sialylation of adhesion molecules and CD22 ligands. Hanasaki, K., Varki, A., Stamenkovic, I., Bevilacqua, M.P. J. Biol. Chem. (1994) [Pubmed]
  9. Carbohydrate residues modulate the activation of coagulation factor X. Sinha, U., Wolf, D.L. J. Biol. Chem. (1993) [Pubmed]
  10. Structural analysis and functional role of the carbohydrate component of somatostatin receptors. Rens-Domiano, S., Reisine, T. J. Biol. Chem. (1991) [Pubmed]
  11. GALT deficiency causes UDP-hexose deficit in human galactosemic cells. Lai, K., Langley, S.D., Khwaja, F.W., Schmitt, E.W., Elsas, L.J. Glycobiology (2003) [Pubmed]
  12. Preparation of a stable subunit of Japanese elderberry (Sambucus sieboldiana) bark lectin and its application for the study of cell surface carbohydrates by flow cytometry. Kaku, H., Shibuya, N. FEBS Lett. (1992) [Pubmed]
  13. Characterisation of an mRNA encoding a metallothionein-like protein that accumulates during ethylene-promoted abscission of Sambucus nigra L. leaflets. Coupe, S.A., Taylor, J.E., Roberts, J.A. Planta (1995) [Pubmed]
  14. Changes in expansin activity and gene expression during ethylene-promoted leaflet abscission in Sambucus nigra. Belfield, E.J., Ruperti, B., Roberts, J.A., McQueen-Mason, S. J. Exp. Bot. (2005) [Pubmed]
  15. Urinary excretion of cyanidin glycosides. Mülleder, U., Murkovic, M., Pfannhauser, W. J. Biochem. Biophys. Methods (2002) [Pubmed]
  16. Alpha-2,3 sialylation differentiate the limbal and corneal epithelial cell phenotypes. Wolosin, J.M., Wang, Y. Invest. Ophthalmol. Vis. Sci. (1995) [Pubmed]
  17. Terminal sialylation is altered in airway cells with impaired CFTR-mediated chloride transport. Kube, D., Adams, L., Perez, A., Davis, P.B. Am. J. Physiol. Lung Cell Mol. Physiol. (2001) [Pubmed]
  18. Changes in the sialylglycoconjugate distribution on the human sperm surface during in-vitro capacitation: partial purification of a 20 kDa sialylglycoprotein of capacitated spermatozoa. Focarelli, R., Giuffrida, A., Rosati, F. Hum. Reprod. (1995) [Pubmed]
  19. Differential expression of sialoglycoproteins in the rat hippocampus and its changes during aging. Sato, Y., Endo, T. Neurosci. Lett. (1999) [Pubmed]
  20. Immunohistochemical analysis of sialic acid and fucose composition in human colorectal adenocarcinoma. Fernández-Rodríguez, J., Feijoo-Carnero, C., Merino-Trigo, A., Páez de la Cadena, M., Rodríguez-Berrocal, F.J., de Carlos, A., Butrón, M., Martínez-Zorzano, V.S. Tumour Biol. (2000) [Pubmed]
  21. 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]
  22. Attachment sites for particles in the urinary tract. Verkoelen, C.F., Van Der Boom, B.G., Kok, D.J., Schroder, F.H., Romijn, J.C. J. Am. Soc. Nephrol. (1999) [Pubmed]
  23. Incorporation of the elderberry anthocyanins by endothelial cells increases protection against oxidative stress. Youdim, K.A., Martin, A., Joseph, J.A. Free Radic. Biol. Med. (2000) [Pubmed]
  24. Binding of salivary glycoprotein-secretory immunoglobulin A complex to the surface protein antigen of Streptococcus mutans. Oho, T., Yu, H., Yamashita, Y., Koga, T. Infect. Immun. (1998) [Pubmed]
  25. Enhanced CMP-NeuAc:Gal beta 1,4GlcNAc-R alpha 2,6 sialyltransferase activity of human colon cancer xenografts in athymic nude mice and of xenograft-derived cell lines. Dall'Olio, F., Malagolini, N., Serafini-Cessi, F. Int. J. Cancer (1992) [Pubmed]
  26. Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis. Acharya, S., Rayborn, M.E., Hollyfield, J.G. Glycobiology (1998) [Pubmed]
  27. The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(alpha 2-6)Gal/GalNAc sequence. Shibuya, N., Goldstein, I.J., Broekaert, W.F., Nsimba-Lubaki, M., Peeters, B., Peumans, W.J. J. Biol. Chem. (1987) [Pubmed]
  28. Identification and functional expression of a second human beta-galactoside alpha2,6-sialyltransferase, ST6Gal II. Krzewinski-Recchi, M.A., Julien, S., Juliant, S., Teintenier-Lelièvre, M., Samyn-Petit, B., Montiel, M.D., Mir, A.M., Cerutti, M., Harduin-Lepers, A., Delannoy, P. Eur. J. Biochem. (2003) [Pubmed]
  29. Reactivity of mucin-specific lectin from Sambucus sieboldiana with simple sugars, normal mucins and tumor-associated mucins. Comparison with other lectins. Devine, P.L., Harada, H. Biol. Chem. Hoppe-Seyler (1991) [Pubmed]
  30. Cell surface alpha 2,6 sialylation affects adhesion of breast carcinoma cells. Lin, S., Kemmner, W., Grigull, S., Schlag, P.M. Exp. Cell Res. (2002) [Pubmed]
  31. Type I allergy to elderberry (Sambucus nigra) is elicited by a 33.2 kDa allergen with significant homology to ribosomal inactivating proteins. Förster-Waldl, E., Marchetti, M., Schöll, I., Focke, M., Radauer, C., Kinaciyan, T., Nentwich, I., Jäger, S., Schmid, E.R., Boltz-Nitulescu, G., Scheiner, O., Jensen-Jarolim, E. Clin. Exp. Allergy (2003) [Pubmed]
  32. Mucin-specific bark lectin from elderberry Sambucus sieboldiana and its applications to the affinity chromatography of mucin. Harada, H., Kondo, M., Yanagisawa, M., Sunada, S. Anal. Biochem. (1990) [Pubmed]
  33. Characterization and molecular cloning of Sambucus nigra agglutinin V (nigrin b), a GalNAc-specific type-2 ribosome-inactivating protein from the bark of elderberry (Sambucus nigra). Van Damme, E.J., Barre, A., Rougé, P., Van Leuven, F., Peumans, W.J. Eur. J. Biochem. (1996) [Pubmed]
  34. Analysis of natural food pigments by capillary electrophoresis. Watanabe, T., Terabe, S. Journal of chromatography. A. (2000) [Pubmed]
  35. Elderberry bark lectin--gold techniques for the detection of Neu5Ac (alpha 2,6) Gal/GalNAc sequences: applications and limitations. Taatjes, D.J., Roth, J., Peumans, W., Goldstein, I.J. Histochem. J. (1988) [Pubmed]
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