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gliadin/atrophy

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Association between villous atrophy in rheumatoid arthritis and a rheumatoid factor and gliadin-specific IgG.

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93 patients with rheumatoid arthritis (RA) were examined for histological or other evidence of gut abnormalities. 44 had raised levels of IgG to gliadin, and of these 38 (86%) were also positive for IgA rheumatoid factor (RF). 24 patients (15 with raised levels of IgA RF and wheat protein IgG [AB+]

[Case of anti-TPO/gliadin antibody-positive cerebellar atrophy that responded to intravenous immunoglobulin therapy begun 16 years after onset].

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We present a case of slowly progressive gait ataxia with a 16-year history in an 87-year-old woman. In 1994 she became aware of a slight unsteadiness while walking and cortical cerebellar atrophy was diagnosed. She had no familial history of neurological disorders. In 2007, idiopathic
OBJECTIVE Mucosal healing is important in celiac disease (CD) for the prevention of complications. However, obtaining duodenal biopsies is invasive, and there is currently no reliable surrogate marker for histological remission in clinical practice. We aimed to assess the role of a point-of-care

Gliadin antibodies identify gluten-sensitive oral ulceration in the absence of villous atrophy.

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This study demonstrates gluten-sensitive recurrent oral ulceration (ROU) in the absence of gastrointestinal abnormalities which is associated with a humoral response to wheat protein. Ten patients with severe ROU were investigated; all had normal small intestinal biopsies. Four patients had raised

Small-bowel mucosal inflammation in reticulin or gliadin antibody-positive patients without villous atrophy.

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BACKGROUND We investigated whether individuals with positive coeliac disease antibodies but without small-bowel villous atrophy have mucosal inflammation implicating gluten-sensitivity. METHODS Small-bowel mucosal morphology; CD3+, alphabeta+, and gammadelta+ T-cell receptor-bearing intraepithelial

Gliadin-dependent neuromuscular and epithelial secretory responses in gluten-sensitive HLA-DQ8 transgenic mice.

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Celiac disease is a gluten intolerance caused by a T-cell response against human leukocyte antigen (HLA)-DQ2 and DQ8-bound gluten peptides. Some subjects experience gastrointestinal symptoms in the absence of villous atrophy. Here we investigate the potential mechanisms of gut dysfunction in

[Oligosymptomatic celiac disease--axis correction of extreme genu valgum with a gliadin-free diet].

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We report on a girl who suffered from a severe left-sided Genu valgum. As there was a remarkable deterioration despite a conservative orthopedic therapy on osteotomy was planned. However, preoperative investigations revealed a malabsorption syndrome with osteomalacia due to coeliac disease. This

Measurement of gluten using a monoclonal antibody to a coeliac toxic peptide of A-gliadin.

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BACKGROUND Future European Community regulations will require a sensitive and specific assay for measurement of coeliac toxic gluten proteins in foods marketed as gluten-free. To avoid spurious cross reactions with non-toxic proteins, specific antibodies and target antigens are required. A synthetic

Increased lymphocyte infiltration in duodenal mucosa from patients with psoriasis and serum IgA antibodies to gliadin.

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In a screening study concerning IgA and IgG antibodies to gliadin (IgA AGA and IgG AGA, respectively) in psoriasis, raised levels of IgA and AGA were found to be more common than in a reference group. To determine whether elevated AGA levels were associated with an increased number of
Celiac disease, a chronic disorder of the small intestine, is caused by dietary gluten and is characterized by villous atrophy and local inflammation associated with infiltration of B and T lymphocytes and/or macrophages into the intestinal wall. In genetically predisposed individuals, the

IgG anti-gliadin determination with an immunological microfluidic system applied to the automated diagnostic of the celiac disease.

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In the present article, a novel microfluidic immunosensor coupled with electrochemical detection for anti-gliadin IgG antibody quantification is proposed. This device represents an important tool for a fast, simple, sensitive, and automated diagnostic for celiac disease, which is carried out through

Dietary intake, smoking, and transient anti-gliadin antibodies.

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BACKGROUND The detection of IgA anti-gliadin antibodies in adults can either be helpful in the diagnosis of coeliac disease, be persistent in subjects with normal jejunal mucosa, or occur transiently. We decided to investigate the effects of smoking, alcohol consumption, and dietary intake on the

Effect of frozen storage on the foaming properties of wheat gliadin.

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In this study, the effect of frozen storage on the foaming properties of wheat gliadin was investigated and further elucidated by evaluating its physicochemical changes. The foaming volumes of gliadin solution decreased while the foaming stability increased during the frozen storage. This was

Cell-mediated immunity to gliadin within the small-intestinal mucosa in coeliac disease.

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In an attempt to demonstrate local cell-mediated immunity (C.M.I.) to gliadin in patients with coeliac disease, fragments of jejunal-biopsy specimens were cultured in the presence and absence of alpha-gliadin and the culture-medium was assayed for its capacity to inhibit migration of normal human

Application of Deamidated Gliadin Antibodies in the Follow-Up of Treated Celiac Disease.

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BACKGROUND The role of serological tests such as IgA anti-transglutaminase autoantibodies has become increasingly important in celiac disease (CD) diagnosis. However, the efficiency of these tests for patient follow-up is controversial. We investigated the correlation of 12 different serological
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