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Results for “Gliadin”

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At least 19 recordsLinked to original sources
PubMed1979

Failure to detect gliadin or gliadin binding sites in the skin of patients with dermatitis herpetiformis: immunofluorescence, organ culture and autoradiographic studies.

Recent investigations indicate an abnormal binding of gluten or gliadin to lymphocytes or intestinal mucosa cells in gluten sensitive enteropathy. Since dermatitis herpetiformis is closely associated to gluten sensitive enteropathy, similar receptors could also exist in the skin of patients with dermatitis herpetiformis. To prove this hypothesis, skin of normal volunteers and uninvolved skin of 3 patients with dermatitis herpetiformis was investigated for the presence of gliadin and gliadin binding sites. In vivo bound gliadin was not found by direct immunofluorescence using 3 different rabbit antigliadin antisera. In order to test skin for gliadin binding sites, normal sera and autologous dermatitis herpetiformis sera containing 25 mg% gliadin and tritium labeled gliadin, respectively, were used for incubation of normal and dermatitis herpetiformis skin cryocut sections and of normal and dermatitis herpetiformis skin specimens, grown under organ culture conditions. As checked by direct immunofluorescence and autoradiography, there was no specific in vitro binding of gliadin, indicating that gliadin does not fix to normal human or dermatitis herpetiformis skin. Thus, the role of gliadin in the fixation in vivo, of antibodies or immune complexes to skin in dermatitis herpetiformis, remains obscure.

Antibodies↗
PubMed1992

Specific circulating anti-gliadin IgG-class antibody does not mediate intestinal enteropathy in gliadin-fed mice.

The effects of specific circulating IgG antibody on the uptake of dietary antigen and in the generation of intestinal enteropathy have been investigated in Balb/c mice bred on a gluten-free diet. A monoclonal IgG1 antibody (GD3) was prepared against gliadin. After adoptive transfer into mice, this antibody was capable of mediating a type III hypersensitivity response in vivo to footpad challenge with gliadin. The titres of circulating GD3, as estimated in vitro by ELISA, correlated well with the degree of inflammation at sites of type III responses in vivo. Following footpad challenge with gliadin, titres of circulating GD3 antibody were reduced. GD3 antibody was tested for its ability to mediate inflammatory responses in vivo in the intestinal mucosa of mice fed with gliadin. Circulating GD3 antibody was removed selectively and specifically by dietary gliadin, compared to feeding with bovine serum albumin or maintenance on a gliadin-free diet only. However, we were unable to demonstrate any pathological changes in the intestine as a result of possible local antigen-antibody complex formation or deposition. Using radio-iodinated gliadin as a trace marker, no significant retention of gliadin in the intestinal mucosa was found in mice pre-injected with GD3 antibody. These data suggest that circulating IgG antibody has little effect on dietary antigen uptake in the gut, and alone is insufficient to mediate an enteropathy.

Animals↗
PubMed1979

Immunofluorescent serum gliadin antibodies in children with coeliac disease and various malabsorptive disorders. I. Technique, clinical evaluation and diagnostic use of a gliadin antibody assay using pyruvic aldehyde-treated human red cells.

An immunofluorescent gliadin antibody assay is described using pyruvic aldehyde-stabilized human erythrocytes coated with gliadin. Fifty coeliac children all had high serum IgG-antigliadin titres during a normal diet or a challenge with gluten. On a gluten-free diet (30 children), titres were much lower. In patients followed-up for one year on a gluten-free diet, an initial rise in titres was followed by a slow decline. On challenge, IgG-antigliadin titres showed a slow rise or persistence at the same level in most patients. Fifty-two percent of control children with malabosrptive disorders, but without the typical "flat" mucosal lesion on jejunal biopsy, were shown to have positive titres in their sera, as were 6% of normal children and 4% of adult blood donors. The fluorescent antibody technique was compared with methods commonly used to detect wheat-protein antibodies, and was found to be superior to all of them. The immunofluorescent gliadin antibody assay appears to be useful in following-up children with coeliac disease, and in selecting patients for jejunal biopsy, although it does not replace biopsy.

Antibodies↗
PubMed1979

Antibodies to gliadin as a screening test for coeliac disease. A prospective study.

The diagnostic value of gliadin antibody determination using the fluorescent immunosorbent test was examined in a prospective study of 57 children with gastrointestinal disease. Antibodies to gliadin were found in all 20 patients with active coeliac disease, whereas 7 of these children (37%) had a normal xylose absorption test despite a flat small gut mucosa. Only 4 (14%) of 28 children with other gastrointestinal conditions had antibodies to gliadin, invariably in low titre. After at least 2 years on a gluten-free diet none of 9 children with coeliac disease in remission had demonstrable gliadin antibodies. The gliadin antibodies disappear slowly, within 6 to 24 months, after withdrawal of gliadin from the diet. 0.8% (5/606) of a healthy control group of children, adolescents and adults (not biopsied) had gliadin antibodies in low titre. Increased mean cow's milk antibody titres were demonstrable in 8 (40%) of 20 patients with active coeliac disease as well as in 9 (32%) of 28 patients with other gastrointestinal lesions. Our studies show that determination of circulating gliadin antibodies is a worthwhile screening test in suspected cases of coeliac disease. In patients so selected there is a definite indication for small intestinal biopsy to confirm the diagnosis.

Adolescent↗
PubMed1976

Immunofluorescent antibodies against gliadin: a screening test for coeliac disease.

A sensitive and simple immunofluorescence test for gliadin antibodies is described, which may be suitable as a screening method for coeliac disease especially in cases with no clear-cut indication for performing a biopsy. In serum samples of 19 from 23 patients (83%) with coeliac disease proved by biopsy antibodies against gliadin could be detected. In a control group of 71 children in whom the clinical diagnosis of another malabsorptive disorder was made gliadin-IF-antibodies were found in only 3 children (4%). With better timing of blood sampling (first sample during a period with gluten containing food and in case of a negative result a second sample after 4-8 days of gluten withdrawal) the sensitivity of the screening test will be improved. The described gliadin-IF-test permits the classification of the antibodies into the different immunoglobulin classes. In each child with a positive result IgG antibodies against gliadin were detected. In 9 respectively 4 of the 19 patients with IgG antibodies IgA- respectively IgM-antibodies against gliadin were also found. Antibodies against at least one cow milk protein were identified in nearly all (91%) coeliac patients and in half (49%) of the patients with other malabsorptive disorders.

Antibodies↗
PubMed1975

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

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 peripheral-blood leucocytes (i.e., for a migration-inhibition factor [M.I.F.]). No M.I.F. activity was detected in the culture-medium when biopsy specimens from patients with coeliac disease or controls were cultured without added antigen. However, an M.I.F. was secreted into the culture-medium when biopsy specimens from patients with coeliac disease were cultured with alpha-gliadin. These findings suggest that there is a population of lymphocytes which are sensitised to gliadin in the intestinal mucosa of patients with untreated coeliac disease. They support the theory that a local C.M.I. reaction to gliadin may be the cause of villous atrophy and crypt hyperplasia in coeliac disease.

Adult↗
PubMed1978

Genetic aspects of wheat gliadin proteins.

Inheritance of gliadin components unique to three different varieties of common wheat (Triticum aestivum L.) was studied in F1 and F2 seeds of intervarietal crosses using protein patterns obtained by polyacrylamide gel electrophoresis in aluminum lactate buffer (pH 3.2). The patterns of F1 seeds of the crosses Cheyenne X Justin and INIA 66R X Justin evidenced all the bands present in the patterns of the parents; band intensities reflected gene dosage levels dependent on whether the contributing parent was maternal or paternal in accordance with the triploid nature of endosperm tissue. Most of the gliadin components examined segregated in accordance with control by a single dominant gene, but in two instances single bands in the one-dimensional electrophoretic patterns segregated in the F2 as expected if controlled by two genes. A method of two-dimensional electrophoresis was developed that resolved these apparently single bands into two components each, which could segregate independently. Linkage analysis provided evidence of codominant alleles and closely linked genes coding for gliadin protein components in both coupling and repulsion situations. The gliadin protein components seem to be coded for by clusters of genes located on chromosomes of homoeologous groups 1 and 6 in hexaploid wheats.

Aluminum↗
PubMed1977

Radioimmunoassay for antigliadin-antibodies using 14C-labelled gliadin.

A sensitive radioimmunoassay for antibodies to gliadin has been developed. Gliadin from wheat gluten was labelled with [1-14C]acetic anhydride to a specific activity of 2.6 X 10(6) dpm/mg. Immunological evidence is presented that the antigen was not essentially altered by the labelling procedure. Experimentally-induced antigliadin antibodies or sera of patients with coeliac disease (CD) were reacted with labelled gliadin and the immune complexes formed precipitated by antiglobulin. Precipitating antibodies were determined by incubating CD sera with labelled gliadin and measuring the radioactivity in precipitates formed without the addition of second antibody. Comparison with other methods for the detection of antigliadin antibodies, including immunoelectrophoresis, immunodiffusion and passive hemagglutination indicated that total and precipitating antibodies were determined only by RIA. The assay also provides information on the immunoglobulin class of antigliadin-antibodies present in sera of patients with coeliac disease.

Animals↗
PubMed1977

Coeliac disease: the abolition of gliadin toxicity by enzymes from Aspergillus niger.

1. Gliadin from which carbohydrate was removed by treatment with carbohydrase from Aspergillus niger was fed to three coeliac patients in remission. 2. Xylose absorption, mucosal morphology and brush-border enzymes were used to assess the toxicity of the carbohydrase-treated gliadin. 3. Gliadin treated with carbohydrases did not damage the intestinal mucosa of the coeliac patients. 4. The primary structure of the gliadin proteins was not altered by the enzyme treatment.

Adolescent↗
PubMed1992

Coeliac disease: characterisation of monoclonal antibodies raised against a synthetic peptide corresponding to amino acid residues 206-217 of A-gliadin.

A dodecapeptide of A-gliadin, which shares amino acid homologies with the E1b protein of adenovirus 12, was used to produce murine monoclonal antibodies. Five monoclonal antibodies were produced and were screened by enzyme linked immunosorbant assay, immunodot assay, and immunoblotting. The antibodies were tested against whole wheat gliadin and its alpha, beta, gamma, and omega subfractions, and the prolamins of rye, barley, oats, maize, millet, rice, and sorghum. Four of the five antibodies cross reacted with one or more of the coeliac non-toxic cereals--maize, millet, sorghum, and rice. The monoclonal antibody that did not cross react with these non-toxic cereals, did not recognize Frazer's fraction III, a peptic-tryptic digest of wheat gluten which is known to be toxic. The results suggest that the A-gliadin dodecapeptide shares a region of homology with cereals that do not exacerbate coeliac disease. This study does not support the hypothesis that prior infection with adenovirus 12 is a precipitating factor in coeliac disease.

Adenovirus E1B Proteins↗
PubMed1979

[Comparative studies of the preparation of alpha-gliadin].

alpha-gliadin was prepared from wheat flour by two different methods. The products were compared electrophoretically and by double radial immuno-diffusion. The alpha-gliadin fraction proved to be identical in the immunological test. Only the alpha-gliadin preparation received by ion exchange chromatography is suitable for further purification by multiple gel filtrations.

Electrophoresis, Polyacrylamide Gel↗
PubMed1978

Molecular weights of wheat gamma2-, beta6-, alpha7-, alpha8- and alpha9-gliadins.

The molecular weights of wheat gamma2-, beta6-, alpha7-, alpha8- and alpha9-gliadins were calculated with the aid of a computer technique from sedimentation equilibrium data obtained in an ultracentrifuge equipped with photoelectric scanner. The dissociative solvents, all at pH 3.1 by addition of HCl, included 3 M urea, 0.15 M KCl; 8 M urea, 0.15 M KCl and 6 M guanidine-HCl. The minimum molecular weights for gamma2-, alpha7- and alpha9-gliadins, obtained in 6 M guanidine-HCl, were 34 600, 30 400 and 30 900, respectively. The beta6- and alpha8-gliadins gave minimum molecular weights of 33 000 and 36 900, respectively, in 3 M urea, 0.15 M KCl.

Amino Acids↗