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PubMed2001

Gluten sensitivity in sporadic and hereditary cerebellar ataxia.

Gluten sensitivity, with or without classical celiac disease symptoms and intestinal pathology, has been suggested as a potentially treatable cause of sporadic cerebellar ataxia. Here, we investigated the prevalence of abnormally high serum immunoglobulin A (IgA) and IgG anti-gliadin antibody titers and typical human lymphocyte antigen (HLA) genotypes in 50 patients presenting with cerebellar ataxia who were tested for molecularly characterized hereditary ataxias. A high prevalence of gluten sensitivity was found in patients with sporadic (7/26; 27%) and autosomal dominant (9/24; 37%) ataxias, including patients with known ataxia genotypes indicating a hitherto unrecognized association between hereditary ataxias and gluten sensitivity. Further studies are needed to determine whether gluten sensitivity contributes to cerebellar degeneration in patients with hereditary cerebellar ataxia. Patients with hereditary ataxia (including asymptomatic patients with known ataxia genotype) should be considered for screening for gluten sensitivity and gluten-free diet trials.

Adolescent↗
PubMed2002

Evaluation by SDS-Page and immunoblotting of residual antigenicity in gluten-treated wine: a preliminary study.

Hydrolyzed gluten could be a suitable alternative to animal proteins in the wine clarification process, but the residual proteins could constitute a risk for subjects suffering from celiac disease or allergy to cereals. The aim of this study was to investigate possible traces of gluten in treated wine and to assess its antigenicity in commercial products. The presence of gluten in treated wine was evaluated by an electrophoretic method [sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE)] and its immunoreactivity was evaluated by immunoblotting. No traces of protein were found in untreated samples. A small quantity of protein was detected in treated wine but this produced no significant immunochemical reaction. In an experimental clarification process, a protein fraction was detectable in untreated samples and in the first stages of the clarification process. However, there was no significant gluten-associated immunochemical reaction in clarified wine samples, confirming strong binding between the clarifying agent and the phenolic fraction. In conclusion, the clarifying process strongly reduced the amount of protein material, at least in red wines. Under the most restrictive tests of the presence of gluten in the product, the predictable residue of gluten in wine was safe for celiac subjects. For allergic subjects the data are less conclusive because there is no known limit for allergic reactions, but clear labeling of the method of treating the wine should also protect this group of consumers.

Antigens↗
PubMed1976

Positive skin reactions to gluten in coeliac disease.

Following intradermal challenge with a peptic-tryptic digest of gluten, visible Arthus-type skin reactions were observed in 33 per cent of a group of 55 adults with coeliac disease. Of the 23 with untreated disease positive skin reactions occurred in 52 per cent. There was an invariable association between serum gluten antibodies and the presence of a skin reaction to gluten, indicating that gluten antibody combination with gluten in the skin provides the basis of the skin response. Since no false positive reactions were found in 52 normal controls, skin testing with gluten may provide a useful adjunct to the diagnosis and management of coeliac disease, especially in the outpatient department.

Adult↗
PubMedDate not supplied

Chemistry, coeliac-toxicity and detection of gluten and related prolamins in foods.

Some recent advances in the understanding of the chemistry of gluten proteins and its relationship to the toxicity of different fractions in coeliac disease (gluten intolerance) is reviewed. Most recent studies on gluten toxicity have used in vitro analyses of cellular immune activation by gluten fractions and peptides. Our work indicates that gliadin is the most active of the different protein families found within the wheat grain and that a specific peptide sequence located in the amino terminus domain of alpha-gliadin and containing the sequence proline-serine-glutamine-glutamine was most active. Improvement in the dietary management of coeliac disease is possible by use of test kits for the detection of gluten in foods. Both laboratory kits and home test kits (suitable for use by individual coeliacs) are available and reliably detect gluten from wheat, rye and barley even after cooking or baking.

Celiac Disease↗
PubMed1991

[Gluten-free diet in infantile autism. A therapeutic trial].

It has been postulated that there may be a connection between wheat-gluten/milk-casein and mental disorders such as schizophrenia, hyperactivity and autism. In this study seven patients with infantile autism, three before puberty and four after puberty, were given a gluten-free diet. Three children were provoked with gluten/placebo in a double-blind study. Four young patients participated in an open study and were given a gluten-free diet in six months. Behaviour was registered before, during and after the period with a gluten-free diet. Visual Analogue Scale and Real Life Rating Scale were used to register changes in behaviour. No connection was observed between gluten and behaviour typical for these patients. On the contrary, the gluten-free diet seemed to be another negative factor leading to further social isolation in this group of highly socially handicapped patients and families.

Adolescent↗
PubMed1990

Diagnosis and treatment of gluten-sensitive enteropathy.

Celiac disease is defined as a GSE. The small intestinal histological appearance of villous atrophy with crypt hyperplasia, inflammatory cell infiltrate of the lamina propria, and epithelial cell abnormalities is characteristic but not pathognomonic of the disorder. Confirmation of the diagnosis depends on histological improvement when gluten is removed from the diet and deterioration following gluten reintroduction. The pathogenesis of celiac disease appears to require interaction between a number of factors both intrinsic (genetic susceptibility, activation of the immune system) and extrinsic (gluten susceptibility, activation of the immune system) and extrinsic (gluten and possibly other environmental factors). The diagnosis of GSE may be delayed or missed unless the clinician is aware of the broad clinical spectrum of disease presentation. Although celiac disease is widely perceived as a malabsorption syndrome of childhood, the diagnosis is increasingly being made for the first time in adult life. A significant number of patients have no GI symptoms whatsoever. Small intestinal biopsy through the endoscope is the initial and definitive investigation. Most patients show excellent clinical and histological response to a gluten-free diet. The commonest reason for poor response is continuing intentional or inadvertent gluten intake. A minority of patients develop complications, in particular intestinal malignancy, including enteropathy-associated T-cell lymphoma.

Celiac Disease↗
PubMed1989

Transplantation of skin grafts in rats fed plant protein wheat gluten.

The effects of diets containing low biologic value plant protein wheat gluten and the high biologic value protein casein on skin allograft survival were studied in growing Charles River (C.D. strain) rats. Five groups of weanling rats were fed 16% casein or gluten with or without supplementation with the amino acids L-lysine and L-threonine. Allografts were obtained from the hooded Lister strain. Autograft experiments were also performed. The skin bed and the allografts were prepared by round-punch biopsies, and the grafts were retained in situ by cellophane tape dressings. In the gluten-fed rats, no rejection of allografts was observed during the 45-day study period. In the casein-fed rats, a 90% rejection rate occurred on Days 10-14 after transplantation. The absence of rejection in gluten-fed rats may be explained by an impaired cellular immune response due to protein malnutrition. Supplementing the gluten diet with the essential amino acids L-lysine and L-threonine restored the rejection rate to that of the control rats. The cell-mediated immune response, as measured by in vitro stimulation of lymphocytes with the mitogen concanavalin A, was severely impaired by the gluten diet. These experiments indicate that low biologic value protein diet in the rat is associated with skin allograft acceptance, probably due to impairment of cell-mediated immunity.

Animals↗
PubMed1986

Small bowel mucosa from celiac patients generates 15-hydroxyeicosatetraenoic acid (15-HETE) after in vitro challenge with gluten.

Celiac disease (gluten-sensitive enteropathy [GSE]) is a disorder characterized by small intestinal mucosal injury caused by dietary exposure to wheat gluten and similar proteins. There is evidence that the mucosal injury is immunologically mediated and there is an inflammatory infiltrate present in the mucosa. It is postulated that release of lipid-derived inflammatory mediators may be involved in the pathogenesis of the mucosal injury. Jejunal mucosal biopsy samples from patients with GSE and from a group of patients who were subsequently shown to have normal jejunal mucosa were incubated with tritiated arachidonate and a peptic/tryptic digest of either gluten or casein. Generation of lipid-derived inflammatory mediators was measured by beta-scintillation counting after separation of metabolites by reverse-phase high performance liquid chromatography with two different buffer systems. The predominant arachidonic acid metabolite generated was 15-hydroxyeicosatetraenoic acid (15-HETE). Mucosa from newly diagnosed GSE patients on a normal diet generated more 15-HETE than either control patients or GSE patients maintained on a gluten-free diet. In addition, gluten acted as a specific stimulus to 15-HETE production by mucosa from the GSE patients on a normal diet. 15-HETE has a number of biologic effects that could contribute to the mucosal changes seen in GSE, and the specific release of 15-HETE by gluten suggests involvement in the pathogenesis of the disorder.

Adolescent↗
PubMed1981

Gluten-free diet for dermatitis herpetiformis: the long-term effect on cutaneous, immunological and jejunal manifestations.

In 32 patients with dermatitis herpetiformis (DH) we studied the effect of gluten-free (22 patients) and gluten-reduced (10 patients) diet for periods ranging between 15 and 43 months. Variables such as cutaneous manifestations, dependence on dapsone, IgA deposits in the skin, small-bowel function, and jejunal mucosal morphology were studied. 59% of the patients on gluten-free diet could stop dapsone medication and remain symptom-free, compared with 10% on gluten-reduced diet. The time needed to achieve this therapeutic response varied from 5 to 31 months. IgA decreased in the skin to a degree which roughly paralleled the morphological normalization of the jejunal mucosa. In no patient, however, did the IgA completely disappear. It is suggested that IgA is not the main factor inducing DH symptoms, but rather a secondary phenomenon. Repeated jejunal biopsies revealed normalization of the mucosal histology in 52% of the patients on gluten-free diet, compared with none in the gluten-reduced diet group.

Adolescent↗
PubMed1984

Physiological casein and gluten protein requirements of growing rats.

Using mounting casein and wheat gluten protein values (0-40%) in the animals' diet, the optimum and minimum physiological daily doses were determined in 49-day-old growing rats from changes in their body water, body nitrogen and protein intake. The optimum physiological doses were identical with the peak of linearity of the given parameters, which coincided with a 15% casein protein and a 20% gluten protein concentration in the diet. This was also confirmed by the maximum body amino acid values, which were found in animals given a 15% casein or 20% gluten protein diet. It was further confirmed by the finding of significantly elevated alanine aminotransferase and aspartate aminotransferase activity in the liver of animals with a higher intake of the above protein sources. The minimum physiological dose of the given protein was determined from the equations of the regression curves in the presence of zero changes in the body nitrogen or body water content. The optimum physiological daily doses of casein and wheat gluten protein were 3.25 g and 4.05 g respectively. The minimum physiological daily doses of casein protein were 268 mg (from body nitrogen changes) and 371 mg (from body water changes) and the minimum physiological daily doses of gluten protein were 892 mg (from body nitrogen changes) and 1,000 mg (from body water changes). The above indicators demonstrate, in the presence of higher and high dietary concentrations, that an intake of the given proteins over and above the optimum physiological daily dose is at the very least uneconomical (gluten), if not harmful (casein), making this a highly topical problem for further study.

Aging↗
PubMed1997

Compliance to a gluten-free diet in adolescents, or "what do 300 coeliac adolescents eat every day?".

BACKGROUND/AIMS: Compliance to a gluten-free diet is currently an important issue in the care of both adolescent and adult coeliac patients. The aim of this study was evaluate the compliance to a gluten-free diet and the dietary habits in general of coeliac teenagers and young adults. PATIENTS AND METHODS: A total of 306 adolescents and young adults were followed in a coeliac clinic. They were grouped on the basis of: strict compliance to a gluten-free dietary regimen (n = 223, 73%); dietary transgressions 2-3 times/month (n = 46, 15%); and frequent transgressions or a full gluten-containing diet (n = 37, 12%). RESULTS: The physical growth status was optimal in the male patients, and less so in the females, but was not related to compliance. Symptoms were very rare in all groups. Compliance to the diet was related to sex (females better than males), age (younger better than older), good school grades, and good self-esteem. CONCLUSIONS: The teen-agers studied consumed an average of about 11.32 kg/month of gluten-free products provided by the Italian Health System. Gluten-free pasta and bread were the daily choices. The mean cost for each patient was estimated to be Italian Lire 242,640 (ECU 124) per month or ECU 1,490/year.

Adolescent↗
PubMed1995

Effect of gluten exorphins A5 and B5 on the postprandial plasma insulin level in conscious rats.

The effect of exogenous opioid peptides, gluten exorphins A5 and B5, which were isolated from the enzymatic digest of wheat gluten, on the postprandial insulin level were examined in rats. The oral administration of gluten exorphin A5 at a dose of 30 mg/kg w. potentiated the postprandial plasma insulin level and the effect was reversed by naloxone. The administration of gluten exorphin B5 showed a similar effect at a higher dose (300 mg/kg w). Furthermore, intravenous administration of gluten exorphin A5 at a dose of 30 mg/kg w. also stimulated the postprandial insulin release. The fact that orally and intravenously administered gluten exorphin A5 stimulates insulin release suggests that it modulates pancreatic endocrine function by the action after the absorption rather than within the the gastrointestinal tract.

Administration, Oral↗
PubMedDate not supplied

Mechanism of heat and shear mediated aggregation of wheat gluten protein upon mixing.

Changes in wheat gluten network structure upon mixing were studied from the biochemical analyses of gluten/glycerol blends mixed at 100 rpm with increasing times (up to 30 min) and temperatures of regulation (40, 60, and 80 degrees C). Whereas mixing induced protein solubility loss, the reduction of disulfide bonds restored protein extractability. But disulfide bond reduction became less efficient in promoting gluten extractability as mixing severity increased. This feature is consistent with the formation of a three-dimensional protein network stabilized by the formation of an increasing number of interchain disulfide bonds. Mixing induced a transient increase in free thiol groups while total thiol-equivalent groups dropped continuously. The changes were attributed to a shear-mediated scission of gluten disulfide bonds followed by oxidation of the thiyl radical moieties. Upon mixing, gluten solubility loss showed an Arrhenius-type temperature dependence with activation energy of 33.7 kJ.mol-1 instead of the more than 100 kJ.mol-1 reported for heat-induced gluten protein solubility loss. To explain this discrepancy, we postulated that during mixing, the disulfide interchange reactions are mediated by thiyl radicals in place of free thiol groups. A general model accounting for shear and temperature effects on gluten network structure is proposed.

Dimerization↗
PubMed2004

Anti-ganglioside antibodies in children with coeliac disease: correlation with gluten-free diet and neurological complications.

BACKGROUND: Emerging evidence points to humoural mechanisms in neurological complications of coeliac disease. Immunoglobulin G anti-ganglioside antibodies have been reported in coeliac disease patients with neuropathy, suggesting an immune response to peripheral nerve antigens. No data are so far available on anti-ganglioside antibodies in coeliac disease children or on antibody modifications after gluten-free diet. AIM: To evaluate the presence of antibodies to ganglioside antigens in children with coeliac disease, their modification after gluten-free diet, and possible correlations with neurological manifestations. METHODS: Sera from 42 coeliac disease children, before and after gluten-free diet, were tested by enzyme-linked immunosorbent assay for the presence of antibodies (immunoglobulin M, immunoglobulin A, immunoglobulin G) to gangliosides. Thirty-five sera of age-matched children with dyspepsia were used as control. RESULTS: High anti-ganglioside antibodies titres were present in two patients. In one patient, antibody titre reversed after gluten-free diet, whereas in the other one the titre increased after diet. Neither one complained of neurological symptoms. CONCLUSIONS: Anti-ganglioside antibodies do not seem to correlate with gluten ingestion or with neurological manifestations in children with coeliac disease. Mechanisms different from gluten exposure may be implicated in the antibody production. An ongoing prospective study will help clarify the role, if any, of these antibodies in coeliac disease.

Adolescent↗
PubMed1998

Hepatic damage in gluten sensitive enteropathy.

BACKGROUND: Gluten sensitive enteropathy has been reported to occur concomitantly with liver abnormalities, such as primary biliary cirrhosis, chronic active hepatitis and primary sclerosing cholangitis. METHODS: Duodenal biopsy was performed in nine children (all with short stature, five with chronic diarrhea and three with hepatosplenomegaly of unknown etiology) with a possible diagnosis of gluten sensitive enteropathy. All of the patients had different abnormalities in serum aminotransferase levels. With the help of laboratory investigations, viral, autoimmune, metabolic and toxic etiologies which cause hepatic damage were excluded. Liver biopsy was performed in five of these patients, two showing fibrosis and three nonspecific reactive changes. Gliadin antibodies were measured in six cases. RESULTS: Intestinal mucosal histopathology was compatible with gluten sensitive enteropathy in all patients. While immunoglobulin (Ig) G gliadin antibodies were positive in all cases, only three cases were found to have positive IgA gliadin antibodies. After a gluten-free diet, levels of transaminases fell to normal within 3 months and remained so in seven of these patients. A second intestinal biopsy, which was performed after 1 year of gluten-free diet revealed normal intestinal mucosa in all patients. CONCLUSION: Gluten sensitive enteropathy should be considered when evaluating a child with elevated levels of serum transaminase and in cases with cryptogenic liver disease.

Alanine Transaminase↗
PubMed1993

Morphometric analysis of intestinal mucosa. V. Quantitative histological and immunocytochemical studies of rectal mucosae in gluten sensitivity.

To study changes in rectal mucosa that might be attributable to the effects of gluten, rectal biopsy specimens from untreated and treated gluten sensitised subjects were analysed morphometrically and by immunohistochemical techniques and were compared with a series of disease control mucosae. Although morphometry showed increased populations of plasma cells, lymphocytes, and mast cells in the mucosae of untreated patients, which were reduced (except for mast cells) by dietary gluten restriction, immunohistochemical techniques were far more sensitive in defining these changes. There were highly significant increases in CD3+ and gamma delta+ lymphocytes within both the lamina propria and the epithelium while neutrophils (CD15+ cells) were not at all prominent. Activated (CD25+) lymphocytes expressing interleukin (IL)-2 receptors were increased in lamina propria, usually subjacent to basal lamina, although a few IL-2R+ intraepithelial lymphocytes were found: other IL-2R+ cells were deemed to be macrophages (CD68+). These results clearly indicate that in untreated, gluten sensitised subjects the rectal mucosa shows a lymphoplasmacytoid reaction that is responsive to gluten restriction. The absence of neutrophilia suggests that this lesion is not a conventional inflammatory type proctitis, but rather one presumed to be induced by gluten antigen(s) present in the faecal stream--that is, a cell mediated form of response.

CD3 Complex↗
PubMedDate not supplied

Gluten intolerance and skin diseases.

Gluten sensitivity with or without coeliac disease (CD) symptoms and intestinal pathology has been suggested as a potentially treatable cause of various diseases. CD is a chronic disease which improves on withdrawal of wheat gliadins and barley, rye and oat prolamins from the diet. There have been numerous reports linking CD with several skin conditions. A body of evidence shows that dermatitis herpetiformis is actually a cutaneous manifestation of CD. Autoimmune diseases, allergic diseases, psoriasis and miscellaneous diseases have also been described with gluten intolerance. Dermatologists should be familiar with the appraisal of gluten sensitive enteropathy and should be able to search for an underlying gluten intolerance (GI). Serological screening by means of antigliadin, antiendomysial and transglutaminase antibodies should be performed. HLA typing is often useful in association with serologic tests. Intestinal biopsy is usually needed to establish the diagnosis of CD or GI. Thus, gluten intolerance gives rise to a variety of dermatological manifestations which may benefit from a gluten-free diet.

Celiac Disease↗
PubMed1989

Anti-gliadin antibody specificity for gluten-derived peptides toxic to coeliac patients.

The specificities of serum and intestinal antibodies from coeliac and normal individuals towards gluten-derived peptides, known to be toxic in coeliac disease, has been investigated. Though untreated coeliacs had high serum antibody levels towards gliadin and some gluten-derived peptides, antibody specificities to various toxic gluten-derived peptides were similar to normal patients. Further, no significant binding in any patient group was found to the alpha-gliadin-derived peptides B1342 (Wieser, Belitz & Ashkenazi, 1984) or the 12 amino-acid A-gliadin peptide (Kagnoff, 1985). There appears to be no direct relationship between the toxicities and the antigenic reactivity of gluten-derived peptides. Thus, the intestinal damage in coeliac disease is probably not primarily caused by antibody-dependent mechanisms. The specificities of several monoclonal antibodies which bound to wheat prolamins as well as prolamins from other coeliac-toxic cereals have also been investigated with these toxic gluten-derived peptides, in order to identify possible common epitopes. No monoclonal antibody tested bound the B1342 and 12-amino-acid A-gliadin peptide. However the monoclonal antibodies which were specific for the coeliac-toxic cereal prolamins did show the strongest binding to other coeliac-toxic gluten-derived peptides.

Adult↗