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

• Evaluation of toxicity after one-months treatment with Bauhinia forficata decoction in streptozotocin-induced diabetic rats [9].
• METHODS: Antitumor activity and antioxidant status of methanol extract (50, 100, and 200 mg/kg) of Bauhinia racemosa stem bark was evaluated against Ehrlich ascites carcinoma (EAC) tumor in mice [10].

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

• Chemoprevention and cytotoxic effect of Bauhinia variegata against N-nitrosodiethylamine induced liver tumors and human cancer cell lines [16].

References