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Biochemical Parameters: Childhood Diarrhea and Malabsorption Syndrome
Published in Anil Gupta, 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
Published in Lionel Fry, 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.
Lactic Acid Bacteria Application to Decrease Food Allergies
Published in Marcela Albuquerque Cavalcanti de Albuquerque, Alejandra de Moreno de LeBlanc, Jean Guy LeBlanc, Raquel Bedani, Lactic Acid Bacteria, 2020
Vanessa Biscola, Marcela Albuquerque Cavalcanti de Albuquerque, Tatiana Pacheco Nunes, Antonio Diogo Silva Vieira, Bernadette Dora Gombossy de Melo Franco
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).
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.
A Peptide from Kiwifruit Exerts Anti-Inflammatory Effects in Celiac Disease Mucosa
Published in Journal of the American College of Nutrition, 2019
Ilaria Russo, Chiara Del Giorno, Ivana Giangrieco, Najla Hajji, Maria Antonietta Ciardiello, Paola Iovino, Carolina Ciacci
Celiac disease (CeD) is a food-intestinal disease frequently observed in Western countries (1%). The disease occurs in genetically predisposed people positive for either human leukocyte antigen DQ2 or human leukocyte antigen DQ (1). The disease is related to the intake of gluten, contained in wheat, rye, and barley. The gluten contains the soluble gliadins and the insoluble glutenins. As reported, “The extracellular matrix enzyme tissue transglutaminase 2 (TG2) selectively modifies gliadin peptides, through deamidation inducing the adaptative immune response. These modified peptides have an elevated affinity for human leucocyte antigen (HLA) DQ2 and DQ8 molecules that cause the T cell activation and finally the mucosa damage (2, 3). In our in vitro study, however, we use the P31 -43 peptide (from alpha-gliadin) which induces the inflammation through the innate immune response pathway in mucosal explants from celiac patients, as already shown in several previous studies” (4). During the inflammatory process, the intestinal surface expresses proteins such as human leukocyte antigen-antigen D related (HLA-DR) and cyclooxygenase 2 (COX-2) and the interleukin-15 (IL-15) production increases, delivering signals that drive chronic inflammation (5). In fact, IL-15 is hyperexpressed in intestinal epithelium and lamina propria of untreated celiac patients compared with healthy controls and patients who follow a gluten-free diet (6).
Genetic and flow cytometry analysis of seronegative celiac disease: a cohort study
Published in Scandinavian Journal of Gastroenterology, 2019
Raquel Ríos León, Laura Crespo Pérez, Enrique Rodríguez de Santiago, Garbiñe Roy Ariño, Ana De Andrés Martín, Carlota García Hoz Jiménez, Eugenia Sánchez Rodríguez, Ana Saiz González, Francisco León Prieto, Agustín Albillos
The initial diagnostic approach is based on a series of blood tests detecting anti-gluten antibodies and auto-antibodies [4]. At the time of diagnosis, before initiating a gluten-free diet (GFD), the sensitivity and specificity of antibodies are very high, especially anti-tissue transglutaminase type 2 IgA (antiTg2: sensitivity = 91%/specificity = 91%) [2]. For a diagnosis of CD, agreement among clinical, serological, histological and genetic findings is ideal although it is common that not all tests will confirm an initial suspicion of the disease [4]. In this context, there have been recent descriptions of seronegative CD. Among patients with CD, the reported prevalence of seronegative CD ranges from 1.7 [5] to 22% [6]. Such discrepancy arises from the lack of a universal consensus definition and the use of new antibody tests based on detecting antiTg2 and endomysial antibodies (EMA).