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The Heartbreak of Wheat-Related Disorders
Published in Stephen T. Sinatra, Mark C. Houston, Nutritional and Integrative Strategies in Cardiovascular Medicine, 2022
Multiple components of poorly digested wheat, outside the family of gluten proteins, may have deleterious effects on cardiovascular function including fermentable oligo-, di-, and monosaccharides and polyols (FODMAPS),71 wheat amylase trypsin inhibitors (ATIs),72 wheat germ agglutinins (WGA),73 and wheat exorphins74 (Figure 11.3).
Relation of Antigliadin Antibodies to Gluten-Sensitive Enteropathy
Published in Tadeusz P. Chorzelski, Ernst H. Beutner, Vijay Kumar, Tadeusz K. Zalewski, Serologic Diagnosis of Celiac Disease, 2020
Wim Th. J. M. Hekkens, Marja van Twist - de Graaf
Apart from the main fractions of gluten (glutenin and gliadin), there are other fractions that can be of interest regarding the formation of antibodies. Wheat germ agglutinin and purothionin are mentioned in this relation. Pur-othionin is bound to lipids and can be extracted by the normal lipid solvents like hexane. Antibodies against wheat germ agglutinin have been demonstrated in the serum of celiac patients by Sollid et al.90,91 with an enzyme-linked immunosorbent assay (ELISA) method, indicating that these agglutinins could be the cause of the intestinal damage in celiac disease.
The N-Formylpeptide Chemotactic Receptor
Published in Richard Horuk, Chemoattractant Ligands and Their Receptors, 2020
The FPR protein can be detected experimentally by covalently cross-linking it to a radiolabeled ligand such as N-fNle-Leu-Phe-Nle-[125I]Tyr-Lys, and by using receptor specific antibodies. This has permitted studies of the physical and biochemical properties of the receptor. When cross-linked to ligand and analyzed by SDS-PAGE, both human neutrophil FPR and FPR in transfected cells appear as broad 50–70 kDa bands;45,63,64 two isoelectric forms, pi 5.8 and 6.2, have been identified for native FPR.63 Slight differences in these values have been identified for the human monocyte and HL-60 neutrophil receptors. The molecular basis for the different pi forms is unknown. The native receptor binds to wheat germ agglutinin, indicating that it is a glycoprotein.
Nanocarrier functionalization strategies for targeted drug delivery in skin cancer therapy: current progress and upcoming challenges
Published in Expert Opinion on Drug Delivery, 2023
Leonardo Delello Di Filippo, Mariana Carlomagno de Paula, Jonatas Lobato Duarte, Geanne Aparecida de Paula, Isadora Frigieri, Marlus Chorilli
Lectins are carbohydrate-binding proteins that can bind to specific glycans on the surface of cells, such as sialic acid, which is overexpressed in neoplastic cells. Some lectins have been studied for their potential use in cancer treatment, including their ability to specifically target and bind to cancer cells. Research has shown that some lectins may have anti-cancer properties and can induce apoptosis (programmed cell death) in cancer cells. For example, wheat germ agglutinin (WGA) has been shown to inhibit the growth and proliferation of various types of cancer cells, including skin, breast, and colon cancer cells. Other lectins, such as concanavalin A (ConA), have also been shown to have anti-cancer properties. ConA has been shown to induce apoptosis in leukemia cells, while Jacalin has been shown to inhibit the growth and metastasis of breast cancer cells [38,39].
Improving cellular uptake of therapeutic entities through interaction with components of cell membrane
Published in Drug Delivery, 2019
Renshuai Zhang, Xiaofei Qin, Fandong Kong, Pengwei Chen, Guojun Pan
Lectins are glycoproteins possessing at least one non-catalytic domain, which bind reversibly to specific mono- or oligosaccharides of the cell membrane (Peumans & Van Damme, 1995). Typically involving a high number of binding sites and determined by a specific sugar code, lectin binding is usually rapid and strong. Based on the outstanding binding properties, lectin-mediated drug delivery may become a promising strategy to improve the efficacy of poorly permeable drugs. Gabor et al. found that the dietary lectin wheat germ agglutinin can facilitate binding and uptake of protein drugs due to its cytoadhesive and cytoinvasive properties (Gabor et al., 2002). However, the potential disadvantage of natural lectins is of large size that results in immunogenicity and toxicity when they were used as drug carriers (Lehr & Gabor, 2004). One of the probable methods to overcome these problems is to design smaller peptides or even organic small molecules which can mimic the function of lectins. Several small size lectins (peptides) have been found, and shown better performance than natural lectins (Lü et al., 1999; Wang et al., 2003; Li et al., 2008). For example, odorranalectin, a lectin-like peptide from skin secretions of Odorrana grahami, showing extremely low toxicity and immunogenicity in mice (Li et al., 2008). However, the study of utilizing lectins as drug carriers was very little in recent 10 years compared to CPP and antibody delivery systems which have been discussed in above part. More efforts need to be put into the design field of lectins mimic before the ideal mimics were available.
Vinorelbine cationic liposomes modified with wheat germ agglutinin for inhibiting tumor metastasis in treatment of brain glioma
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2018
Yao Xiao, Lan Cheng, Hong-jun Xie, Rui-jun Ju, Xin Wang, Min Fu, Jing-jing Liu, Xue-tao Li
Vinorelbine is a semisynthetic vinca-alkaloid and is often used as a microtubule destabilizing agent [12]. It suppresses tumor cell karyomitosis which in turn disrupts mitotic spindle formation and prevents cell division by inhibiting the polymerization of microtubules [13]. In addition, related studies had shown that the vinca-alkaloid had the potential to inhibit tumor metastasis [14]. However, the application of vinorelbine for treating glioma in clinic is still limited due to the intravenous toxicity, the serious side effects and the limitation to cross the BBB. Wheat germ agglutinin (WGA) is an agglutinin protein which protects wheat from insects, yeast and bacteria. WGA could binds to N-acetyl-d-glucosamine and sialic acid with low toxicity to the normal tissues [15]. It was reported that WGA could enhance the transport ability across the BBB by receptor-mediated endocytosis [16], and the modification of WGA on nanoparticles could potentiate the targeting effects to tumor cells by the specifically binding to glycoproteins overexpressed on cytomembrane [17]. As one of the most useful strategies, cationic liposomes have been used as excellent delivery carriers for their targeting property to tumor cells or tumor vascular cells by electrostatic interaction [18]. Moreover, the cationic charge centers on the liposomal surface could make it easier to cross the BBB via adsorption-mediated endocytosis.