Search results for "gliadin"

showing 10 items of 35 documents

Gliadin, zonulin and gut permeabilità: effects on celiac and non-celiac intestinal mucosa and intestinal cell lines.

2006

Objective. Little is known about the interaction of gliadin with intestinal epithelial cells and the mechanism(s) through which gliadin crosses the intestinal epithelial barrier. We investigated whether gliadin has any immediate effect on zonulin release and signaling. Material and methods. Both ex vivo human small intestines and intestinal cell monolayers were exposed to gliadin, and zonulin release and changes in paracellular permeability were monitored in the presence and absence of zonulin antagonism. Zonulin binding, cytoskeletal rearrangement, and zonula occludens-1 (ZO-1) redistribution were evaluated by immunofluorescence microscopy. Tight junction occludin and ZO-1 gene expression …

Cholera ToxinGene ExpressionEnzyme-Linked Immunosorbent AssayOccludindigestive systemCoeliac diseaseGliadinPermeabilityTight JunctionsIntestinal mucosaOccludinIntestine SmallmedicineAnimalsHumansIntestinal MucosaProtein PrecursorsCells CulturedIntestinal permeabilitybiologyTight junctionHaptoglobinsGastroenterologynutritional and metabolic diseasesZonulinMembrane ProteinsEpithelial Cellsmedicine.diseasePhosphoproteinsMolecular biologydigestive system diseasesRatsCeliac DiseaseMicroscopy FluorescenceParacellular transportImmunologybiology.proteinZonula Occludens-1 ProteinGliadin
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Identification of proteolytic enzymes from Eriphia verrucosa and Palinurus elephas capable to degrade gliadin

2009

In small intestinal disease, coeliac sprue, proline-rich gluten peptides from wheat, rye and barley are relatively resistant to gastrointestinal digestion, and therefore remain in the intestinal lumen to elicit immunopathology in genetically susceptible individuals. Since most serine endopeptidases are unable to hydrolyse proline residues, proline specific proteases may be therapeutic keys in digestive diseases. Partial hydrolysis reduces the risk of allergenic sensitization while total hydrolysis ensures the elimination of the allergenicity of whey protein (Villad´oniga and others 2007). Kimoto and others (1998) reported that 18-, 31-, 37- and 58-kDa wheat allergens were recognized by the …

Eriphia verrucosaproteolytic enzymePalinurus elephasSettore BIO/10 - Biochimicagliadincoeliac
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Wheat amylase trypsin inhibitors drive intestinal inflammation via activation of toll-like receptor 4

2012

Ingestion of wheat, barley, or rye triggers small intestinal inflammation in patients with celiac disease. Specifically, the storage proteins of these cereals (gluten) elicit an adaptive Th1-mediated immune response in individuals carrying HLA-DQ2 or HLA-DQ8 as major genetic predisposition. This well-defined role of adaptive immunity contrasts with an ill-defined component of innate immunity in celiac disease. We identify the α-amylase/trypsin inhibitors (ATIs) CM3 and 0.19, pest resistance molecules in wheat, as strong activators of innate immune responses in monocytes, macrophages, and dendritic cells. ATIs engage the TLR4–MD2–CD14 complex and lead to up-regulation of maturation markers a…

GliadinMice0302 clinical medicineHEK293 CellImmunology and AllergyTriticumPlant Proteins2. Zero hungerMice Knockout0303 health sciencesToll-like receptorMice Inbred C3Hfood and beveragesPlant ProteinU937 CellsAcquired immune system3. Good health030211 gastroenterology & hepatologymedicine.symptomTrypsin InhibitorsHumanSignal TransductionImmunologyMolecular Sequence DataInflammationBiologyProinflammatory cytokineCell Line03 medical and health sciencesImmune systemImmunitymedicineAnimalsHumansAmino Acid Sequence030304 developmental biologyInnate immune systemSequence Homology Amino AcidAnimalBIO/13 - BIOLOGIA APPLICATAnutritional and metabolic diseasesHordeumImmunity InnateToll-Like Receptor 4Mice Inbred C57BLCeliac DiseaseHEK293 CellsImmunologyMyeloid Differentiation Factor 88TLR4Trypsin Inhibitor
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Gliadin-mediated production of polyamines by RAW264.7 macrophages modulates intestinal epithelial permeability in vitro

2015

AbstractCeliac disease (CD) is an immune-mediated enteropathy sustained by dietary gluten in susceptible individuals, and characterized by a complex interplay between adaptive and innate responses against gluten peptides (PTG). In a recent contribution we have demonstrated that the treatment with PTG induces the expression and activity of arginase in both murine macrophages and human monocytes from healthy subjects, thus suggesting a role for arginine and its metabolites in gluten-triggered response of these cells. Here we further explore this field, by addressing the effects of PTG on polyamine synthesis and release in murine RAW264.7 macrophages, and how they affect epithelial permeabilit…

Intestinal permeabilityArginineArginaseInflammationBiologyIntestinal permeabilitymedicine.diseaseIn vitroGliadinCell biologyArginasechemistry.chemical_compoundBiochemistrychemistrymedicinePutrescinebiology.proteinPolyaminesMolecular MedicineCeliac diseaseSecretionmedicine.symptomGliadinMolecular BiologyBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
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Testing safety of germinated rye sourdough in a celiac disease model based on the adoptive transfer of prolamin-primed memory T cells into lymphopeni…

2014

The current treatment for celiac disease is strict gluten-free diet. Technical processing may render gluten-containing foods safe for consumption by celiac patients, but so far in vivo safety testing can only be performed on patients. We modified a celiac disease mouse model to test antigenicity and inflammatory effects of germinated rye sourdough, a food product characterized by extensive prolamin hydrolysis. Lymphopenic Rag1−/− or nude mice were injected with splenic CD4+CD62L−CD44high-memory T cells from gliadin- or secalin-immunized wild-type donor mice. We found that: 1) Rag1−/− recipients challenged with wheat or rye gluten lost more body weight and developed more severe histological…

MaleAdoptive cell transferGlutensPhysiologyT-LymphocytesGerminationDiseaseDiet Gluten-FreeMiceIn vivoPhysiology (medical)medicineAnimalsEnteropathyFood scienceProlaminB cell2. Zero hungerchemistry.chemical_classificationHepatologybiologyDuodenitisSecaleGastroenterologyfood and beveragesmedicine.diseaseGlutenAdoptive Transfer3. Good healthAnti-Bacterial AgentsIntestinesCeliac Diseasemedicine.anatomical_structurechemistryImmunologybiology.proteinGliadinProlaminsAmerican journal of physiology. Gastrointestinal and liver physiology
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Evidence of Transient IgA Anti-Endomysial Antibody Positivity in a Patient with Graves’ Disease

1999

<i>Background:</i> Anti-endomysial antibodies (EmA) have been shown to have a high specificity and sensitivity in celiac disease (CD) diagnosis, and their use is considered effective in improving the diagnostic accuracy of CD screening. <i>Aims:</i> To report the clinical details of transient IgA EmA positivity in a patient with Graves’ disease. <i>Methods:</i> We screened 48 patients (7 males, age range 19–79, median 58.3 years) for CD. They were hospitalized for thyroid disorders (30 patients had autoimmune hypothyroidism and 18 had Graves’ disease with clinical hyperthyroidism associated with diffuse goitre). CD screening was carried out on all patient…

MaleImmunoglobulin ATime FactorsBiopsyGraves' diseasemedicine.disease_causeGliadinCoeliac diseaseAutoimmunityMyofibrilsImmunopathologyHumansMedicineAgedbiologybusiness.industryGastroenterologyMiddle AgedEndomysiummedicine.diseaseGraves DiseaseImmunoglobulin ACeliac Diseasemedicine.anatomical_structureImmunologyAnti-gliadin antibodiesbiology.proteinFemaleAntibodybusinessFollow-Up StudiesDigestion
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IgA antiendomysial antibodies on the umbilical cord in diagnosing celiac disease. Sensitivity, specificity, and comparative evaluation with the tradi…

1996

The possibility of assaying antiendomysial antibodies (EmA) on the human umbilical cord instead of monkey esophagus has recently been suggested. We therefore evaluated in patients with celiac disease (CD) the sensitivity and specificity of EmA and of antigliadin antibodies (AGA) for both umbilical cord and monkey esophagus.We studied 36 patients with CD and atrophy of the intestinal mucosa (median age, 1.4 years), 14 patients with CD on gluten-free diet for 8-12 months (median age, 3.0 years), 36 controls without gastrointestinal disease (median age, 4.0 years), and 72 patients with cow's milk protein enteropathy (CMPE) (median age, 1.2 years). AGA and EmA on monkey esophagus were assayed w…

MalePathologymedicine.medical_specialtyAdolescentEnzyme-Linked Immunosorbent AssaySensitivity and SpecificityUmbilical cordGliadinCoeliac diseaseUmbilical CordEsophagusAtrophyIntestinal mucosaImmunopathologymedicineAnimalsHumansEsophagusChildFluorescent Antibody Technique IndirectAutoantibodiesbiologybusiness.industryGastroenterologyInfantHaplorhinimedicine.diseaseImmunoglobulin ACeliac Diseasemedicine.anatomical_structureGastrointestinal diseaseChild Preschoolbiology.proteinFemaleReagent Kits DiagnosticAntibodybusiness
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Response to Molina-Infante et al.

2013

MaleSettore MED/09 - Medicina InternaHepatologybusiness.industryNon-celiac gluten sensitivityGastroenterologyComputational biologymedicine.diseaseGliadinmedicineHumansFemalebusinessNon-celiac gluten sensitivityFood HypersensitivityTriticumAutoantibodies
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Diagnostic efficacy of the ELISA test for the detection of deamidated anti-gliadin peptide antibodies in the diagnosis and monitoring of celiac disea…

2009

Background and Aim: We evaluated the diagnostic performance of an ELISA test for anti-gliadin IgA and IgG antibodies, which uses synthetic deamidated gliadin peptides (anti-gliadin antibodies, AGAs) as coating; the results were compared with a test that uses extracted gliadin (AGAe). Methods: The study was conducted on the sera of 144 patients suffering from celiac disease (CD), including 20 patients with IgA deficiency and 9 who were following a gluten-free diet (GFD), and 129 controls. Results: In the 115 CD patients (without IgA deficiency), the sensitivity of AGAe IgA and IgG was 32.2 and 60.9%, whereas that of AGAs IgA and IgG was 59.1 and 72.2%. The specificity for AGAe IgA and IgG, a…

MaleSettore MED/09 - Medicina InternaTissue transglutaminaseClinical BiochemistryGliadinSerologyImmunology and AllergyMedicinedeamidated anti-gliadin peptide antibodieChildFalse Negative Reactionsreproductive and urinary physiologybiologyHematologyMiddle Agedfemale genital diseases and pregnancy complicationsMedical Laboratory TechnologyChild PreschoolAnti-transglutaminase antibodiesAnti-gliadin antibodiesELISAFemaleAntibodyMicrobiology (medical)AdultAdolescenteducationEnzyme-Linked Immunosorbent AssaySensitivity and SpecificityAntibodiesYoung AdultAntigenELISA; deamidated anti-gliadin peptide antibodies; celiac diseaseHumansFalse Positive ReactionsSerologic TestsAgedAutoantibodiesTransglutaminasesbusiness.industryBiochemistry (medical)Public Health Environmental and Occupational HealthAutoantibodyOriginal ArticlesImmunoglobulin Abody regionsCeliac DiseaseROC CurveCase-Control StudiesImmunoglobulin GImmunologybiology.proteinbusinessGliadinPeptides
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Immunologic and absorptive tests in celiac disease: can they replace intestinal biopsies?

1993

The sensitivity and specificity of several immunologic and absorption tests were determined in infants with celiac disease (31 male, 39 female; median age, 2.6 years) in different phases of the disease and in a group of control subjects with chronic diarrhea of different etiologies (32 male, 28 female; median age, 1.2 years). Intestinal biopsy was performed both in the patients and in the controls as a 'gold standard' for the diagnosis. The anti-gliadin antibody (AGA) IgG values showed a sensitivity of 89% and a specificity of 47%; AGA IgA were 69% sensitive and 92% specific; anti-endomysial antibodies (EmA) were 100% sensitive and 97% specific; the xylose test was 71% sensitive and 53% spe…

Malemedicine.medical_specialtyPathologyBiopsyFluorescent Antibody TechniqueEnzyme-Linked Immunosorbent AssayDiseaseGastroenterologySensitivity and SpecificityCoeliac diseaseGliadinFecesInternal medicinemedicineFatty mealHumansIntestinal MucosaChildXylosebiologybusiness.industryGastroenterologyInfantGold standard (test)medicine.diseaseControl subjectsImmunoglobulin ACeliac DiseaseIntestinal AbsorptionChild PreschoolImmunoglobulin GAnti-gliadin antibodiesbiology.proteinEtiologyFemaleAntibodybusinessScandinavian journal of gastroenterology
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