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The Onset of Enhanced Intestinal Permeability and Food Sensitivity Triggered by Medication Used in Dental Procedures: A Case Report  [PDF]
Aristo Vojdani,Jama Lambert
Case Reports in Gastrointestinal Medicine , 2012, DOI: 10.1155/2012/265052
Abstract: Enhanced intestinal permeability and food sensitivity are two of the many proven causes of gastrointestinal disorders. This present report describes a woman with no previous gastrointestinal (GI) complaints, who underwent dental root canal, bone graft, and implant procedures. Postsurgery she experienced an allergic reaction to the combined medications. In the weeks that followed, she presented with multiple food intolerances. Four weeks after the final dental procedure, she was assessed serologically for mucosal immune function, salivary, and blood-gluten reactivity, intestinal permeability, and other food sensitivities. Compared to her test reports from two months prior to her first dental procedure, the patient’s results showed high total secretory IgA (SIgA) and elevated salivary antibodies to alpha-gliadin, indicating abnormal mucosal immunity and loss of tolerance to gluten. Her serologic assessments revealed immunoglobulin G (IgG) and IgA antibodies to a range of wheat/gluten proteins and peptides, gut bacterial endotoxins and tight junction proteins. These test results indicate gut dysbiosis, enhanced intestinal permeability, systemic gluten-reactivity, and immune response to other dietary macromolecules. The present case suggests that patients who experience severe allergic or pseudoallergic reactions to medication should be assessed and monitored for gut dysfunction. If left untreated this could lead to autoimmune reactions to self tissues. 1. Introduction Adverse reaction to many antibiotics and local analgesics have been reported in some patients [1–6]. Haptens are chemicals with very small molecular weights. By themselves, haptens do not elicit immune responses; however, they may do so by binding to other larger molecules such as tissue antigens or food proteins [7]. There is potential for interaction between haptens and food proteins with respect to the induction of oral tolerance by regulatory T cells and associated cytokines. It is also postulated that haptens can impact protein tolerance mechanisms through their ability to bind to soluble proteins or peptides within the gut-associated lymphoid tissue [7]. Although rare [1], anesthesic reactions are a growing concern [8]. Adverse reactions have been categorized as follows: toxic (drug overdose, rapid absorption, and intravascular injection), psychogenic, idiosyncratic, and allergic [2]. The usual trigger of the reactions is the paraben or sulfite preservatives in the anesthetics [1]. Reactions may range from psychomotor responses to Type I, Type II, Type III, and Type IV allergic
Detection of IgE, IgG, IgA and IgM antibodies against raw and processed food antigens
Aristo Vojdani
Nutrition & Metabolism , 2009, DOI: 10.1186/1743-7075-6-22
Abstract: We developed an enzyme-linked immunosorbent assay for the measurement of IgE, IgG, IgA and IgM antibodies against raw and processed food antigens. Sera with low or high reactivity to modified food antigens were subjected to myelin basic protein, oxidized low density lipoprotein, and advanced glycation end products (AGE) such as AGE-human serum albumin and AGE-hemoglobin.Compared to raw food antigens, IgE antibodies showed a 3–8-fold increase against processed food antigens in 31% of the patients. Similarly, IgG, IgA and IgM antibodies against modified food antigens overall were found at much higher levels than antibody reactions against raw food antigens. Almost every tested serum with high levels of antibodies against modified food antigens showed very high levels of antibodies against myelin basic protein, oxidized low density lipoprotein, AGE-human serum albumin and AGE-hemoglobin.We conclude that the determination of food allergy, intolerance and sensitivity would be improved by testing IgE, IgG, IgA and IgM antibodies against both raw and processed food antigens. Antibodies against modified food antigens, by reacting with AGEs and tissue proteins, may cause perturbation in degenerative and autoimmune diseases such as diabetes, atherosclerosis, inflammation, autoimmunity, neurodegeneration and neuroautoimmunity.Adverse reactions to foods in which the pathogenesis involves an immunological response to food components are appropriately called food-hypersensitivity reactions. This term is considered to be synonymous with "food allergy." This adverse immune reaction to food proteins affects many children and adults [1]. In a study using double-blind placebo-controlled food challenge, 39% of participants showed hypersensitivity to food antigens [2].Based on clinical presentation and antibody response, immune-mediated adverse reactions to foods can be divided into immediate and delayed hypersensitivity reactions. Immediate reactions to food antigens are IgE-mediated a
Humoral immunoreactivity to gliadin and to tissue transglutaminase is present in some patients with multiple myeloma
Zorica Juranic, Jelena Radic, Aleksandra Konic-Ristic, Svetislav Jelic, Biljana Mihaljevic, Ivan Stankovic, Suzana Matkovic, Irina Besu, Du?ica Gavrilovi?
BMC Immunology , 2008, DOI: 10.1186/1471-2172-9-22
Abstract: Sera from 61 patients with MM in various stages of disease, before, or after some cycles of conventional therapy were analyzed by commercial Binding Site ELISA tests. The control group consisted of 50 healthy volunteers. Statistical analysis of data obtained was performed by Mann Whitney Test.The higher serum IgA immunoreactivity to gliadin was found in 14/56 patients and in one of control people. The enhanced serum IgG immunoreactivity to gliadin was found in only two of tested patients and in two controls. The enhanced IgA immunoreactivity to tTG-2 was found in 10/49 patients' sera, while 4/45 patients had higher serum IgG immunoreactivity. The enhanced serum IgG immunoreactivity to RoSSà antigen was found in 9/47 analyzed MM patients' sera. Statistical analysis of data obtained revealed that only the levels of anti-tTG-2 IgA immunoreactivity in patients with MM were significantly higher than these obtained in healthy controls (P < 0.02)Data obtained showed the existence of the enhanced serum immunoreactivity to gliadin, tTG-2 and Ro/SSA antigens in some patients with MM. These at least partially could contribute to the immunological imbalance frequently found in this disease.Multiple myeloma (MM) is a clonal B-cell disorder which diagnosis comprise the examination of bone marrow for plasma cell infiltration, detection and quantification of monoclonal protein "M" component in the serum or urine, and evidence of end-organ damage (hypercalcemia, renal insufficiency, anemia or bone lesions). Many of the laboratory parameters contribute to myeloma diagnosis due to plenty of immunological disturbances [1]. It was shown that the antibodies contained in M component have various specificity to: some proteins, double-stranded DNA, several antibiotics [2], and sometimes to gliadin (and/or calreticulin?) [3].As the enhanced levels of the serum antibodies to gliadin are found in patients with celiac disease, as well as of antibodies to transglutaminase-2 (TTG-2) [4,5], to cal
Correlation analysis of celiac sprue tissue transglutaminase and deamidated gliadin IgG/IgA  [cached]
Eric V Marietta, Shadi Rashtak, Joseph A Murray
World Journal of Gastroenterology , 2009,
Abstract: AIM: To indirectly determine if tissue transglutaminase (tTG)-specific T cells play a crucial role in the propagation of celiac disease.METHODS: Anti-deamidated gliadin peptide (DGP) and anti-tTG IgA and IgG were measured in the sera of celiac patients (both untreated and treated). The correlations were determined by Spearman’s rank correlation test.RESULTS: In celiac patients, we found a very significant correlation between the production of DGP IgA and IgG (r = 0.75), indicating a simultaneous and ongoing production of these two isotypes reminiscent of oral vaccination studies. However, there was far less association between the production of tTG IgA and tTG IgG in celiac patients (r = 0.52). While tTG IgA was significantly correlated with DGP IgA (r = 0.80) and DGP IgG (r = 0.67), there was a weak correlation between production of anti-tTG IgG and the production of anti-DGP IgA (r = 0.38) and anti-DGP IgG (r = 0.43).CONCLUSION: These data demonstrate that the production of anti-tTG IgA is directly correlated to the production of anti-DGP IgG and IgA, whereas anti-tTG IgG is only weakly correlated. This result therefore supports the hapten-carrier theory that in well-established celiac patients anti-tTG IgA is produced by a set of B cells that are reacting against the complex of tTG-DGP in the absence of a tTG-specific T cell.
Gliadin Peptide P31-43 Localises to Endocytic Vesicles and Interferes with Their Maturation  [PDF]
Maria Vittoria Barone,Merlin Nanayakkara,Giovanni Paolella,Mariantonia Maglio,Virginia Vitale,Raffaele Troiano,Maria Teresa Silvia Ribecco,Giuliana Lania,Delia Zanzi,Sara Santagata,Renata Auricchio,Riccardo Troncone,Salvatore Auricchio
PLOS ONE , 2012, DOI: 10.1371/journal.pone.0012246
Abstract: Celiac Disease (CD) is both a frequent disease (1:100) and an interesting model of a disease induced by food. It consists in an immunogenic reaction to wheat gluten and glutenins that has been found to arise in a specific genetic background; however, this reaction is still only partially understood. Activation of innate immunity by gliadin peptides is an important component of the early events of the disease. In particular the so-called “toxic” A-gliadin peptide P31-43 induces several pleiotropic effects including Epidermal Growth Factor Receptor (EGFR)-dependent actin remodelling and proliferation in cultured cell lines and in enterocytes from CD patients. These effects are mediated by delayed EGFR degradation and prolonged EGFR activation in endocytic vesicles. In the present study we investigated the effects of gliadin peptides on the trafficking and maturation of endocytic vesicles.
Concurrent exposure to microbial products and food antigens triggers initiation of food allergy
Xiao Chen,Ping-Chang Yang
North American Journal of Medical Sciences , 2009,
Abstract: It is estimated that as much as 6-8% population suffers from food allergy or food antigen-related disorders. The prevalence keeps rising. So far we do not have identified remedy to treat food allergy. Avoidance of the offending food is the only effective method currently. Skewed T helper 2 polarization is one of the major feature in the pathogenesis of food allergy. However, the causative mechanism in the initiation of food allergy remains to be further understood. Research in food allergy has got giant advance in recent years. Several animal models have been established and used in food allergy study. One of the common features of these food allergy animal models is that most of them require using microbial products as adjuvant to sensitize animals. This review documents the recent advance in the mechanistic study on concurrent use of microbial products and food antigens to study food allergy.
CD69 expression on a-gliadin-specific T cells in coeliac disease  [cached]
S Perticarari,M Prodan,E Fragonas,S Canova
European Journal of Histochemistry , 2009, DOI: 10.4081/1650
Abstract: Coeliac disease (CD) is a T-cell mediated immunological disease of the small intestine which is triggered in susceptible individuals by ingestion of gluten. The pathogenic mechanism of coeliac disease, and the role that a-gliadin specific T cells play in mucosal lesions and their involvement in peripheral blood is not yet explained at all. Previous studies have reported proliferative response to a-gliadin measured with the classic assay of 3HTdR incorporation. We analysed the activation antigen CD69 on T cells from CD patients and normal individuals following stimulation with a-gliadin and different antigens (tetanus toxoid, peptides unrelated to gliadin and PHA). CD69 coexpression with T cell CD3+ and proliferation marker Ki67 was evaluated with time. CD69 coexpression with T cell CD3+, CD4+ and CD8+ was also evaluated. It was found that peripheral blood mononuclear cells (PBMC) of coeliac patients increased their percentage of CD69 positive T cells when stimulated with a-gliadin, in comparison with cells from controls. Significant T cell activation was found only in subjects not treated with the gluten free diet; a positive response was found also in two coeliac patients with selective IgA deficiency, anti-endomisium negative, without circulat- ing IgA anti a-gliadin or anti-tissue transglutaminase antibodies. The CD69 expression after stimulation was compared with the standard method of 3HTdR incorporation. Our data show that CD69 expression is useful to asses a specific T cell response to a-gliadin in coeliac disease. in a very short time. Moreover, the method allows to investigate T cell response at the lymphocyte subsets level, which represents a useful tool in the diagnosis of coeliac disease.
Gliadin Peptides Induce Tissue Transglutaminase Activation and ER-Stress through Ca2+ Mobilization in Caco-2 Cells  [PDF]
Ivana Caputo, Agnese Secondo, Marilena Lepretti, Gaetana Paolella, Salvatore Auricchio, Maria Vittoria Barone, Carla Esposito
PLOS ONE , 2012, DOI: 10.1371/journal.pone.0045209
Abstract: Background Celiac disease (CD) is an intestinal inflammatory condition that develops in genetically susceptible individuals after exposure to dietary wheat gliadin. The role of post-translational modifications of gliadin catalyzed by tissue transglutaminase (tTG) seems to play a crucial role in CD. However, it remains to be established how and where tTG is activated in vivo. We have investigated whether gliadin peptides modulate intracellular Ca2+ homeostasis and tTG activity. Methods/Principal Findings We studied Ca2+ homeostasis in Caco-2 cells by single cell microfluorimetry. Under our conditions, A-gliadin peptides 31–43 and 57–68 rapidly mobilized Ca2+ from intracellular stores. Specifically, peptide 31–43 mobilized Ca2+ from the endoplasmic reticulum (ER) and mitochondria, whereas peptide 57–68 mobilized Ca2+ only from mitochondria. We also found that gliadin peptide-induced Ca2+ mobilization activates the enzymatic function of intracellular tTG as revealed by in situ tTG activity using the tTG substrate pentylamine-biotin. Moreover, we demonstrate that peptide 31–43, but not peptide 57–68, induces an increase of tTG expression. Finally, we monitored the expression of glucose-regulated protein-78 and of CCAAT/enhancer binding protein-homologous protein, which are two biochemical markers of ER-stress, by real-time RT-PCR and western blot. We found that chronic administration of peptide 31–43, but not of peptide 57–68, induces the expression of both genes. Conclusions By inducing Ca2+ mobilization from the ER, peptide 31–43 could promote an ER-stress pathway that may be relevant in CD pathogenesis. Furthermore, peptides 31–43 and 57–68, by activating intracellular tTG, could alter inflammatory key regulators, and induce deamidation of immunogenic peptides and gliadin–tTG crosslinking in enterocytes and specialized antigen-presenting cells.
IgG Responses to Tissue-Associated Antigens as Biomarkers of Immunological Treatment Efficacy
Heath A. Smith,Brett B. Maricque,John Eberhardt,Benjamin Petersen,James L. Gulley,Jeffrey Schlom,Douglas G. McNeel
Journal of Biomedicine and Biotechnology , 2011, DOI: 10.1155/2011/454861
Abstract: We previously demonstrated that IgG responses to a panel of 126 prostate tissue-associated antigens are common in patients with prostate cancer. In the current report we questioned whether changes in IgG responses to this panel might be used as a measure of immune response, and potentially antigen spread, following prostate cancer-directed immune-active therapies. Sera were obtained from prostate cancer patients prior to and three months following treatment with androgen deprivation therapy (=34), a poxviral vaccine (=31), and a DNA vaccine (=21). Changes in IgG responses to individual antigens were identified by phage immunoblot. Patterns of IgG recognition following three months of treatment were evaluated using a machine-learned Bayesian Belief Network (ML-BBN). We found that different antigens were recognized following androgen deprivation compared with vaccine therapies. While the number of clinical responders was low in the vaccine-treated populations, we demonstrate that ML-BBN can be used to develop potentially predictive models.
Analytical Performance of a New Gliadin-Activated Anti-tTransglutaminase ELISA Test
Xavier Galan, Marcos López Hoyos, Eva Cacho, Isabel GoirigolzarriPetraki Munujos
The Open Autoimmunity Journal , 2009, DOI: 10.2174/1876894600901010079]
Abstract: 10.2174/1876894600901010079] Analytical Performance of a New Gliadin-Activated Anti-tTransglutaminase ELISA Test Xavier Galan, Marcos López Hoyos, Eva Cacho, Isabel Goirigolzarri and Petraki Munujos Significant progresses on the anti-tissue transglutaminase antibodies (anti-tTG) ELISA tests have been achieved since anti-tTG early development. Our goal was to study the optimization of the antigen immobilization and the antibody reaction conditions in an ELISA test for the detection of anti-tTG. Hence, three variants of an anti-tTG ELISA test were developed: tTG-Gliad-U, tTG-U and tTG-Gliad, according to the coating conditions (presence/absence of gliadin) and the stringency in the sample buffer (presence/absence of urea). To assess IgA and IgG anti-tTG frequencies we used a group of 117 CD patients, 36 under a gluten-free diet and 14 with a selective IgA deficiency, and a control group of 165 non-celiac patients. Sensitivity of IgA anti-tTG in CD patients with villous atrophy was 95.5% (tTG-Gliad-U), 65.0% (tTG-U) and 92.5% (tTG-Gliad), respectively. Sensitivity of the IgG anti-tTG assay was 79.0%, 21.0% and 79.0%, respectively. Specificities ranged between 92.9% and 100%. Significant lower IgA and IgG concentration values were observed in GFD CD patients. Sensitivity and specificity of IgG anti-tTG in CD patients with selective IgA deficiency were 64.3 and 100%, respectively. In conclusion, we have developed an ELISA test for IgA anti-tTG based on calcium and gliadin activated recombinant human transglutaminase. This test is sensitive and specific, and it is useful to ensure the compliance with diet of CD patients.
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