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Svend Kirkeby - One of the best experts on this subject based on the ideXlab platform.
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differential binding of Griffonia simplicifolia 1 isolectin b4 gs1b4 to alpha galactose antigen in porcine adrenal gland
Xenotransplantation, 2005Co-Authors: Gitte Christensen, Axel Kornerup Hansen, Svend KirkebyAbstract:Differential binding of Griffonia simplicifolia 1 isolectin B4 (GS1B4) to alpha-galactose antigen in porcine adrenal gland: P6:02 Gitte Christensen;Axel Hansen;Svend Kirkeby; Xenotransplantation
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comparison of the binding properties of the mushroom marasmius oreades lectin and Griffonia simplicifolia i b4 isolectin to αgalactosyl carbohydrate antigens in the surface phase
Xenotransplantation, 2004Co-Authors: Svend Kirkeby, Harry C. Winter, Irwin J. GoldsteinAbstract:The binding of two alpha-galactophilic lectins, Marasmius oreades agglutinin (MOA), and Griffonia simplicifolia I isolectin B(4) (GS I-B(4)) to neoglycoproteins and natural glycoproteins were compared in a surface phase assay. Neoglycoproteins carrying various alpha-galactosylated glycans and laminin from basement membrane of mouse sarcoma that contains the xenogenic Galalpha1-3Gal1-4GlcNAc epitope were immobilized in microtiter plate wells and lectin binding determined with an enzyme-linked assay. After 24 h of incubation, MOA had higher affinity for the xenogenic pentasaccharide (Galalpha1-3Gal1-4GlcNAcbeta1-3Galbeta1-4Glc) than for the Galalpha-monosaccharide. The binding properties of MOA and GS I-B(4) to the xenogenic disaccharide (Galalpha1-3Galbeta1) were comparable while the binding of MOA to the xenogenic pentasaccharide was much stronger than the binding of GS I-B(4) to the same epitope. Non-xenogenic disaccharide-coupled neoglycoproteins having galactose end groups linked alpha1-2 or alpha1-4 to Gal or linked alpha1-3 to GalNAc bound very weakly to MOA, whereas GS I-B(4) recognized all of these disaccharides with similarly high affinity. MOA also showed high affinity for laminin. The results indicate that the Marasmius oreades lectin has nearly the same affinities as does GS I-B(4) for the simple xenogenic carbohydrate antigens, but MOA has greater affinity for the pentasaccharide and is far more specific in its binding preferences than the Griffonia lectin.
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Comparison of the binding properties of the mushroom Marasmius oreades lectin and Griffonia simplicifolia I‐B4 isolectin to αgalactosyl carbohydrate antigens in the surface phase
Xenotransplantation, 2004Co-Authors: Svend Kirkeby, Harry C. Winter, Irwin J. GoldsteinAbstract:The binding of two alpha-galactophilic lectins, Marasmius oreades agglutinin (MOA), and Griffonia simplicifolia I isolectin B(4) (GS I-B(4)) to neoglycoproteins and natural glycoproteins were compared in a surface phase assay. Neoglycoproteins carrying various alpha-galactosylated glycans and laminin from basement membrane of mouse sarcoma that contains the xenogenic Galalpha1-3Gal1-4GlcNAc epitope were immobilized in microtiter plate wells and lectin binding determined with an enzyme-linked assay. After 24 h of incubation, MOA had higher affinity for the xenogenic pentasaccharide (Galalpha1-3Gal1-4GlcNAcbeta1-3Galbeta1-4Glc) than for the Galalpha-monosaccharide. The binding properties of MOA and GS I-B(4) to the xenogenic disaccharide (Galalpha1-3Galbeta1) were comparable while the binding of MOA to the xenogenic pentasaccharide was much stronger than the binding of GS I-B(4) to the same epitope. Non-xenogenic disaccharide-coupled neoglycoproteins having galactose end groups linked alpha1-2 or alpha1-4 to Gal or linked alpha1-3 to GalNAc bound very weakly to MOA, whereas GS I-B(4) recognized all of these disaccharides with similarly high affinity. MOA also showed high affinity for laminin. The results indicate that the Marasmius oreades lectin has nearly the same affinities as does GS I-B(4) for the simple xenogenic carbohydrate antigens, but MOA has greater affinity for the pentasaccharide and is far more specific in its binding preferences than the Griffonia lectin.
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binding of Griffonia simplicifolia 1 isolectin b4 gs1 b4 to α galactose antigens
Immunology and Cell Biology, 2001Co-Authors: Svend KirkebyAbstract:: Glycoconjugates with terminal Galalpha1-3Galbeta1-4GlcNAc sequences (alpha-galactosyl epitopes, natural xenoreactive antigens) are present on various tissues in pigs and are recognized by human anti-alphagalactosyl (alphaGal) antibodies1. Hence xenotransplantation (pig-to-human) would trigger immune reactions involving complement activation and lead to the hyperactute rejection of the graft. Xenoreactive antigens are often studied by using the lectin Griffonia simplicifolia 1 isolectin B4 (GS1 B4), which shows high affinity to galactose. We here estimate the specificity of GS1 B4 for detecting various galactosyl epitopes by measuring lectin binding to neoglycoproteins, thyroglobulin and pig skeletal muscle. Enzyme linked lectin assays confirmed that GS1 B4 was highly specific to alpha-galactosylated neoglycoproteins while the lectin did not detect a beta-galactosylated ligand. The length of the sugar chains influenced the lectin-carbohydrate interaction. A monosaccharide linked to serum albumin showed higher lectin affinity than did neoglycoproteins with di- and tri-alpha-galactosyl epitopes. When the carbohydrate was extended, as in the xenoreactive pentasaccharide (Galalpha1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc), the carbohydrate- lectin interaction was meagre. Not only the terminal, but also the subterminal sugar affected the lectin binding because the GS1 B4 affinity to Galalpha1-3Gal was much stronger than to Galalpha1-3GalNAc. In bovine and porcine thyroglobulin most alphaGal epitopes appear to be cryptic, but are unmasked by a heat denaturation. In pig skeletal muscle there was lectin reaction not only in the muscle capillaries, but also in the connective tissue and intracellularly in muscle fibres. In Western blots of isolated proteins from pig muscle at least three bands were strongly stained after incubation with lectin.
E. A. Kabat - One of the best experts on this subject based on the ideXlab platform.
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bandeiraea Griffonia simplicifolia lectin i isolectin a4 reacting with tn galnaαl ser thr or galabiose galα1 4gal containing ligands
FEBS Letters, 1996Co-Authors: Wu M Albert, Shuh-chyung Song, Wu H June, E. A. KabatAbstract:Abstract Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A4(GS I-A4) reacting with the Tn(GalNAcα1 → Ser/Thr) sequence or human blood group Pk active dissacharide (E, Galα1 → 4Gal, galabiose) was studied by quantitative precipitin (QPA) and precipitin-inhibition assays. When human blood group P1 or Tn active glycoproteins were tested by QPA, GS IA4 reacted strongly with both the Tn active glycoproteins purified from asialo porcine, ovine and armadillo submandibular glands and a P1 active glycoprotein isolated from sheep hydatid fluid. They precipitated over 80% of the lectin nitrogen added. The asialo porcine salivary glycoprotein-GS I-A4 interaction was inhibited by both Tn containing glycopeptides and Galα1 → 4Gal indicating that GS I-A4 not only reacts with human blood group A(GalNAcα1 → 3Gal) and B(Galα1 → 3Gal) active dissacharides, but also recognizes the Tn sequence and the E(Galα1 → 4Gal) ligand. From these results, the carbohydrate specificity of GS I-A4 can be defined as A, Tn ≥ B and E.
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Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A4, reacting with Tn (GalNAαl → Ser/Thr or galabiose (Galα1 → 4Gal) containing ligands
FEBS Letters, 1996Co-Authors: M Wu Albert, Shuh-chyung Song, H Wu June, E. A. KabatAbstract:Abstract Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A4(GS I-A4) reacting with the Tn(GalNAcα1 → Ser/Thr) sequence or human blood group Pk active dissacharide (E, Galα1 → 4Gal, galabiose) was studied by quantitative precipitin (QPA) and precipitin-inhibition assays. When human blood group P1 or Tn active glycoproteins were tested by QPA, GS IA4 reacted strongly with both the Tn active glycoproteins purified from asialo porcine, ovine and armadillo submandibular glands and a P1 active glycoprotein isolated from sheep hydatid fluid. They precipitated over 80% of the lectin nitrogen added. The asialo porcine salivary glycoprotein-GS I-A4 interaction was inhibited by both Tn containing glycopeptides and Galα1 → 4Gal indicating that GS I-A4 not only reacts with human blood group A(GalNAcα1 → 3Gal) and B(Galα1 → 3Gal) active dissacharides, but also recognizes the Tn sequence and the E(Galα1 → 4Gal) ligand. From these results, the carbohydrate specificity of GS I-A4 can be defined as A, Tn ≥ B and E.
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Affinity of Bandeiraea (Griffonia) simplicifolia Lectin-I, Isolectin-B4 (BSI-B4) for Galα1→4Gal Ligand
Biochemical and biophysical research communications, 1995Co-Authors: Shuh-chyung Song, E. A. KabatAbstract:The affinity of Bandeiraea (Griffonia) simplicifolia lectin-I isolectin B-4 (BSI-B-4) for the isomer of human blood group B active disaccharide (B, Galα1→3Gal), the Galα1→4Gal galabiose ligand, was studied by quantitative precipitin(QPA) and precipitin-inhibition assays. When human blood group B, P1 and H active glycoproteins were tested by QPA. BSI-B4 reacted strongly with both the B active glycoprotein purified from human ovarian cyst fluid and a P1 active glycoprotein isolated from sheep hydatid fluid and precipitated over 86% of the lectin nitrogen added. The P1 active glycoprotein-BSI-B4 interaction was inhibited by both Galα1→3Galα1→methyl and Galα1→4Gal disaccharide indicating that BSI-B4 is not only reacting with Gal α1→3Gal disaccharide, but also recognizing Galα1→4Gal. The galabiose sequence is frequently found in the carbohydrate chains of many glycosphingolipids located at the mammalian cell membranes such as intestinal and red blood cell membranes, for E. coli ligand binding and toxin attachment.
Larry L. Murdock - One of the best experts on this subject based on the ideXlab platform.
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Calcium modulates protease resistance and carbohydrate binding of a plant defense legume lectin, Griffonia simplicifolia lectin II (GSII).
Comparative Biochemistry and Physiology B, 2002Co-Authors: Keyan Zhu-salzman, Ron A Salzman, Hisashi Koiwa, Philip K. Hammen, Ray A. Bressan, Larry L. Murdock, Paul M. HasegawaAbstract:Site-directed mutagenesis previously identified the residues responsible for the biological activity of the plant defense legume lectin, Griffonia simplicifolia lectin II (GSII) wProc. Natl. Acad. Sci. USA 95, (1998) 15123–15128x. However, these results were inconclusive as to whether these residues function as direct defense determinants through carbohydrate binding, or whether substantial changes of the protein structure had occurred in mutated proteins, with this structural disruption actually causing the loss of biochemical and biological functions. Evidence shown here supports the former explanation: circular dichroism and fluorescence spectra showed that mutations at carbohydrate-binding residues of GSII do not render it disfunctional because of substantial secondary or tertiary structure modifications; and trypsin treatment confirmed that rGSII structural integrity is retained in these mutants. Reduced biochemical stability was observed through papain digestion and urea denaturation in mutant versions that had lost carbohydrate-binding ability, and this was correlated with lower Ca content. Accordingly, the re-addition of Ca to demetalized proteins could recover resistance 2q 2q
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Identification of N‐acetylglucosamine binding residues in Griffonia simplicifolia lectin II
FEBS letters, 1996Co-Authors: Keyan Zhu, Ray A. Bressan, Paul M. Hasegawa, Larry L. MurdockAbstract:Primary structure and crystallographic data of several legume lectins were used to predict the involvement in carbohydrate binding of six amino acid residues (Asp88, Glu108, Tyr134, Asn136, Leu226 and Gln227) in Griffonia simplicifolia lectin II (GS-II). The functional involvement of these residues was evaluated by assessing GlcNAc binding of modified forms of GS-II in which these residues were eliminated in truncated peptides or systematically substituted with other amino acids by site-specific mutations. Mutations at (Asp88, Tyr134 or Asn136 eliminated GlcNAc binding activity by GS-II, while those at Glut108, Leu226 or Gln227 did not alter the activity. The former three amino acids were functionally essential for carbohydrate binding by GS-II presumably through hydrogen bonding to and hydrophobic interactions with GlcNAc. Although an Asp or Gly substitution for Tyr134 eliminated GlcNAc affinity, substitution with Phe did not appreciably affect binding. Despite the fact that mutations to Leu226 and Gln227 did not alter carbohydrate binding, a truncated form of GS-II lacking these residues no longer exhibited carbohydrate binding affinity.
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identification of n acetylglucosamine binding residues in Griffonia simplicifolia lectin ii
FEBS Letters, 1996Co-Authors: Keyan Zhu, Ray A. Bressan, Paul M. Hasegawa, Larry L. MurdockAbstract:Primary structure and crystallographic data of several legume lectins were used to predict the involvement in carbohydrate binding of six amino acid residues (Asp88, Glu108, Tyr134, Asn136, Leu226 and Gln227) in Griffonia simplicifolia lectin II (GS-II). The functional involvement of these residues was evaluated by assessing GlcNAc binding of modified forms of GS-II in which these residues were eliminated in truncated peptides or systematically substituted with other amino acids by site-specific mutations. Mutations at (Asp88, Tyr134 or Asn136 eliminated GlcNAc binding activity by GS-II, while those at Glut108, Leu226 or Gln227 did not alter the activity. The former three amino acids were functionally essential for carbohydrate binding by GS-II presumably through hydrogen bonding to and hydrophobic interactions with GlcNAc. Although an Asp or Gly substitution for Tyr134 eliminated GlcNAc affinity, substitution with Phe did not appreciably affect binding. Despite the fact that mutations to Leu226 and Gln227 did not alter carbohydrate binding, a truncated form of GS-II lacking these residues no longer exhibited carbohydrate binding affinity.
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An Insecticidal N-Acetylglucosamine-Specific Lectin Gene from Griffonia simplicifolia (Leguminosae)
Plant Physiology, 1996Co-Authors: Joseph E. Huesing, Richard E Shade, Ray A. Bressan, Paul M. Hasegawa, Larry L. MurdockAbstract:Griffonia simplicifolia II, an N-acetylglucosamine-specific legume lectin, has insecticidal activity when fed to the cowpea weevil, Callosobruchus maculatus (F.). A cDNA clone encoding G. simplicifolia II was isolated from a leaf cDNA library, sequenced, and expressed in a bacterial expression system. The recombinant protein exhibited N-acetylglucosamine-binding and insecticidal activity against cowpea weevil, indicating that glycosylation and multimeric structure are not required for these properties. These results support the hypothesis that genes of the legume lectin gene family encode proteins that function in plant defense against herbivores.
Paola Zanoli - One of the best experts on this subject based on the ideXlab platform.
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anxiolytic like effect of Griffonia simplicifolia baill seed extract in rats
Phytomedicine, 2011Co-Authors: Gianluca Carnevale, V. Di Viesti, Manuela Zavatti, Paola ZanoliAbstract:The seeds of Griffonia simplicifolia Baill., a tropical shrub native to West Africa, are rich in 5-hydroxy-l-tryptophan (5-HTP), a direct precursor in the synthesis of serotonin (5-HT). In spite of the modern therapeutic application of Griffonia simplicifolia seed extract in mood disorders, no scientific evidence has been provided till now. For this reason the aim of our study was to investigate the effect of Griffonia simplicifolia seed extract on anxiety behavior. Griffonia simplicifolia seed extract, dosed at 1, 5, 10 and 25 mg/kg, was orally administered in rats which were submitted to the dark-light test and open field test, 60 min after the treatment. In the dark-light test, the administration of the extract at the doses of 10 and 25 mg/kg was able to significantly increase the time spent in the light compartment (P<0.05). In the open field test, the extract dosed at 5, 10 and 25 mg/kg induced an anti-tigmotactic effect, as indicated by a significant increase of time spent in the central area of the open field (P<0.01). In conclusion these findings indicate that Griffonia simplicifolia seed extract exerts anxiolytic-like effect in rats and suggest its potential usefulness for the treatment of anxiety in humans.
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Anxiolytic-like effect of Griffonia simplicifolia Baill. seed extract in rats
Phytomedicine : international journal of phytotherapy and phytopharmacology, 2011Co-Authors: Gianluca Carnevale, V. Di Viesti, Manuela Zavatti, Paola ZanoliAbstract:The seeds of Griffonia simplicifolia Baill., a tropical shrub native to West Africa, are rich in 5-hydroxy-l-tryptophan (5-HTP), a direct precursor in the synthesis of serotonin (5-HT). In spite of the modern therapeutic application of Griffonia simplicifolia seed extract in mood disorders, no scientific evidence has been provided till now. For this reason the aim of our study was to investigate the effect of Griffonia simplicifolia seed extract on anxiety behavior. Griffonia simplicifolia seed extract, dosed at 1, 5, 10 and 25 mg/kg, was orally administered in rats which were submitted to the dark-light test and open field test, 60 min after the treatment. In the dark-light test, the administration of the extract at the doses of 10 and 25 mg/kg was able to significantly increase the time spent in the light compartment (P
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Griffonia simplicifolia negatively affects sexual behavior in female rats
Phytomedicine : international journal of phytotherapy and phytopharmacology, 2010Co-Authors: Gianluca Carnevale, V. Di Viesti, Manuela Zavatti, Augusta Benelli, Paola ZanoliAbstract:At present Griffonia simplicifolia is used in food supplement aimed to treat mood disorders as well as to reduce food intake and body weight. The plant has gained increasing interest for its high content in 5-hydroxy-L-tryptophan (5-HTP) particularly in the seed. The present study was designed to evaluate the influence of a seed extract of the plant, dosed at 25, 50 and 100 mg/kg, on the sexual behavior of ovariectomized hormone-primed rats after acute and subchronic treatment. The single administration of G. simplicifolia significantly reduced lordosis response and increased rejection behavior in female rats treated with the highest dose while it did not influence proceptive behaviors. On the other hand the subchronic administration of the extract significantly reduced proceptivity but not receptivity, and increased rejection behavior. All the tested dosages were able to markedly decrease food intake and body weight after a 9-day treatment. Taken together the present results, possibly ascribed to increased levels of 5-hydroxytryptamine (5-HT) in the brain, suggest a cautious administration of the plant extract owing to its negative influence on female sexual behavior.
Shuh-chyung Song - One of the best experts on this subject based on the ideXlab platform.
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bandeiraea Griffonia simplicifolia lectin i isolectin a4 reacting with tn galnaαl ser thr or galabiose galα1 4gal containing ligands
FEBS Letters, 1996Co-Authors: Wu M Albert, Shuh-chyung Song, Wu H June, E. A. KabatAbstract:Abstract Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A4(GS I-A4) reacting with the Tn(GalNAcα1 → Ser/Thr) sequence or human blood group Pk active dissacharide (E, Galα1 → 4Gal, galabiose) was studied by quantitative precipitin (QPA) and precipitin-inhibition assays. When human blood group P1 or Tn active glycoproteins were tested by QPA, GS IA4 reacted strongly with both the Tn active glycoproteins purified from asialo porcine, ovine and armadillo submandibular glands and a P1 active glycoprotein isolated from sheep hydatid fluid. They precipitated over 80% of the lectin nitrogen added. The asialo porcine salivary glycoprotein-GS I-A4 interaction was inhibited by both Tn containing glycopeptides and Galα1 → 4Gal indicating that GS I-A4 not only reacts with human blood group A(GalNAcα1 → 3Gal) and B(Galα1 → 3Gal) active dissacharides, but also recognizes the Tn sequence and the E(Galα1 → 4Gal) ligand. From these results, the carbohydrate specificity of GS I-A4 can be defined as A, Tn ≥ B and E.
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Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A4, reacting with Tn (GalNAαl → Ser/Thr or galabiose (Galα1 → 4Gal) containing ligands
FEBS Letters, 1996Co-Authors: M Wu Albert, Shuh-chyung Song, H Wu June, E. A. KabatAbstract:Abstract Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A4(GS I-A4) reacting with the Tn(GalNAcα1 → Ser/Thr) sequence or human blood group Pk active dissacharide (E, Galα1 → 4Gal, galabiose) was studied by quantitative precipitin (QPA) and precipitin-inhibition assays. When human blood group P1 or Tn active glycoproteins were tested by QPA, GS IA4 reacted strongly with both the Tn active glycoproteins purified from asialo porcine, ovine and armadillo submandibular glands and a P1 active glycoprotein isolated from sheep hydatid fluid. They precipitated over 80% of the lectin nitrogen added. The asialo porcine salivary glycoprotein-GS I-A4 interaction was inhibited by both Tn containing glycopeptides and Galα1 → 4Gal indicating that GS I-A4 not only reacts with human blood group A(GalNAcα1 → 3Gal) and B(Galα1 → 3Gal) active dissacharides, but also recognizes the Tn sequence and the E(Galα1 → 4Gal) ligand. From these results, the carbohydrate specificity of GS I-A4 can be defined as A, Tn ≥ B and E.
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Affinity of Bandeiraea (Griffonia) simplicifolia Lectin-I, Isolectin-B4 (BSI-B4) for Galα1→4Gal Ligand
Biochemical and biophysical research communications, 1995Co-Authors: Shuh-chyung Song, E. A. KabatAbstract:The affinity of Bandeiraea (Griffonia) simplicifolia lectin-I isolectin B-4 (BSI-B-4) for the isomer of human blood group B active disaccharide (B, Galα1→3Gal), the Galα1→4Gal galabiose ligand, was studied by quantitative precipitin(QPA) and precipitin-inhibition assays. When human blood group B, P1 and H active glycoproteins were tested by QPA. BSI-B4 reacted strongly with both the B active glycoprotein purified from human ovarian cyst fluid and a P1 active glycoprotein isolated from sheep hydatid fluid and precipitated over 86% of the lectin nitrogen added. The P1 active glycoprotein-BSI-B4 interaction was inhibited by both Galα1→3Galα1→methyl and Galα1→4Gal disaccharide indicating that BSI-B4 is not only reacting with Gal α1→3Gal disaccharide, but also recognizing Galα1→4Gal. The galabiose sequence is frequently found in the carbohydrate chains of many glycosphingolipids located at the mammalian cell membranes such as intestinal and red blood cell membranes, for E. coli ligand binding and toxin attachment.
