Bauhinia Purpurea (BPA) Binding to Normal and Neoplastic Thyroid Glands

Sarker, Ashit Baran; Akagi, Tadaatsu; Teramoto, Norihiro; Nose, Sohichiro; Yoshino, Tadashi; Kondo, Eisaku

doi:10.1016/s0344-0338(11)80894-0

Cited by 10 publications

(8 citation statements)

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“…The second and third lectins have not been examined for mitogenic activity toward spleen cells, antiproliferative activity toward tumor cells, HIV-1 reverse transcriptase inhibitory, HIV-1 integrase inhibitory, SARS proteinase inhibitory and antifungal activities. B. purpurea lectin has been shown to have larvicidal activity on the European corn borer Ostrinia nubilalis (32), antiviral activity on Herpes simplex virus (33), and to bind to normal and cancerous thyroid glands (34). Only the insecticidal activity of B. monandra lectin against a lepidopteran and two coleopterans have been demonstrated (31).…”

Section: Resultsmentioning

confidence: 99%

Preparation and Biological Properties of a Melibiose Binding Lectin from Bauhinia variegata Seeds

Lin

2008

J. Agric. Food Chem.

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A dimeric 64-kDa melibiose-binding lectin was isolated from the seeds of Bauhinia variegata. The isolation procedure comprised affinity chromatography on Affi-gel blue gel, ion exchange chromatography on Mono Q, and gel filtration on Superdex 75. The lectin was adsorbed on the first two chromatographic media. Its hemagglutinating activity was stable after 30-min exposure to temperatures up to 70 degrees C. Since lectins may demonstrate biological activities such as antiproliferative, immunomodulatory, antifungal, antiviral, and HIV-1 reverse transcriptase inhibitory activities, the isolated lectin was tested for these activities. It was found that the lectin inhibited proliferation in hepatoma HepG2 cells and breast cancer MCF7 cells with an IC(50) of 1.4 microM and 0.18 microM, respectively. HIV-1 reverse transcriptase activity was inhibited with an IC(50) of 1.02 microM. The lectin and concanavalin A (Con A) evoked maximal mitogenic response from mouse splenocytes at similar concentrations, but the maximal response to B. variegata lectin was only 1/5 of that induced by Con A in magnitude. B. variegata lectin was devoid of antifungal activity.

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Section: Resultsmentioning

confidence: 99%

Preparation and Biological Properties of a Melibiose Binding Lectin from Bauhinia variegata Seeds

Lin

2008

J. Agric. Food Chem.

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“…Additionally, we have previously shown that B. variegata lectin has pro-infl ammatory activity, inducing neutrophil migration dependent on resident mast cells (Alencar et al 2001). BVL is similar to B. purpurea agglutinin, which has been used to probe the structural and functional role of cell surface carbohydrates (Horan et al 1999), to detect sugar moieties on normal and neoplastic cell surfaces (Sarker et al 1994), to serve as a marker for identifi cation of different cell types and as a reagent for cell separations (Shue et al 1993;Kasper et al 1994;Sarker et al 1995). This observation suggests that BVL I and BVL II can also be used as potential tools for the study of several biological activities in different cellular systems.…”

Section: Characterization Of the Predicted Bvl Proteinmentioning

confidence: 99%

Purification and molecular cloning of a new galactose-specific lectin from Bauhinia variegata seeds

et al. 2008

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A new galactose-specific lectin was purified from seeds of a Caesalpinoideae plant, Bauhinia variegata, by affinity chromatography on lactose-agarose. Protein extracts haemagglutinated rabbit and human erythrocytes (native and treated with proteolytic enzymes), showing preference for rabbit blood treated with papain and trypsin. Among various carbohydrates tested, the lectin was best inhibited by D-galactose and its derivatives, especially lactose. SDS-PAGE showed that the lectin, named BVL, has a pattern similar to other lectins isolated from the same genus, Bauhinia purpurea agglutinin (BPA). The molecular mass of BVL subunit is 32 871 Da, determined by MALDI-TOF spectrometry. DNA extracted from B.variegata young leaves and primers designed according to the B. purpurea lectin were used to generate specific fragments which were cloned and sequenced, revealing two distinct isoforms. The bvl gene sequence comprised an open reading frame of 876 base pairs which encodes a protein of 291 amino acids. The protein carried a putative signal peptide. The mature protein was predicted to have 263 amino acid residues and 28 963 Da in size.

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“…BPA has been used in multiple histochemical studies, with diverse target tissues being identified, including breast carcinoma (Sarker et al, 1995), Reed-Sternberg cells in Hodgkin's disease (Sarker et al, 1992), and follicular thyroid carcinoma (Sarker et al, 1994). However, so far the interpretations for a positive staining are mainly confined to its T specificity.…”

Section: + Ndmentioning

confidence: 99%

“…It is a glycoprotein (gp) containing a long metal-binding loop, part of which determines its carbohydrate specificity (Yamamoto et al, 2000a). The specific binding properties of BPA have been applied to probe the structural and functional role of cell surface carbohydrates (Horan et al, 1999), to detect sugar moieties on normal and neoplastic cell surfaces (Sarker et al, 1994), to serve as a marker for identification of different cell types, and as a reagent for cell separations (Kasper et al, 1994;Sarker et al, 1992Sarker et al, , 1995Shue et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

“…A chimeric lectin recombinantly produced from BPA and Lens culinaris showed a different binding affinity than its original parental ones (Yamamoto et al, 2000b). Because of the different affinity of BPA to the surface, as well as cytoplasmic glycan distribution in various cell types described previously (Kasper et al, 1994;Sarker et al, 1992Sarker et al, , 1994Sarker et al, , 1995Shue et al, 1993), we were impelled to examine its binding characteristics. Although the structural nature required for BPA binding with carbohydrates has been documented via quantitative precipitin (QPA) and precipitin inhibition assays (QPIA) (Wu et al, 1980), this information is mainly limited to monomer or submolecular Galh1-3GalNAc (T) and Galh1-related oligosaccharides.…”

Section: Introductionmentioning

confidence: 99%

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