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PubMed2004

[Hidden food allergens: peanut and gluten--in Polish foodstuffs].

Undeclared allergens in processed products represent a major health problem for sensitized persons. Peanut flour and gluten are known as potent food allergens. The study was designed to evaluate with enzymeimmunoassay (ELISA) test kits the presence of gluten and peanut in Polish products. Hidden peanut contamination was detected in 4 of 34 (11.8%) processed foods (corn crisps, wafers, cereal bar and halva). 5 of 37 (13.5%) foodstuffs (cornflakes, corn crisps, bouillon cube, vegetable soup for infants, curry powder) contained undeclared gluten. The nutritional management of sensitized persons with food allergy requires new labeling regulations.

Allergens↗
PubMed2006

Cerebellar ataxia, peripheral neuropathy, "gluten sensitivity" and anti-neuronal autoantibodies.

"Gluten sensitive" neurological syndromes (ataxia, peripheral neuropathy, and other conditions) have been hypothesised in patients with various idiopathic neuropathologies, detectable anti-gliadin antibodies and HLA-DQ2 or DQ7. Further investigation of these cases has suggested a high incidence of anti-neuronal antibodies (anti-Purkinje, anti- neuronal nuclear, anti-GAD). This study investigates this contentious area. Over a two-year period, from a local UK population base of two million, seeing over 5000 general neurology referrals per year, we collected 20 cases with idiopathic ataxia, and 32 with idiopathic peripheral neuropathy, and referred them all for blinded antibody testing. 30 adult healthy blood donors, and 7 cases of hereditary ataxia were used as control subjects. Anti-gliadin antibodies (IgG and or IgA) were found in 40% of cases with idiopathic ataxia, 34% with idiopathic peripheral neuropathy, 17% healthy blood donors and 43% with hereditary ataxia. None was positive for antiPurkinje cell or anti-neuronal nuclear antibodies. Only two patients with idiopathic ataxia were positive for antiGAD antibodies (one also being anti-gliadin positive). We were unable to confirm the findings of other groups. First, cases of so-called "gluten sensitive" neurological syndromes were extremely rare in our centre. Second, our idiopathic cases, whether they be gliadin antibody seropositive or not (i.e. "gluten sensitive" or not) were rarely neuronal autoantibody positive.

Autoantibodies↗
PubMedDate not supplied

[The efficacy of enriching wheat meal, bread and gluten with L-lysine evaluated experimentally and theoretically].

The effect of enrichment of wheat meal, bread and gluten with L-lysine was studied by the routine method (basing on the biological value estimated on growing rats), and theoretically (by the changes in the potential extent of the biological value). A higher value of the enrichment effect in the second case has confirmed the existence of the compensation induced by significant lysine deficiency. Enrichment of the studied products with lysine leads to elimination of the compensation that consists in lysine economy through decreasing its oxidizing catabolism. The dependence of the biological value on the level of gluten protein in the ration was also studied. Maximum figures of the biological value were recorded at 15% of gluten protein level and they were decreased at 7 and 30% levels.

Animals↗
PubMed1989

[Evaluation of the effect of gluten-free diet on nutritional status of children with florid celiac disease].

A dynamics of Nutritional Status of 55 children with recently diagnosed coeliac disease was assessed during the treatment with gluten free diet. No deterioration of the nutritional status was seen in 34.1% of the investigated children (time 0) whereas different degree of nutritional deficiency was noted in the remaining 75.9% of children including 10% of children with severe deficiency. After a 2-year therapy with gluten-free diet a deteriorated nutritional status was only found in 8.6% of children. In 27 children with gluten free diet for nearly 3 years, with maintenance of histological remission, the percentage of children with nutritional deficiency was 7.2%. The fact of normal Nutritional Status in more than 30% of the investigated coeliac children at the time of the initial diagnosis seems to be an effect of early and proper initial diagnosis.

Celiac Disease↗
PubMed1986

Body composition and physiological casein and wheat gluten protein requirements of 180-day-old rats.

Six-month-old male rats were given diets with mounting casein and wheat gluten protein concentrations from 0% to 40% and after 14 days the optimum and minimum physiological doses were determined from changes in body nitrogen, body water, body weight and protein intake. The optimum dose for casein protein was 1.54 g/d (5% protein in the diet) and for wheat gluten protein 2.10 g/d (7.5% protein in the diet). The minimum casein and wheat gluten protein doses for 180- to 194-day-old rats, determined from body nitrogen changes, were 1499 mg/d (4.86%) and 1995 mg/d (7.12%) respectively, from body water changes 1561 mg/d (5.06%) and 2027 mg/d (7.23%) and from body weight changes 1333 mg/d (4.32%) and 1951 mg/d (6.06%). It should be noted that, unlike younger animals aged 35-49, 75-89 and 120-134 days, the optimum and minimum doses for six-month-old rats were approximately the same.

Amino Acids↗
PubMed1986

Effect of a calcium-binding gluten fraction on the superprecipitation of actomyosin.

The Ca2+-binding gluten fraction isolated by the authors has been shown to prolong the clearing phase and to shorten the physiological contraction phase of ATP activated natural actomyosin suspension in the presence of physiological potassium chloride in a dose dependent manner. The mean ATPase activity of myosin and actomyosin was calculated for each phase from the actual ATP concentrations, measured at 30 sec intervals, and from the phase lengths. The preparation was found markedly to inhibit the ATPase activity during the clearing and physiological contraction phase. Since both myosin and actomyosin ATPase is Ca2+-dependent, it is assumed that the inhibitory effect of the gluten fraction on ATPase activity may be mediated by its free Ca2+-binding capacity, resulting in modified phase lengths of actomyosin superprecipitation. On the basis of these experimental results a hypothesis is put forward of the part of the Ca2+-binding gluten fraction played in the pathomechanism of coeliac disease.

Actomyosin↗
PubMedDate not supplied

The contribution of some environmental factors to the development of cow's milk and gluten intolerance in children.

The analysis performed by the authors includes correlation between certain environmental factors i.e. the kind of food (natural, mixed, artificial), the role of infection and therapy applied (including antibiotic therapy), living conditions (residence place, the age of parents, number of siblings) and the body birth weight and the established food intolerance in children. The patients were hospitalized at the Clinic of Infectious Diseases of Children during 1978-1982. There were 45 children aged from 5 months to 5 years with gluten intolerance and 50 children aged from 2 months to 5 years with cow's milk intolerance. A close correlation between feeding and the development of food intolerance was stated. There had been found that 92% of children were given mixed cow milk already at the 2nd month of life and 46.6% were fed with this protein between the 2nd to the 3rd month of life. The former had cow milk allergy while the latter gluten intolerance. Due to longlasting diarrhea multiple antibiotic therapy was applied in the total group studied. Stool samples taken from the both groups revealed salmonella in 15.5% to 18.0%. Apart from this type of infection agent chemotherapy due to viral, parasitic and parenteral infections was used, too. The above presented findings confirmed significant role of the factors mentioned in the development and further progress of milk or gluten intolerance in the patients.

Animals↗
PubMed1988

Studies of intestinal lymphoid tissue. XI--The immunopathology of cell-mediated reactions in gluten sensitivity and other enteropathies.

Computerised image-analysis was used to quantitate small intestinal mucosae from celiac sprue and dermatitis herpetiformis patients, Gambian children with tropical-sprue-like malabsorption, first-degree celiac sprue relatives, and treated celiac sprue patients during challenge with a peptic-tryptic digest of gluten. A wide range of mucosal appearances was observed. Typically, 'flat' lesions (Type 2) revealed a reduced number of epithelial lymphocytes that were large and mitotically active. At the other extreme, mucosal architecture was relatively well preserved (Type 1) but surface epithelium contained an expanded population of small, non-mitotic lymphocytes, with or without crypt hyperplasia. Similar changes were observed in one-third of celiac relatives and following small dose gluten challenge. Larger dose challenges revealed a transition from Type 1 to Type 2 lesions over a 5-day period. Studies in a few patients over 2-4 years showed a similar type of progression. A major feature of this sequence was early appearance of crypt hypertrophy while villi persisted, indicating a role for factors other than increased loss of enterocytes from surface epithelium. These changes parallel the T lymphocyte-mediated events in graft-versus-host reactions in animals. It is thus concluded that the spectrum of immunopathologic changes observed in gluten sensitivity is fundamentally a cell-mediated effect, the degree of change being controlled by host genetic factors. In becoming flat, it appears obligatory for the mucosa to evolve through the earlier Type 1 lesion in which crypt hypertrophy is a prominent response.

Adult↗
PubMed1985

A radioimmunoassay for wheat gliadin to assess the suitability of gluten free foods for patients with coeliac disease.

Coeliac disease is a clinical condition characterised by malabsorption secondary to abnormalities of the small intestine. The condition is known to be exacerbated by wheat gliadin, rye, barley and possibly oats. The only assays that are available for testing for the presence of wheat gluten in foods are double diffusion against rabbit anti-gliadin antiserum and measurement of Kjeldahl nitrogen in products derived from wheat flour. We have developed a radioimmunoassay for wheat gliadin with a detection limit of 1 ng. Nominally gluten free foods based on wheat starch have been shown to contain up to 1.9 X 10(-2)% wheat gliadin. Bread made from Nutregen wheat starch which has now been withdrawn contains 6.4 mg gliadin per standard 30 g slice. A radioimmunoassay for wheat gliadin could be used to define standards for the suitability of gluten free products based on wheat starch for patients with coeliac disease.

Celiac Disease↗
PubMed1985

Gluten in pills: a hazard for patients with celiac disease.

It has recently been recognized that many pharmaceutical products contain gluten. Patients with celiac disease are at risk of acute illness if they are treated with such products. This paper lists the products available in Canada, according to the "Compendium of Pharmaceuticals and Specialties, 1985", that contain gluten and the Canadian manufacturers who stated that they do not use gluten as an excipient.

Canada↗
PubMed1984

Gluten intolerance (coeliac disease).

Coeliac disease is a permanent condition of gluten intolerance associated with characteristic gluten-sensitive changes in the jejunal mucosa. In Edinburgh and the Lothians Region of Scotland, the prevalence of the disease is one in 1637 (61/100,000) with considerable variation in age, and sex-specific prevalence and incidence. Several lines of evidence indicate an immunologic basis for the gluten-sensitive enteropathy in coeliac disease. Animal models of intestinal T cell-mediated reactions in the gut have shown pathologic features similar to those of coeliac disease. These include changes in villus and crypt architecture with crypt hyperplasia, and increased numbers of intraepithelial lymphocytes and of intraepithelial lymphocyte mitosis. Experimental CMI reactions also influence differentiation of goblet cells and expression of Ia antigen on epithelial cells, but these factors have not yet been reported for the coeliac mucosa. In addition to this circumstantial evidence, based on animal work, other factors which suggest that CMI reactions rather than antibodies are relevant to coeliac disease include the findings of antigliadin antibodies in a proportion of normal individuals, patients without gastrointestinal disease (seen in hospital), and patients with jejunal Crohn's disease. In addition, there is a well documented patient with adult onset primary hypogammaglobulinaemia and coeliac disease. The underlying pathogenesis in coeliac disease can be envisaged as failure of the normal inhibition of immune responses to this particular food antigen in the gut. Manipulation of immunoregulatory mechanisms would provide a new approach to treatment or cure of this disease and of other food protein-sensitive enteropathies.

Adult↗
PubMed1981

[Gluten enteropathy in children from south-eastern France (author's transl)].

Between 1969 and 1979, 123 cases of gluten-induced enteropathy were diagnosed in south-eastern France. The overall incidence of the disease was estimated at approximately one for 4 600 births. The mean age of the patients was 3.2 years. At the time of diagnosis, 71 children (57,7%) were less than 2 years old, and 52 children (42,3%) were above that age. There was a strong predominance of girls (60%) and North-Africans (48%). Children younger than 2 years presented with the usual malabsorption syndrome, whereas growth retardation, often isolated, was the main feature in older children. The relative increase observed since 1976 in the number of patients of the latter group despite a lower incidence of the disease was probably due to the withdrawal of infants' foods containing gluten. In 58 children followed up dietetic measures resulted in rapid clinical improvement, but healing of the mucosal lesions was much slower (19 months on average). In 28 patients who could be followed for longer periods, reintroducing gluten into the diet regularly led to histological relapse. These patients, however, had been selected for particular reasons. The true incidence of transient intolerance to gliadin is difficult to determine, since most subjects in perfect health refuse control biopsies.

Adolescent↗
PubMed1993

Protein synthesis in growing and adult rats on casein and gluten nutrition.

Male weaning rats were put on a diet with a physiological nutrient combination adjusted for age, milk casein (E/N = 0.79) and wheat gluten (E/N = 0.30) being the sources of protein. The net protein ratio (NPR) was evaluated weekly until 140 days of age. On days 70 and 140, L-(U-14C)-tyrosine was administered intraperitoneally and 12 h later specific tyrosine activity was determined in the protein fraction of liver and muscle by measuring the incorporation of the labeled amino acid in order to assess protein synthesis over the corresponding time period. Regression lines describing the relationship between animals' weight, age and protein source suggested that the daily weight increase was 6.99 g between days 30-77, 2.97 g between days 77-105 and 0.64 g between days 105-140. Muscle tyrosine levels in rapidly growing animals aged 70 days were 91.0 micrograms/g/12 h for casein and 65.6 micrograms/g/12 h for gluten. Liver tyrosine levels were 336.4 and 189.6 micrograms/g/12 h, respectively. The differences observed at this age were highly significant. In adult animals (140 days old) there were non-significant differences between tyrosine levels in the casein- and gluten-fed groups. The isotope study clearly showed that protein synthesis was reduced in growing and developing animals on vegetable nutrition, which is deficient in essential amino acids, (especially the limiting amino acid lysine, crucial for the utilization of all other amino acids in peptide chain synthesis). The low rate of amino acid utilization found in animals younger than 105 days is consistent with the findings obtained by the isotope method.

Aging↗
PubMed1977

Activation of the alternative pathway by gluten. A possible aetiological factor in dermatitis herpetiformis.

Gluten fractions are shown to activate the alternative pathway of complement when added to normal human serum. Breakdown of C3 and Factor B occur in a manner analogous to that when activated by zymosan, in the presence of MgEGTA and in serum devoid of classical pathway activity. The suggestion is made that bypass activation may be the primary event when gluten enters the serum across a damaged gut mucosa. Immune complexes containing non-complement fixing IgA antigluten antibody are carried to the skin where it is proposed that complexed gluten activates C3 and initiates an inflammatory reaction.

Antigen-Antibody Complex↗
PubMed1997

[Correlative study of the anti-gluten IgA level in celiac disease. Apropos of some observations].

This work concerns the level of anti-gluten IgA in Coeliac disease, following subjects who have already been diagnosed by clinical signs, biopsy and measurement of anti-gluten IgA. Even if this study had been limited only to a single patient, it would have shown well the clinical sensitivity to these levels, so allowing the following of the development, correlated with improvement of the clinical symptoms with lowering of the level of anti-gluten IgA.

Aged↗
PubMed1998

Anti-gliadin and anti-endomysium antibodies in children with celiac disease consuming a gluten free diet.

A group of 26 children (13 boys and 13 girls; average age 12.2 years) with CD who had been on a gluten free diet for 5-15 years was examined in order to find out how effectively they could manage their diet. The diagnosis of CD was established on the basis of ESPGAN criteria (1969). 5-15 years ago. Antigliadin antibodies, IgG-, and IgA-AGA (by fluorescence enzyme immunoassay), Gliastick by ELISA technique, and Anti-endomysium antibodies (by indirect immunofluorescence on sections of monkey esophagus) were examined in the serum. Only 5 patients had no antigliadin or anti-endomysium antibodies. In 21 cases the IgG-AGA showed positive results; the IgA-AGA was positive in 6, the Gliastick in 19, and the anti-endomysium antibodies in 8 cases. The main cause of the mismanagement of the diet was inadequate food labeling; so it seems to be important to also establish a Food Intolerance Data Bank in Hungary. The 5 sero-negative children volunteered for a gluten challenge; 3 of them became positive in a few weeks or months. Two patients remained negative even after 1 year. Their gluten sensitivity may not prove to be permanent.

Adolescent↗
PubMed1997

Matrix-assisted laser desorption/ionization time-of-flight mass spectrometric micro-analysis: the first non-immunological alternative attempt to quantify gluten gliadins in food samples.

The first epitope-independent procedure for rapidly quantifying gluten gliadins in food by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI/TOF-MS) based on the direct observation of the characteristic gliadin mass pattern is presented. This pattern was identified in both processed and unprocessed gluten-containing food samples. The procedure allows the micro-quantification of gluten in food samples below levels toxic for coeliac patients, with a linear response in the 0.4-10 mg per 100 g range and a high detection sensitivity similar to that of enzyme-linked immunosorbent assay (ELISA) systems. Food samples simultaneously analyzed by MALDI/TOF-MS and a highly sensitive laboratory-made sandwich ELISA revealed a good correlation between the two techniques. In addition, MALDI/TOF-MS provides a rapid screening system to determine the presence of gliadins in food samples by directly monitoring the occurrence of the protonated gliadin mass pattern. The procedure also permits the study of the alteration of gliadins in food during the baking process, providing data on the heart effect by changes in protein mass signals.

Bread↗
PubMed2001

Tissue transglutaminase and endomysial antibodies-diagnostic markers of gluten-sensitive enteropathy in dermatitis herpetiformis.

The association of Durhing's disease, commonly referred to as dermatitis herpetiformis (DH), with gluten-sensitive enteropathy (GSE) is supported by the presence of villous atrophy and endomysial antibodies (EMA). EMA are found to be a marker of GSE both in celiac disease (CD) and in DH. Since tissue transglutaminase (tTG) is believed to be the major autoantigen in GSE, the aim of our study was to determine the specificity and sensitivity of anti-tTG antibody ELISA compared to the EMA indirect immunofluorescence test. We studied 44 cases of DH, confirmed by the presence of IgA immune deposits in the dermal papillae, and 58 cases of CD conforming to the International Criteria of Diagnosing CD. The control group comprised 161 sera from patients with vesiculobullous disorders other than DH and 106 sera from normal healthy blood donors. Anti-tTG antibodies were detected in 36 of 44 DH (79%) and in 32 of 58 CD (55%) patients. EMA were positive in 33 of 44 DH (74%) and in 36 of 58 CD (62%) patients. Both the EMA and the antibodies to tTG were present in the majority of patients with DH and CD when they were on a normal gluten-containing diet and were absent when on a gluten-free diet for an extended period of time. There were, however, small discrepancies in positivity and negativity in tTG antibody-positive and EMA-negative patients and vice versa. There seems to be a correlation between the EMA titers and the anti-tTG antibody levels. This study confirms the high specificity and sensitivity of anti-tTG antibody ELISA for GSE and its strong correlation with EMA both in CD and in DH. The results of anti-tTG antibody and EMA assays were comparable; however, in DH, tTG was somewhat more sensitive than the EMA test. For screening of DH, it is advisable to perform both EMA and anti-tTG antibody tests.

Autoantibodies↗