Targeting alpha2,3-sialylated glycan in glioma stem-like cells by Maackia amurensis lectin-II: A promising strategy for glioma treatment

2021 ◽  
pp. 112949
Author(s):  
Siyaporn Putthisen ◽  
Atit Silsirivanit ◽  
Orasa Panawan ◽  
Akiko Niibori-Nambu ◽  
Yuki Nishiyama-Ikeda ◽  
...  
Keyword(s):  
Maackia Amurensis ◽  
Promising Strategy ◽  
Maackia Amurensis Lectin

scholarly journals Location of Sialoglycoconjugates Containing the Siaα2–3Gal and Siaα2–6Gal Groups in the Rat Hippocampus and the Effect of Aging on Their Expression

2001 ◽  
Vol 49 (10) ◽  
pp. 1311-1319 ◽  
Author(s):  
Yuji Sato ◽  
Yoshihiro Akimoto ◽  
Hayato Kawakami ◽  
Hiroshi Hirano ◽  
Tamao Endo
Keyword(s):  
Electron Microscopy ◽  
Plasma Membranes ◽  
Pyramidal Cells ◽  
Staining Intensity ◽  
Rat Hippocampus ◽  
Maackia Amurensis ◽  
Ca1 Region ◽  
Old Rats ◽  
Maackia Amurensis Lectin ◽  
Stratum Lacunosum Moleculare

The histochemical distribution of sialoglycoconjugates in the CA1 region in the hippocampus formation of 9-week-old rats and 30-month-old rats was examined using electron microscopy in combination with two lectins, Maackia amurensis lectin, specific for Siaα2–3Gal, and Sambucus sieboldiana agglutinin, specific for Siaα2–6Gal. Each lectin stained the plasma membranes of pyramidal cells, indicating that the Siaα2–3Gal and Siaα2–6Gal groups were expressed on their plasma membranes. These lectins also bound to synapses in the stratum lacunosum moleculare. The staining intensity of the lectins in the synapses in these layers was downregulated in the 30-month-old rats. These results indicated that both the Siaα2–3Gal and Siaα2–6Gal groups are expressed on these synapses and that the expression of these sialyl linkages decreases in the aged brain.

scholarly journals The investigation of the changes in the surface glycoconjugates using two different spheroid models of breast cancer cells and availability assessment of these spheroid models for rapid diagnosis

2021 ◽  
Vol 38 (3) ◽  
pp. 266-271
Author(s):  
Yosun MATER ◽  
Günnur DEMİRCAN
Keyword(s):  
Breast Cancer ◽  
Cell Culture ◽  
Sialic Acid ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Sialic Acids ◽  
Maackia Amurensis ◽  
Maackia Amurensis Lectin

The importance of early cancer diagnosis has led to development of many different diagnostic methods. In this context, the studies investigating the presence and amount of sugar residues to use as indicators in the identification of cancer cell type have become prominent. In the present study, sialic acids found on the membrane surfaces of ER (+) MCF-7 and ER (-) MDA-MB-231 breast cancer cell lines were labeled using three-dimensional (3D) cell culture (Spheroid) model as the closest method to the patient sample, thus its natural environment, among the cell culture methods. These sugar units that play a role in regulation of important immune characteristics such as recognition, binding and metastasis were made visualizable by applying fluorescent-labeled lectins such as FITC-(Wheat Germ Agglutinin) specifically binding to sialic acid units (GlcNAc, Neu5Ac) including particularly ß-GlcNAc and FITC-(Maackia Amurensis-Lectin-1) specifically binding to Galß4GlcNAc type sialic acids. These glycan units were specifically labeled with FITC-(Maackia Amurensis-Lectin-1) and FITC- (Wheat Germ Agglutinin) and radiation intensities were analyzed relatively. The two different breast cancer cell cultures were compared with respect to change in the amounts of sialic acid residues containing α-2,3- and α-2,6 bonds using fluorescent-labeled lectins. In the present study, we have performed a precise, accurate and rapid determination of the sugar content in the different breast cancer cell surface lines by means of fluorescent-labeled lectins and carried out a relative comparison between the micrographs.

scholarly journals Serum glycopattern and Maackia amurensis lectin-II binding glycoproteins in autism spectrum disorder

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Yannan Qin ◽  
Yanni Chen ◽  
Juan Yang ◽  
Fei Wu ◽  
Lingyu Zhao ◽  
...  
Keyword(s):  
Autism Spectrum Disorder ◽  
Autism Spectrum ◽  
Spectrum Disorder ◽  
Maackia Amurensis ◽  
Maackia Amurensis Lectin

scholarly journals Detection of the Neu5 Ac (alpha 2,3) Gal (beta 1,4) GlcNAc sequence with the leukoagglutinin from Maackia amurensis: light and electron microscopic demonstration of differential tissue expression of terminal sialic acid in alpha 2,3- and alpha 2,6-linkage.

1989 ◽  
Vol 37 (11) ◽  
pp. 1577-1588 ◽  
Author(s):  
T Sata ◽  
P M Lackie ◽  
D J Taatjes ◽  
W Peumans ◽  
J Roth
Keyword(s):  
Sialic Acid ◽  
High Specificity ◽  
Histochemical Staining ◽  
Gold Complex ◽  
Differential Distribution ◽  
Electron Microscopic ◽  
Gold Complexes ◽  
Double Labeling ◽  
Maackia Amurensis ◽  
Maackia Amurensis Lectin

The Maackia amurensis leukoagglutinin has been shown to react specifically with the Neu5Ac (alpha 2,3) Gal sequence of asparagine-linked complex type oligosaccharides. We report here the preparation of Maackia amurensis lectin-gold complexes and their application for light and electron microscopic detection of the Neu5 Ac (alpha 2,3) Gal sequence in various tissues. The use of the lectin directly gold labeled was superior to a two-step cytochemical affinity technique using a fetuin-gold complex. The Maackia amurensis lectin-gold staining was inhibited by pre-incubation of the lectin-gold complexes with 50 mM alpha 2,3 sialyllactose, whereas alpha 2,6 sialyllactose up to concentrations of 1 M had no effect, thus demonstrating the high specificity of the histochemical staining. In addition to N-glycanase-sensitive asparagine-linked oligosaccharides, beta-elimination-sensitive serine/threonine-linked oligosaccharides could be detected. Data are presented which show that cellular staining patterns obtained with Maackia amurensis lectin-gold complexes may differ from those with elderberry bark lectin-gold, which detects the Neu5 Ac (alpha 2,6) Gal/GalN Ac sequence. Electron microscopic double labeling for direct study of the differential distribution of the Neu5 Ac (alpha 2,3) Gal and Neu5 Ac (alpha 2,6) Gal sequences is reported. Therefore, the availability of two sialic acid binding lectins with different linkage specificity for histochemistry provides the first opportunity to study tissue and cell type expression of these terminal sequences of glycoproteins.

Accessibility of glycolipid and oligosaccharide epitopes on rabbit villus and follicle-associated epithelium

2000 ◽  
Vol 278 (6) ◽  
pp. G915-G923 ◽  
Author(s):  
Nicholas J. Mantis ◽  
Andreas Frey ◽  
Marian R. Neutra
Keyword(s):  
Epithelial Cells ◽  
Intestinal Epithelial Cells ◽  
Initial Step ◽  
Cell Types ◽  
Specific Cell ◽  
M Cells ◽  
Intestinal Epithelial ◽  
B Subunit ◽  
Maackia Amurensis ◽  
Maackia Amurensis Lectin

The initial step in many mucosal infections is pathogen attachment to glycoconjugates on the apical surfaces of intestinal epithelial cells. We examined the ability of virus-sized (120-nm) and bacterium-sized (1-μm) particles to adhere to specific glycolipids and protein-linked oligosaccharides on the apical surfaces of rabbit Peyer's patch villus enterocytes, follicle-associated enterocytes, and M cells. Particles coated with the B subunit of cholera toxin, which binds the ubiquitous glycolipid GM1, were unable to adhere to enterocytes or M cells. This confirms that both the filamentous brush border glycocalyx on enterocytes and the thin glycoprotein coat on M cells can function as size-selective barriers. Oligosaccharides containing terminal β(1,4)-linked galactose were accessible to soluble lectin Ricinus communistype I on all epithelial cells but were not accessible to lectin immobilized on beads. Oligosaccharides containing α(2,3)-linked sialic acid were recognized on all epithelial cells by soluble Maackia amurensis lectin II (Mal II). Mal II coated 120-nm (but not 1-μm) particles adhered to follicle-associated enterocytes and M cells but not to villus enterocytes. The differences in receptor availability observed may explain in part the selective attachment of viruses and bacteria to specific cell types in the intestinal mucosa.

Isolation and Immobilization of Influenza Virus-Specific N-SA-α-2,3-Gal Receptors Using Magnetic Nanoparticles Coated with Chitosan and Maackia amurensis Lectin

2014 ◽  
Vol 174 (5) ◽  
pp. 1945-1958 ◽  
Author(s):  
Susana Araceli Carrizales Álvarez ◽  
Anna Ilyina ◽  
Karla Monzerratt Gregorio Jáuregui ◽  
José Luis Martínez Hernández ◽  
Brenda Berenice Vazquez Gutiérrez ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Magnetic Nanoparticles ◽  
Maackia Amurensis ◽  
Maackia Amurensis Lectin

scholarly journals Distribution of Sialoglycoconjugates in the Rat Cerebellum and Its Change with Aging

2002 ◽  
Vol 50 (9) ◽  
pp. 1179-1186 ◽  
Author(s):  
Tasuku Sasaki ◽  
Yoshihiro Akimoto ◽  
Yuji Sato ◽  
Hayato Kawakami ◽  
Hiroshi Hirano ◽  
...  
Keyword(s):  
Granular Layer ◽  
Molecular Layer ◽  
Expression Patterns ◽  
Aged Rats ◽  
Adult Rats ◽  
Rat Cerebellum ◽  
Maackia Amurensis ◽  
Old Rats ◽  
Maackia Amurensis Lectin ◽  
Granular Layers

We examined the distribution of sialoglycoconjugates in the cerebellum of 9-week-old and 30-month-old rats using light microscopy and electron microscopy in combination with two lectins, Maackia amurensis lectin (MAL) for Siaα2-3Gal and Sambucus sieboldiana agglutinin (SSA) for Siaα2-6Gal. Each lectin showed characteristic staining patterns. In young adult rats, MAL stained a strongly granular layer, a weakly molecular layer, and the medullary lamina, while SSA more strongly stained the medullary lamina than the molecular and granular layers. After aging, different staining patterns were obtained. Intense SSA reactivity was observed in the granular layer and intense MAL reactivity was observed in the medullary lamina of the aged groups. The reactivity of Purkinje cells with MAL was downregulated in the aged rats. These results indicated that Siaα2-3Gal and Siaα2-6Gal were expressed in distinct regions of the rat cerebellum and that their expression patterns changed in the aged brain.

scholarly journals Increase of MAL-II Binding Alpha2,3-Sialylated Glycan Is Associated with 5-FU Resistance and Short Survival of Cholangiocarcinoma Patients

Medicina ◽  
2019 ◽  
Vol 55 (12) ◽  
pp. 761 ◽  
Author(s):  
Sasiprapa Wattanavises ◽  
Atit Silsirivanit ◽  
Kanlayanee Sawanyawisuth ◽  
Ubon Cha’on ◽  
Sakda Waraasawapati ◽  
...  
Keyword(s):  
Cell Lines ◽  
Bile Ducts ◽  
Lectin Histochemistry ◽  
Positive Staining ◽  
Sambucus Nigra ◽  
Short Survival ◽  
Maackia Amurensis ◽  
Sambucus Nigra Agglutinin ◽  
Maackia Amurensis Lectin ◽  
Chemosensitivity Assays

Background and objectives: Sialylation plays important roles in tumor progression. Our present study aimed to demonstrate the alteration of sialylation and its role in cholangiocarcinoma (CCA). Materials and Methods: The α2,3- and α2,6-sialylation in CCA tissue was analyzed by lectin-histochemistry using Maackia amurensis lectin-II (MAL-II) and Sambucus nigra agglutinin (SNA). CCA cell lines were treated with the pan-sialylation inhibitor 3Fax-peracetyl-Neu5Ac (3F-Sia) followed by proliferation and chemosensitivity assays. Results: MAL-II binding α2,3-Sialylated Glycan (MAL-SG) and SNA binding α2,6-Sialylated Glycan (SNA-SG) were both elevated in CCA compared with hyperplastic/dysplastic (HP/DP) and normal bile ducts (NBD). The positive staining for MAL-SG or SNA-SG were found in 82% (61/74) of the CCA cases. Higher expression of MAL-SG in CCA was associated with shorter survival of the patients. The median survival of patients with high and low MAL-SG were 167 and 308 days, respectively, with overall survival of 233 days, suggesting the involvement of MAL-SG in CCA progression. MAL-SG expression of CCA cell lines was markedly decreased after treatment with 3F-Sia for 48 to 72 h. While proliferation of CCA cells were not affected by 3F-Sia treatment, their susceptibility to 5-fluorouracil (5-FU) was significantly enhanced. These results suggest that sialylation is involved in the development of 5-FU resistance and the sialylation inhibitor 3F-Sia can be used as a chemosensitizer for CCA. Conclusions: Sialylation is critically involved in the development of chemoresistance of CCA, and sialylation inhibitors may be used as a chemosensitizer in CCA treatment.

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