Erythroagglutinin from<i>Phaseolus coccineus</i>Var. Alubia:  Chemical Characterization, Sugar Specificity, and Effect on Blood Coagulation Factors

Pérez-Campos, Eduardo; Lascuraín, Ricardo; Sierra, Claudia; Espinosa, Blanca; Debray, Henri; Bouquelet, Stéphane; Zenteno, Edgar

doi:10.1021/jf970231y

Cited by 5 publications

(4 citation statements)

References 37 publications

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“…These results agree with those reported by Rutella et al, who identified that CD8+ cells exhibited a greater activation response to PHA (33). The P. Vulgaris and P. coccineus lectins recognize Nglycosidically linked oligosaccharides with a minimal octasaccharide structure with the sequence Gal(β1-4)GlcNAc(β1-2) Man(R1-6)[GlcNAc(R 1-2)Man(R1-3)]Man(R1-4) (34)(35)(36)(37)(38). Lectins of 21 and 30 kDa have been described in P. acutifolius var.…”

Section: Discussionsupporting

confidence: 92%

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Lectin fromPhaseolus acutifoliusvar. escumite: Chemical Characterization, Sugar Specificity, and Effect on Human T-Lymphocytes

Castillo-Villanueva

Caballero-Ortega

Abdullaev-Jafarova

et al. 2007

J. Agric. Food Chem.

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Purification of the lectin from Phaseolus acutifolius var. escumite was achieved by affinity chromatography on a column containing glutaraldehyzed membranes from blood group O erythrocytes. The lectin is a tetrameric glycoprotein of 121 kDa with 10% of sugar by weight composed by four subunits of 30 kDa as determined by SDS-PAGE. The lectin is composed of four isolectins as determined by ion-exchange chromatography on a mono-S column. The lectin and its isolectins showed identical NH2 terminal residues (ANDLSFNFQR FNETN) with homology to the PHA leucoagglutinin-precursor. Peptide mass fingerprint from each lectin isoform determined from tryptic peptides by MALDI-TOF (matrix assisted laser desorption ionization-time-of-flight) showed differences among subunits, thus suggesting microheterogeneity in their amino acid sequences or different glycosylation patterns. The lectin and its four isolectins agglutinated erythrocytes without serological specificity and showed mitogenic activity on human leukocytes; moreover, the main effect was rather toward CD8+ than to CD4+ human peripheral lymphocytes. The lectin from escumite was not inhibitable by simple sugars; however, the specificity of the lectin and its isoforms was mainly addressed toward galactose residues present in bi- or triantennary N-acetyllactosamine-type glycans.

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Section: Discussionsupporting

confidence: 92%

“…The P. vulgaris and P. coccineus lectins recognize N-glycosidically linked oligosaccharides with a minimal octasaccharide structure with the sequence Gal(β1−4)GlcNAc(β1−2) Man(α1−6)[GlcNAc(α 1−2)Man(α1−3)]Man(α1−4) ( − ). Lectins of 21 and 30 kDa have been described in P. acutifolius var.…”

Section: Discussionmentioning

confidence: 99%

Lectin fromPhaseolus acutifoliusvar. escumite: Chemical Characterization, Sugar Specificity, and Effect on Human T-Lymphocytes

Castillo-Villanueva

Caballero-Ortega

Abdullaev-Jafarova

et al. 2007

J. Agric. Food Chem.

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“…The relevance of the functional role of carbohydrate residues in coagulation factors has been demonstrated using lectins from Galanthus nivalis agglutinin (Manspecific) (Koyama et al 1991), Sambucus nigra (NeuAc-α -2,6) (Sinha and Wolf 1993), Maackia amurensis (NeuAc-α -2,3) (Sinha and Wolf 1993), peanut (galactose), Datura stramonium (GlcNAc) (Koyama et al 1991), Phaseolus coccineus Var. Alubia erythroagglutinin (Pérez-Campos et al 1997), as well as through glycosydase treatment activating either the extrinsic or intrinsic pathways (Sinha and Wolf 1993).…”

Section: Discussionmentioning

confidence: 99%

Lectin Activity of the Coagulation Factor VIII/von Willebrand Complex

Santizo

Zenteno

Pina-Canseco

et al. 2009

Tohoku J. Exp. Med.

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The human coagulation factor VIII (FVIII) is an essential cofactor for the proteolytic activation of factor X. FVIII is activated by thrombin and blood coagulation factor Xa; factor IXa (FIXa) activates factor X (FXa), requiring Ca 2+ , phospholipids, and activated Factor VIII (FVIIIa) (Schmidt et al. 2005). FVIII and von Willebrand factor (VWF) form a non-covalently bound complex. This complex (FVIII/ VWF) circulates in the human plasma, is critical to homeostasis, and normally exists in inactive form. The binding of FVIII to VWF is essential for the survival of FVIII in vivo (Kaufman and Pipe 1999). Deficiencies or structural defects in FVIII are responsible for the most common inherited bleeding disorders, such as hemophilia and von Willebrand disease (Lillicrap 2008).FVIII is a polypeptide of 2332 amino acids, synthesized in the liver by parenchyma cells and hepatic sinusoidal endothelium cells, as well as by the pulmonary endothelium. FVIII has several glycosylation sites that appear to be important in its circulation kinetics. This factor possesses N-glycosydically linked glycans, which are characterized by a N-acetyl-glucosamine (GlcNAc)-asparagine inner core and are relevant for the folding and productive secretion of FVIII, and O-glycosydically glycans, which are characterized by N-acetyl-galactosamine (GalNAc)-serine/threonine and are involved in determining protein conformation and interact with other glycoproteins. FVIII possesses two unusual mannosylated sites that can be recognized by mannose receptors on Kupffer cells (Dasgupta et al. 2007).

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“…The hemagglutinating titer is reported as the inverse of the last dilution with agglutinating activity. The sugar specificity of the PNA and each purified isoform was determined by comparing the effect of lactose, at different concentrations, on the hemagglutination induced by each lectin against sialidase-treated human O erythrocytes (Perez-Campos et al, 1997).…”

Section: Methodsmentioning

confidence: 99%

The Hydrophobic Character of Peanut (Arachishypogaea) Isoagglutinins

Ortiz

Bacilio

Gorocica

et al. 2000

J. Agric. Food Chem.

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Peanut seed lectin (PNA) is widely used to identify tumor-specific antigens on the eukaryotic cell surface. In this work PNA was purified by affinity chromatography, using a column containing glutaraldehyde-treated human erythrocytes, whereas PNA isoforms were purified by hydrophobic interaction chromatography using Phenyl-Sepharose. The affinity-purified PNA and its isoforms consist of four equal subunits of 24.5 kDa each, all of which agglutinated human sialidase-treated erythrocytes equally well; however, differences in their relative thermostabilities and sugar specificities for lactose were observed. Fractions PNA-I and PNA-II possess higher affinity for lactose residues than the more hydrophobic isoforms III and IV. These findings suggest that the differences observed in PNA isoagglutinins are due to hydrophobic regions of the protein that influence the three-dimensional organization of the molecule as well as its thermal stability and sugar specificity.

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Erythroagglutinin fromPhaseolus coccineusVar. Alubia: Chemical Characterization, Sugar Specificity, and Effect on Blood Coagulation Factors

Cited by 5 publications

References 37 publications

Lectin fromPhaseolus acutifoliusvar. escumite: Chemical Characterization, Sugar Specificity, and Effect on Human T-Lymphocytes

Lectin fromPhaseolus acutifoliusvar. escumite: Chemical Characterization, Sugar Specificity, and Effect on Human T-Lymphocytes

Lectin Activity of the Coagulation Factor VIII/von Willebrand Complex

The Hydrophobic Character of Peanut (Arachishypogaea) Isoagglutinins

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