Disease relevance of Griffonia

• Ehrlich ascites tumor cells were strongly agglutinated by 0.4 micrograms/mL Griffonia simplicifolia I-B4 isolectin (GS I-B4), indicating the presence of nonreducing terminal alpha-D-galactopyranose (alpha-D-Galp) residues on the cell surface [1].
• Increase in the number of microglia/macrophages by a stab wound injury, which was determined by Griffonia simplicifolia isolectin B4 staining, was not affected by BQ788 and FR139317 [2].
• Bacillus anthracis was agglutinated by several lectins, including those from Griffonia simplicifolia, Glycine max, Abrus precatorius, and Ricinus communis [3].
• In dorsal root ganglia, S100A4-positive cells appear to constitute a subpopulation of small ganglion neurons, a few of which coexpressed calcitonin gene-related peptide (CGRP) and Griffonia simplicifolia agglutinin (GSA) isolectin B4 (B4) [4].
• In this study the distribution of alkaline phosphatase (APase) was compared with a novel microvascular marker, Griffonia simplicifolia I (GSI), to determine whether the respective markers were expressed by muscle capillaries during hypoxic conditions and to probe for the presence or absence of angiogenesis in response to short-term hypoxia [5].

High impact information on Griffonia

• Phenotypically corrected transformants were separated from mutants in a fluorescent-activated cell sorter after labeling of K. lactis cells with fluorescein isothiocyanate (FITC) conjugated to Griffonia simplicifolia II lectin, which binds terminal N-acetylglucosamine [6].
• This inhibitory activity can be absorbed with the murine IgD-binding lectin from Griffonia simplicifolia 1 (GS-1) immobilized on Sepharose [7].
• Stimulated macrophages express a new glycoprotein receptor reactive with Griffonia simplicifolia I-B4 isolectin [8].
• Non-trkA cells that expressed BDNF included some trkC cells and some small cells that labeled with the lectin Griffonia simplicifolia IB4, a marker for cells that do not express trks [9].
• Isolectins I-A and I-B of Griffonia (Bandeiraea) simplicifolia. Crystal structure of metal-free GS I-B(4) and molecular basis for metal binding and monosaccharide specificity [10].

Biological context of Griffonia

• These PD cells expressed keratin 14 and Griffonia simplicifolia I-isolectin B4 (GSI-B4) lectin binding sites, which are specific for basal cells in normal epithelium but did not react with secretory or ciliated cell markers [11].
• The authors confirmed the endothelial phenotype of sorted cells based upon endothelial-specific Griffonia simplicifolia lectin staining, uptake of acetylated low-density lipoprotein (LDL), and von Willebrand factor (vWF) and VE-cadherin staining [12].

Anatomical context of Griffonia

• In serum containing media primary (0 to 7 day old) CNS pericytes are nestin positive, NG2 positive, alpha smooth muscle actin (alphaSMA) positive, and do not bind the endothelial cell specific griffonia symplicifolia agglutinin (GSA) [13].
• Endothelial cells that had been treated with alpha-galactosidase did not react with fluorescein-labeled Griffonia simplicifolia I B4 (GS-IB4), a lectin that detects the alpha-galactosyl epitope on intact cells [14].
• Three of these lectins (bauhinia purpurea, glysine maximus, and griffonia simplicifolia-I) bind to only small granulosa cells from either DES- or eCG- treated immature rats [15].
• Lectin histochemistry using the Griffonia simplicifolia II lectin (GSL II) has revealed a novel group of glycoproteins containing terminal N-acetyl-D-glucosamine (GlcNAc) residues in oligodendrocytes [16].
• Previous studies showed that Griffonia simplicifolia I-isolectin B4 (GS I-B4) and monoclonal antibodies (mAbs) against keratin 14 labeled basal cells in the adult rat trachea while other mAbs specifically stained secretory and/or ciliated cells [17].

Associations of Griffonia with chemical compounds

• Activated macrophages and affinity adsorbents prepared by the covalent coupling of galactopyranoside to agarose also bind the plant lectin isolectin B4 prepared from the seeds of Griffonia simplicifolia [18].
• Griffonia simplicifolia agglutinin II served in the present study to further characterise the sequence of abnormal glycogen accumulation in streptozotocin-diabetic rat kidneys [19].
• These cells express angiotensin-converting enzyme, acetylated LDL receptor, constitutive endothelial nitric oxide synthase, and vascular cell adhesion molecule-1 and bind Griffonia simplicifolia-I lectin [20].
• Muscle samples were incubated with rhodamine-labeled Griffonia simplicifolia I lectin, which identifies both perfused and nonperfused microvessels [21].
• The surface of cells in the cutaneous epidermis of the newborn rat exhibits a discrete change in lectin-binding specificity from Griffonia simplicifolia I-B4 (GS I-B4), specific for alpha-D-galactosyl residues, to Ulex europeus agglutinin I (UEA), specific for alpha-L-fucose, as the cell leaves the basal layer and differentiates [22].

Gene context of Griffonia

• The Had-1 mutant was resistant to wheat germ agglutinin, but sensitive to a Griffonia simplicifolia lectin, GS-II, which recognizes terminal N-acetylglucosamine residues [23].
• MCEC-1 cells were characterized by their ability to form tubes, Griffonia simplicifolia isolectin B4 binding, and CD31, intercellular adhesion molecule (ICAM)-2, and endoglin expression [24].
• First, vessel density was increased in the infarct of MMP-9 null mice compared with WT, as quantified by Griffonia (Bandeiraea) simplicifolia lectin I (GSL-I) immunohistochemistry [25].
• Staining with Griffonia simplicifolia isolectin B4 antibody showed no specific vascular changes in any of the rats, while VEGF staining revealed higher immunoreactivity in the retina of rats with normal retinal structure and those with proliferative retinopathy, but only low immunoreactivity in the control animals [26].
• Macrophage membrane glycoprotein binding of Griffonia simplicifolia I-B4 induces TNF-alpha production and a tumoricidal response [27].

Analytical, diagnostic and therapeutic context of Griffonia

• This pig linear-B antigen reacts strongly with the anti-alpha Gal isolectin B4 from Griffonia simplicifolia 1 and with human natural anti-alpha Gal antibodies specifically purified by affinity chromatography on synthetic oligosaccharides containing the terminal nonreducing alpha Gal1-->3 beta Gal-R disaccharide [28].
• This was confirmed by double labeling of either Griffonia simplicifolia isolectin B4, a microglial-specific marker, or glial fibrillary acidic protein, an astrocyte-specific protein with PBR fluorescence immunohistochemistry [29].
• The integrin adhesion molecules LFA-1 (alpha and beta chains) and VLA-4 were expressed on most microglial cells with activated morphology, as verified by co-localization with double immunofluorescence labeling for LFA-1 or VLA-4 and Griffonia simplicifolia isolectin B4 (GFS-B4) [30].
• Mutagenic reverse transcription-polymerase chain reaction, Western immunoblot assay using a CB1 receptor amine terminal domain-specific antibody, and cellular colocalization of CB1 and the microglial marker Griffonia simplicifolia isolectin B4 confirmed the expression of the CB1 receptor in rat microglial cells [31].
• METHODS: Glycolipid fractions were separated on thin layer chromatography plates and immunostained with human AB sera, biotinylated Griffonia simplicifolia isolectin B4, monoclonal antibodies reacting with the HD antigen and with blood group A antigens based on different core saccharide structures [32].

References