Lactic Acid Bacteria Application to Decrease Food Allergies
Marcela Albuquerque Cavalcanti de Albuquerque, Alejandra de Moreno de LeBlanc, Jean Guy LeBlanc, Raquel Bedani in Lactic Acid Bacteria, 2020
Celiac individuals develop an immune reaction mediated by T-cells against tissue transglutaminase, which is an enzyme located in the extracellular matrix. The reaction causes mucosal damage and, in some cases, intestinal villous atrophy. In general, peptides originating from the incomplete digestion of gliadin, such as the 33-mer peptide, reach the small intestine intact and cross the intestinal epithelium barrier, attaining the lamina propria, where they undergo a deamidation process. These peptides trigger an innate immune response, resulting in the activation of the adaptive immune response. Such a process stimulates the production of proinflammatory cytokines, which cause the inflammatory process of the small intestine mucosa. The inflammatory process compromises the cellular junctions from the intestinal epithelium, resulting in increased permeability of the gut membrane due to complete histological disorganization (Elli et al. 2015).
Biochemical Parameters: Childhood Diarrhea and Malabsorption Syndrome
Anil Gupta in Biochemical Parameters and the Nutritional Status of Children, 2020
Tissue transglutaminase is a calcium cofactor dependent enzyme that catalyzes the post-translational modification of polypeptides. It results in the formation of an isopeptide bond between the γ-carboxamide group of glutaminyl residue and ε amino group of lysyl residue, which are present either in similar or different polypeptides (Folk and Finlayson 1977). Tissue transglutaminase enzyme is widely distributed in the body tissues. The tissue transglutaminase enzyme is concerned with the cross linking of peptides in the glutamine residue.
Mixed bullous disease
Lionel Fry in Atlas of Bullous Diseases, 2020
The exception to a common antigen in the subepidermal bullous disorders is DH. The autoantigen in DH and celiac disease has now been defined as tissue-transglutaminase. However, the induction of antibodies to tissue-transglutaminase is due to an external factor, namely gluten, and the antibodies disappear with gluten withdrawal.
Transglutaminase 2 Mediates the Cytotoxicity of Resveratrol in a Human Cholangiocarcinoma and Gallbladder Cancer Cell Lines
Published in Nutrition and Cancer, 2018
Leda Roncoroni, Luca Elli, Paola Braidotti, Delfina Tosi, Valentina Vaira, Lorenza Tacchini, Vincenza Lombardo, Federica Branchi, Alice Scricciolo, Luisa Doneda
To detect tissue transglutaminase (TG2), the cells (5 × 106) were homogenized and lysed for 30 min in 50 mM Tris-HCl (pH 7.5), 150 mM NaCl, 1 mM Na2EDTA, 1 mM EGTA, 1% TRITON, 0.1% SDS, 1% sodium deoxycholate, 4 mM sodium pyrophosphate, 50 mM NaF, 25 mM Na3VO4, 2 mM PMSF, and a protease inhibitor cocktail (Sigma). The lysate was centrifuged in an Eppendorf centrifuge (13,500 rpm) for 30 min at 4°C, and the supernatant was saved for analysis. The total cell lysates were used for Western blotting. Samples for each analysis (10 μg) were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS–PAGE). Gels were transferred to a nitrocellulose membrane and then placed in a blocking solution consisting of TBST (10 mM Tris [pH 8.0], 150 mM NaCl, and 0.05% Tween 20) and 5% skim milk for 1 h. The blotted membranes were incubated with the monoclonal TG2 antibody (Biodesign International, Inc.). After incubation with appropriate secondary antibodies and extensive washing, the antigens were detected by means of chemiluminescence using an ECL Plus immunodetection kit (Amersham Co.). The proteins were densitometrically quantified, making sure that the signals were in the linear range. All the data were calculated by comparing the intensity of the bands. The values were calculated after normalization to the amount of β-actin.
A review on the relationship between gluten and schizophrenia: Is gluten the cause?
Published in Nutritional Neuroscience, 2018
Can Ergün, Murat Urhan, Ahmet Ayer
Genetic predisposition and exposure to a specific group of proteins called prolamines contribute to the complex pathogenesis of CD.12 Immune response against gluten in CD patients is a consequence of both innate and adaptive abnormal immune responses which together promote a pro-inflammatory environment. The gliadin peptides can also directly stimulate the immune response of macrophages and dendritic cells through pattern recognition receptors, such as toll-like receptors. This activation leads to the maturation of these cells and to the secretion of inflammatory cytokines (e.g. IL-1b, IL-8, TNF-α, and monocyte chemotactic protein-1 (MCP-1)). Consequently, the adaptive immune response directed against gluten is enhanced, and intestinal permeability is increased. Characteristic villous atrophy and crypt hyperplasia then begin to appear, which ultimately leads to the clinical manifestations of the disease.12,13 Tissue transglutaminase also plays a central role in the pathogenesis, as it further deaminates gliadin and increases its immunogenicity by causing it to bind to receptors on antigen-presenting cells with stronger affinity. Furthermore, gliadin-tissue transglutaminase complexes formed by protein cross-linkages generate an autoantibody response (predominantly immunoglobulin A [IgA] type) that can exacerbate the inflammatory process.14
Exposure to emamectin benzoate confers cytotoxic effects on human molt-4 T-cells and possible ameliorative role of vitamin E and dithiothreitol
Published in Drug and Chemical Toxicology, 2023
Yongjun Chen, Xuefeng Liu, Dongmei Yan, Jialin Xu, Shaorong Luan, Ciying Xiao, Qingchun Huang
Cell apoptosis is a fundamental and carefully regulated cellular event during development, and its dysfunction can lead to pathological conditions (Nagata 1997). In the current study, we found that EMD treatment resulted in exaggerated chromatin condensation in the nucleus and in a significant increase in the proportion of dead cells. Moreover, apoptosis became more and more significantly increased with increasing concentration of EMB. These results support previous reports that EMB induced cell apoptosis in the brain and liver tissue of rat fetuses (Azoz et al.2020), and suggest that EMB treatment impaired viability of Molt-4 T-cells through an apoptotic mechanism. Moreover, this impairment also may be attributed to the increased dispersion of Molt-4 T-cells by EMB treatment, rather than aggregation. Natsuaki et al. (2014) showed that leukocyte clusters are necessary for effective activation of effector T-cells. Krummel et al. (2016) reported that effector T-cells proliferate in clusters, and that the aggregation of effector T-cells contributes to cytokine production and highly localized immune reaction. In the current study, EMB treatment significantly decreased transglutaminase activity in Molt-4 T-cells. It is well known that, the protein-crosslinking enzyme tissue transglutaminase can deamidate γ-carboxamide groups of protein-bound glutamines, which stimulate cell aggregation (Lorand and Graham 2003, Eckert et al.2015). The decreased transglutaminase activity may be mechanism by which EMB inhibits the viability of Molt-4 T-cells.