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Disease relevance of Bauhinia

  • The constructs express functionally active proteins on the phage particle surface and have been purified by affinity chromatography with an antibody for beta-galactosidase and a mucin as a ligand for Bauhinia purpurea agglutinin [1].
  • Under similar assay conditions, adherence of a mannose-sensitive strain of Escherichia coli was inhibited by concanavalin A but not by the lectin from Bauhinia purpurea [2].
  • In this study we show that the pulmonary edema in isolated perfused rabbit lungs caused by activated neutrophils via release of elastase is significantly decreased by the Kunitz-type Inhibitor BbCI (10(-5) M) from Bauhinia bauhinoides to the same degree as by eglin C (10(-5) M) from Hirudo medicinalis, which was used as a reference [3].
  • The highly homologous proteinase inhibitor BrPI (10(-5) M) from Bauhinia rufa, however, did not reduce edema formation [3].
  • We have earlier prepared a pancreatic cancer-associated mucin, whose altered carbohydrate structure was recognized by Vicia villosa (VVA), Bauhinia purpurea (BPA), and peanut (PNA) lectins and which was found preferentially in the sera of patients with pancreatic or gastric cancer [4].

High impact information on Bauhinia

  • The N-acetylgalactosamine (DGalNAc)-binding lectin from Bauhinia purpurea agglutinated and inhibited the movement of epimastigotes and bloodstream trypomastigotes, but it only inhibited--without agglutinating--culture trypomastigotes [5].
  • The specific Kunitz Bauhinia ungulata factor Xa inhibitor (BuXI) and the Bauhinia variegata trypsin inhibitor (BvTI) blocked the activity of trypsin, chymotrypsin, plasmin, plasma kallikrein and factor XIIa, and factor Xa inhibition was achieved only by BuXI (K(i) 14 nM) [6].
  • Furthermore, four galactose-binding lectins (bauhinia purpurea, glysine maximus, griffonia simplicifolia-I, and arachis hypogaea) were found to identify specific subsets of granulosa cells [7].
  • Lectins from Bauhinia purpurea and Arachis hypogaea which recognize N-acetyl-D-galactosamine, D-galactose, and D-galactose-beta-(1----3)-N-acetyl-D-galactosamine inhibited bacterial attachment, and binding of these lectins to epithelial cells was enhanced by the addition of neuraminidase [2].
  • They also precipitated well Wistaria floribunda (WFA), Glycine max (SBA), Bauhinia purpurea alba, abrin-a and ricin, all of which recognize the Galbeta1--> 4GlcNAcbeta1--> sequence, although at different strength [8].

Chemical compound and disease context of Bauhinia


Biological context of Bauhinia

  • By contrast the lectins from Vicia villosa (VVL) and Bauhinia purpurea (BPA) did not alter the antibody response [11].
  • The purposes of present study were to determine the repercussions of diabetes on the defense system against oxidative stress in pregnant female rats and to characterize the influence of the treatment with Bauhinia forficata extract on the antioxidant system, glycemic control, hepatic glycogen, cholesterol, triglycerides, total proteins and lipids [12].
  • The aim of the present investigation deals with the hematology and hepatorenal function of Caesalpinia bonducella Flem. and Bauhinia racemosa Lam. belonging to the Family: Caesalpiniaceae, and used in the traditional system of medicine [13].

Anatomical context of Bauhinia

  • We studied the binding of Bauhinia purpurea lectin (BPA) to human tonsils and peripheral blood mononuclear cells by immunohistochemical, immunoelectron microscopic, and flow cytometric techniques [14].
  • Enrichment of IL-2-producer T cells from mouse spleen by use of Bauhinia purpurea lectin [15].
  • These results show a significant chemopreventive and cytotoxic effect of ethanol extract of Bauhinia variegata against DEN induced liver tumor and human cancer cell lines [16].
  • The number of lectin receptor sites on the En(a-) erythrocyte membranes was significantly lower than on the OMN erythrocyte membranes for Limulus polyphemus, Triticum vurgaris and Bauhinia purpurea lectins [17].

Associations of Bauhinia with chemical compounds

  • The D-galactose- and N-acetyl-D-galactosamine-reactive plant lectins from peanut and from Bauhinia purpurea inhibit this interaction [18].
  • Action of Bauhinia bauhinioides synthetic peptides on serine proteinases [19].
  • To determine the carbohydrate-binding site of Bauhinia purpurea lectin (BPA), a D-galactose- and lactose-binding lectin, a peptide which interacts with lactose was purified from endoproteinase Asp-N digests of BPA by chromatography on a lactose-Sepharose column [20].
  • Eight Gram-negative, aerobic, rod-shaped and peritrichously flagellated strains were isolated from flowers of the orchid tree (Bauhinia purpurea) and of plumbago (Plumbago auriculata), and from fermented glutinous rice, all collected in Indonesia [21].
  • Bauhinia bauhinoides cruzipain inhibitor (BbCI) and Bauhinia bauhinioides kallikrein inhibitor (BbKI) are cysteine and serine proteinase inhibitors structurally homologous to plant Kunitz-type inhibitors, but are devoid of disulfide bridges [22].

Gene context of Bauhinia

  • In the course of screening for a novel inhibitor of cyclin-dependent kinase (CDK), HY52 (C17H30O2N2; molecular weight 294) was isolated from the leaves of Pata de Vaca (Bauhinia forficata) [23].
  • The kallikrein inhibitor found in Bauhinia bauhinioides seeds (BbKI) differs from classical Kunitz plant inhibitors in the lack of disulfide bridges in its structure [Biochim. Biophys. Acta 1477 (2000) 64-74] [19].
  • Separation and characterization of macrophage precursors and of interleukin 2-responding cells from nylon wool-nonadherent murine spleen cells by using Bauhinia purpurea agglutinin [24].
  • The main eluted peak inhibits trypsin (Ki = 0.6 nM), plasma kallikrein (Ki = 0.35 nM), plasmin (Ki = 33.1 nM), and weakly chymotrypsin (Ki = 2,700 nM), being the most effective plasma kallikrein inhibitor isolated from Bauhinia seeds [25].
  • This binding was inhibited by wheat germ agglutinin (WGA) but not by other lectins such as peanut agglutinin (PA), Maclura pomifera agglutinin (MPA), Bauhinia purpurea agglutinin (BPA), or concanavalin A (Con A) [26].

Analytical, diagnostic and therapeutic context of Bauhinia


  1. Lambda foo: a lambda phage vector for the expression of foreign proteins. Maruyama, I.N., Maruyama, H.I., Brenner, S. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  2. Lectin-dependent attachment of Actinomyces naeslundii to receptors on epithelial cells. Brennan, M.J., Cisar, J.O., Vatter, A.E., Sandberg, A.L. Infect. Immun. (1984) [Pubmed]
  3. Effect of plant Kunitz inhibitors from Bauhinia bauhinioides and Bauhinia rufa on pulmonary edema caused by activated neutrophils. Neuhof, C., Oliva, M.L., Maybauer, D., Maybauer, M., de Oliveira, C., Sampaio, M.U., Sampaio, C.A., Neuhof, H. Biol. Chem. (2003) [Pubmed]
  4. Expression of glycoconjugates in pancreatic, gastric, and colonic tissue by Bauhinia purpurea, Vicia villosa, and peanut lectins. Shue, G.L., Kawa, S., Kato, M., Oguchi, H., Kobayashi, T., Koiwai, T., Tokoo, M., Furuta, S., Kanai, M., Homma, T. Scand. J. Gastroenterol. (1993) [Pubmed]
  5. Lectin receptors as markers for Trypanosoma cruzi. Developmental stages and a study of the interaction of wheat germ agglutinin with sialic acid residues on epimastigote cells. Pereira, M.E., Loures, M.A., Villalta, F., Andrade, A.F. J. Exp. Med. (1980) [Pubmed]
  6. Kinetic characterization of factor Xa binding using a quenched fluorescent substrate based on the reactive site of factor Xa inhibitor from Bauhinia ungulata seeds. Oliva, M.L., Andrade, S.A., Juliano, M.A., Sallai, R.C., Torquato, R.J., Sampaio, M.U., Pott, V.J., Sampaio, C.A. Current medicinal chemistry. (2003) [Pubmed]
  7. Cellular heterogeneity in the membrana granulosa of developing rat follicles: assessment by flow cytometry and lectin binding. Kerketze, K., Blaschuk, O.W., Farookhi, R. Endocrinology (1996) [Pubmed]
  8. Interaction of a human blood group Sd(a-) Tamm-Horsfall glycoprotein with applied lectins. Wu, J.H., Watkins, W.M., Chen, C.P., Song, S.C., Wu, A.M. FEBS Lett. (1996) [Pubmed]
  9. Evaluation of toxicity after one-months treatment with Bauhinia forficata decoction in streptozotocin-induced diabetic rats. Pepato, M.T., Baviera, A.M., Vendramini, R.C., Brunetti, I.L. BMC complementary and alternative medicine [electronic resource]. (2004) [Pubmed]
  10. Antitumor activity and antioxidant role of Bauhinia racemosa against Ehrlich ascites carcinoma in Swiss albino mice [corrected]. Gupta, M., Mazumder, U.K., Kumar, R.S., Kumar, T.S. Acta Pharmacol. Sin. (2004) [Pubmed]
  11. Lectin-induced modulation of the antibody response to type III pneumococcal polysaccharide. Taylor, C.E., Stashak, P.W., Caldes, G., Prescott, B., Fowlkes, B.J., Baker, P.J. Cell. Immunol. (1984) [Pubmed]
  12. Effect of Bauhinia forficata extract in diabetic pregnant rats: maternal repercussions. Damasceno, D.C., Volpato, G.T., Calderon, I.d.e. .M., Aguilar, R., Rudge, M.V. Phytomedicine (2004) [Pubmed]
  13. Effects of methanol extracts of Caesalpinia bonducella and Bauhinia racemosa on hematology and hepatorenal function in mice. Kumar, R.S., Gupta, M., Mazumdar, U.K., Rajeshwar, Y., Kumar, T.S., Gomathi, P., Roy, R. The Journal of toxicological sciences. (2005) [Pubmed]
  14. Bauhinia purpurea lectin (BPA) binding spectra in hyperplastic human tonsil and in peripheral blood: immunohistochemical, immunoelectron microscopic, and flow cytometric analyses. Sarker, A.B., Akagi, T., Yoshino, T., Fujiwara, K., Murakami, I. J. Histochem. Cytochem. (1993) [Pubmed]
  15. Enrichment of IL-2-producer T cells from mouse spleen by use of Bauhinia purpurea lectin. Imai, Y., Osawa, T. Scand. J. Immunol. (1983) [Pubmed]
  16. Chemoprevention and cytotoxic effect of Bauhinia variegata against N-nitrosodiethylamine induced liver tumors and human cancer cell lines. Rajkapoor, B., Jayakar, B., Murugesh, N., Sakthisekaran, D. Journal of ethnopharmacology. (2006) [Pubmed]
  17. Serological and biochemical studies on En(a-) human erythrocytes in a Japanese family. Shinozuka, T., Miyata, Y., Kuroda, N., Takei, S., Kurihara, K., Yanagida, J. Nippon Hoigaku Zasshi (1992) [Pubmed]
  18. A 160-kilodalton epithelial cell surface glycoprotein recognized by plant lectins that inhibit the adherence of Actinomyces naeslundii. Brennan, M.J., Cisar, J.O., Sandberg, A.L. Infect. Immun. (1986) [Pubmed]
  19. Action of Bauhinia bauhinioides synthetic peptides on serine proteinases. Cagliari, C.I., De Caroli, F.P., Nakahata, A.M., Araújo, M.S., Nakaie, C.R., Sampaio, M.U., Sampaio, C.A., Oliva, M.L. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  20. Determination of the carbohydrate-binding site of Bauhinia purpurea lectin by affinity chromatography. Yamamoto, K., Konami, Y., Osawa, T. J. Chromatogr. (1992) [Pubmed]
  21. Asaia bogorensis gen. nov., sp. nov., an unusual acetic acid bacterium in the alpha-Proteobacteria. Yamada, Y., Katsura, K., Kawasaki, H., Widyastuti, Y., Saono, S., Seki, T., Uchimura, T., Komagata, K. Int. J. Syst. Evol. Microbiol. (2000) [Pubmed]
  22. Kunitz-type Bauhinia bauhinioides inhibitors devoid of disulfide bridges: isolation of the cDNAs, heterologous expression and structural studies. Araújo, A.P., Hansen, D., Vieira, D.F., Oliveira, C., Santana, L.A., Beltramini, L.M., Sampaio, C.A., Sampaio, M.U., Oliva, M.L. Biol. Chem. (2005) [Pubmed]
  23. Inhibition of cell-cycle progression in HeLa cells by HY52, a novel cyclin-dependent kinase inhibitor isolated from Bauhinia forficata. Lim, H., Kim, M.K., Lim, Y., Cho, Y.H., Lee, C.H. Cancer Lett. (2006) [Pubmed]
  24. Separation and characterization of macrophage precursors and of interleukin 2-responding cells from nylon wool-nonadherent murine spleen cells by using Bauhinia purpurea agglutinin. Yamaguchi, N., Osawa, T. Int. Arch. Allergy Appl. Immunol. (1984) [Pubmed]
  25. Bauhinia bauhinioides plasma kallikrein inhibitor: interaction with synthetic peptides and fluorogenic peptide substrates related to the reactive site sequence. Oliva, M.L., Mendes, C.R., Santomauro-Vaz, E.M., Juliano, M.A., Mentele, R., Auerswald, E.A., Sampaio, M.U., Sampaio, C.A. Current medicinal chemistry. (2001) [Pubmed]
  26. Glycophorin is the reovirus receptor on human erythrocytes. Paul, R.W., Lee, P.W. Virology (1987) [Pubmed]
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