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PubMed1978

Gluten challenge in treated coeliac disease.

Thirty-two children with a past diagnosis of coeliac disease were reinvestigated by means of gluten challenge. They had received a gluten-free diet for a mean period of 6-5 years (range 0-25-11-0) before gluten challenge, and had a mean age of 9-9 years (range 3-0-15-3) at the onset of challenge. Small intestinal biopsies were performed before and after the gluten challenge (at least 10 g natural gluten per day for 3 months in the majority) and, as judged by light microscopy and morphometric techniques, coeliac disease was confirmed in 25 (78%) of the 32 patients; challenge was continued in the remaining 7 for a total period of 2 years when biopsies were repeated in 6 children and all were normal. Serum and RBC folate, serum iron, Hb level, and clinical symptoms were unpredictable variables in identifying children who developed gluten-induced enteropathies. The social and emotional effects of gluten challenge are discussed. The results highlight the importance of gluten challenge and intestinal biopsy in the diagnosis of coeliac disease and strongly suggest that a normal biopsy after a 3-month gluten challenge (as described above) excludes coeliac disease.

Adolescent↗
PubMed2006

Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease.

Celiac disease is a T cell-driven intolerance to wheat gluten. The gluten-derived T cell epitopes are proline-rich and thereby highly resistant to proteolytic degradation within the gastrointestinal tract. Oral supplementation with prolyl oligopeptidases has therefore been proposed as a potential therapeutic approach. The enzymes studied, however, have limitations as they are irreversibly inactivated by pepsin and acidic pH, both present in the stomach. As a consequence, these enzymes will fail to degrade gluten before it reaches the small intestine, the site where gluten induces inflammatory T cell responses that lead to celiac disease. We have now determined the usefulness of a newly identified prolyl endoprotease from Aspergillus niger for this purpose. Gluten and its peptic/tryptic digest were treated with prolyl endoprotease, and the destruction of the T cell epitopes was tested using mass spectrometry, T cell proliferation assays, ELISA, reverse-phase HPLC, SDS-PAGE, and Western blotting. We observed that the A. niger prolyl endoprotease works optimally at 4-5 pH, remains stable at 2 pH, and is completely resistant to digestion with pepsin. Moreover, the A. niger-derived enzyme efficiently degraded all tested T cell stimulatory peptides as well as intact gluten molecules. On average, the endoprotease from A. niger degraded gluten peptides 60 times faster than a prolyl oligopeptidase. Together these results indicate that the enzyme from A. niger efficiently degrades gluten proteins. Future studies are required to determine if the prolyl endoprotease can be used as an oral supplement to reduce gluten intake in patients.

Amino Acid Sequence↗
PubMed1985

Studies on the significance of the R1 anti-reticulin antibody associated with gluten sensitivity.

The R1 type anti-reticulin antibody (ARA) is closely associated with gluten-sensitive enteropathy. It disappears from the circulation within a few weeks of starting on a gluten-free diet and often reappears following gluten challenge. It is not clear how gluten ingestion leads to the production of the ARA. We have investigated four possibilities. (1) The ARA is simply a food antibody generated against meats in the diet. (2) The ARA is an anti-gluten antibody which cross-reacts with reticulin. (3) Gluten binds to gut reticulin in vivo rendering reticulin autoimmunogenic. (4) Immune complexes of gluten and anti-gluten antibody bind to reticulin (by virtue of the affinity that gluten has for reticulin) to give the appearance of an ARA in immunofluorescence tests. Our results do not support any of these possible explanations, and the significance of the ARA remains obscure.

Antibodies↗
PubMed1985

Changes of serum antibody activities to various dietary antigens related to gluten withdrawal or challenge in children with coeliac disease.

IgG, IgA, and IgM serum antibody activities to gluten, a gluten fraction called glyc-gli, and antigens from egg and cow's milk were monitored by an enzyme-linked immunosorbent assay (ELISA) in children with coeliac disease during treatment and gluten challenge. The IgA activity to gluten antigens showed in most patients a rapid and significant reduction after gluten withdrawal, whereas the IgG activity decreased more slowly. During gluten challenge, both these activities rose significantly, and the increases could usually be detected several months before overt clinical relapse. Such determinations, therefore, represent a valuable adjunct in the follow-up of children with coeliac disease. IgA activities to egg and cow's milk antigens likewise tended to decrease after gluten withdrawal and increase during challenge, but the changes were less consistent for individual antigens. Nevertheless, monitoring of IgA activities to a selection of dietary antigens other than gluten may be particularly valuable when it comes to evaluation of intestinal responses in patients on a gluten-free diet.

Adolescent↗
PubMed2006

Autoantibody targeting of brain and intestinal transglutaminase in gluten ataxia.

OBJECTIVE: To investigate the presence of autoantibody deposition against type 2 tissue transglutaminase (TG2; a reliable marker of the whole spectrum of gluten sensitivity) in the jejunal tissue and brain of patients with gluten ataxia and in control subjects. METHODS: The authors evaluated jejunal biopsy samples from nine patients with gluten ataxia and seven patients with other causes of ataxia for the presence of TG2-related immunoglobulin deposits using double-color immunofluorescence. Autopsy brain tissue from one patient with gluten ataxia and one neurologically intact brain were also studied. RESULTS: IgA deposition on jejunal TG2 was found in the jejunal tissue of all patients with gluten ataxia and in none of the controls. The intestinal IgA deposition pattern was similar to that seen in patients with overt and latent celiac disease and in those with dermatitis herpetiformis. Widespread IgA deposition around vessels was found in the brain of the patient with gluten ataxia but not the control brain. The deposition was most pronounced in the cerebellum, pons, and medulla. CONCLUSIONS: Anti-tissue transglutaminase IgA antibodies are present in the gut and brain of patients with gluten ataxia with or without an enteropathy in a similar fashion to patients with celiac disease, latent celiac disease, and dermatitis herpetiformis but not in ataxia control subjects. This finding strengthens the contention that gluten ataxia is immune mediated and belongs to the same spectrum of gluten sensitivity as celiac disease and dermatitis herpetiformis.

Adult↗
PubMed2002

The humoral response in the pathogenesis of gluten ataxia.

OBJECTIVE: To characterize humoral response to cerebellum in patients with gluten ataxia. BACKGROUND: Gluten ataxia is a common neurologic manifestation of gluten sensitivity. METHODS: The authors assessed the reactivity of sera from patients with gluten ataxia (13), newly diagnosed patients with celiac disease without neurologic dysfunction (24), patients with other causes of cerebellar degeneration (11), and healthy control subjects (17) using indirect immunocytochemistry on human cerebellar and rat CNS tissue. Cross-reactivity of a commercial IgG antigliadin antibody with human cerebellar tissue also was studied. RESULTS: Sera from 12 of 13 patients with gluten ataxia stained Purkinje cells strongly. Less intense staining was seen in some but not all sera from patients with newly diagnosed celiac disease without neurologic dysfunction. At high dilutions (1:800) staining was seen only with sera from patients with gluten ataxia but not in control subjects. Sera from patients with gluten ataxia also stained some brainstem and cortical neurons in rat CNS tissue. Commercial anti-gliadin antibody stained human Purkinje cells in a similar manner. Adsorption of the antigliadin antibodies using crude gliadin abolished the staining in patients with celiac disease without neurologic dysfunction, but not in those with gluten ataxia. CONCLUSIONS: Patients with gluten ataxia have antibodies against Purkinje cells. Antigliadin antibodies cross-react with epitopes on Purkinje cells.

Aged↗
PubMed2004

Effects of concentration and composition of wet corn gluten feed in steam-flaked corn-based finishing diets.

Two finishing experiments were conducted to determine the effects of concentration (Exp. 1) and composition of wet corn gluten feed (Exp. 2) in steam-flaked corn-based diets on feedlot steer performance. In Exp. 1, 192 English x Continental crossbred steer calves (299 +/- 0.6 kg) were used in a completely randomized design with six dietary treatments (four pens per treatment). Treatments were six concentrations of wet corn gluten feed (Sweet Bran, Cargill Inc., Blair, NE; 0, 10, 20, 25, 30, and 35%) replacing steam-flaked corn (DM basis). All diets contained 10% corn silage, 5% supplement, and 3.5% tallow (DM basis). Gain efficiency and ADG were similar (P > 0.25) among treatments. Dry matter intake was lower (P < 0.10) with 0% wet corn gluten feed than with concentrations of 20, 25, and 35% WCGF. Dry matter intake did not differ among treatments containing wet corn gluten feed. In Exp. 2, 160 English x Continental crossbred steer calves (315 +/- 0.6 kg) were used in a completely randomized design with five dietary treatments (four pens/treatment). Treatments were assigned based on four ratios of steep to corn bran/germ meal mix in wet corn gluten feed plus a negative control (CON). Wet corn gluten feed was fed at 25% of the dietary DM and was made by mixing steep and corn bran/germ meal into the diet. The four concentrations of steep in wet corn gluten feed that comprised the ratios were 37.5, 41.7, 45.8, and 50% (DM basis), with the remaining proportion being the bran/germ meal mix. Bran/germ meal mix was comprised of 60% dry corn bran, 24% germ meal, and 16% fine-cracked corn (DM basis). All diets contained 10% corn silage, 5% supplement, and 3.5% tallow (DM basis). Daily gain did not differ (P = 0.18) among treatments. Gain efficiency did not differ between CON and 50% steep; however, G:F was decreased (P < 0.05) for concentrations of 37.5, 41.7, and 45.8% steep compared with CON. A linear improvement (P < 0.05) was observed for G:F as concentration of steep increased as a proportion of wet corn gluten feed. These data suggest that wet corn gluten feed can be used at concentrations up to 35% of the dietary DM without adversely affecting performance, and that steep has more energy than bran/germ meal in steam-flaked corn-based diets.

Animal Feed↗
PubMed1987

Effects of additional dietary gluten on the small-intestinal mucosa of volunteers and of patients with dermatitis herpetiformis.

In an attempt to confirm the existence of latent coeliac disease--dose-related gluten-sensitive enteropathy--we have increased dietary gluten by 20 g daily for 2 weeks, in 6 healthy adults and 11 patients with dermatitis herpetiformis (DH). Six of the DH patients had entirely normal jejunal morphology on a normal diet. Jejunal biopsy specimens were taken before and at the end of the study. Measurements of crypts, villi, and crypt mitoses were made on microdissected specimens; disaccharidases were assayed, and intraepithelial lymphocyte counts performed. In one of the six adult volunteers, gluten loading produced diarrhoea and jejunal biopsy abnormalities. Five DH patients on a gluten-free diet had deterioration of biopsy pathology after the gluten challenge. Features suggestive of a latent gluten-sensitive enteropathy were found in one of the other six DH patients; he developed disaccharidase deficiencies and villus atrophy when 20 g gluten was added to his usual gluten-containing diet. This study supports previous suggestions that a gluten-sensitive enteropathy may be latent and dose-related.

Adult↗
PubMed2004

[Risk markers for insulin-dependent diabetes mellitus and duration of exposure to gluten in celiac patients].

BACKGROUND: Celiac patients are at high risk of developing insulin-dependent diabetes mellitus, a condition that has a long pre-diabetic period. During this lapse, anti-islet cell antibodies serve as markers for future disease. This may be related with the duration of the exposure to gluten. AIM: To test the hypothesis that long term adherence to a gluten free diet decreases the frequency of risk markers for insulin dependent diabetes mellitus during adolescence and early adulthood. PATIENTS AND METHODS: 158 celiac patients were classified as: G1, (n=30 patients) studied at the time of diagnosis; G2 (n=97 patients) exposed to gluten as a result of non compliance with the gluten free diet and, G3 (n=31 patients) who had maintained a long term, strict gluten free diet. Isotype IgG anti-islet cell antibodies were detected by indirect immunofluorescence using monkey pancreas, results were reported in Juvenile Diabetes Foundation (JDF) units. RESULTS: Celiac patients exposed to a gluten containing diet had a significantly higher prevalence of anti-islet cell antibodies than those who had been exposed only briefly (p < 0.017). In addition, a significantly higher prevalence of anti-islet cell antibodies was observed in those patients whose exposure to gluten was longer than 5 years than in those whose exposure was shorter (p < 0.02). CONCLUSIONS: Celiac patients long exposed to gluten have a significantly higher prevalence of anti-islet cell antibodies than those exposed for a short period. This fact supports the hypothesis that the development of these antibodies is associated with the length of the exposure to gluten.

Adolescent↗
PubMed1984

Influence of the amount of dietary gluten on gastrointestinal morphology and function in dermatitis herpetiformis.

The individual daily intake of gluten was calculated in 45 patients with dermatitis herpetiformis (DH) on the basis of a depth interview about food habits. Gastric and small intestinal morphology and function were studied concurrently. Mean daily gluten intake was estimated to be 15 g, a figure which corresponds well to the average gluten intake in Sweden. There was a significant correlation between the degree of morphological mucosal changes of the small intestine and the quantity of gluten ingested. All patients with jejunal villous atrophy consumed more than 10 g gluten daily and all but one patient with normal jejunal villous structure had a gluten intake of less than 10 g/d. The findings suggest a dose-dependent effect of gluten on the intestinal mucosa. Conversely, the daily gluten intake was not correlated to gastric morphology, gastric acid secretion, serum gastrin levels or serum parietal cell antibodies. Patients with reduced ability to secrete gastric acid did not differ from the remaining patients in this respect. Whereas the coeliac-like enteropathy in DH seems to be caused by ingested gluten, the frequently occurring achlorhydric atrophic gastritis must be assumed to be of different immunopathogenesis.

Achlorhydria↗
PubMed1980

[In vitro proteolysis of casein and gluten by pancreatic enzymes].

The time-course of proteolysis of casein and gluten by pancreatic enzymes (trypsin, chymotrypsin, pancreatic juice) was studied in vitro with various concentrations of enzyme or substrate. The effect of a previous peptic proteolysis, with or without sodium phytate, on proteolysis by pancreatic juice was also studied. Proteolysis was evaluated by measuring the nitrogen in products solubilized in trichloroacetic acid (peptides + amino acids) and in phosphotungstic acid (amino acids). Without a previous peptic proteolysis, at a low enzyme/substrate ratio, the release of peptides and amino acids was greater for casein than for gluten. At a high enzyme/substrate ratio, peptide release by pancreatic juice and chymotrypsin was quite similar for casein and gluten but amino acid release was a little less for gluten. After a previous high peptic proteolysis without sodium phytate, pancreatic juice proteolysis, at a low enzyme/substrate ratio, was increased. Peptide release was similar for casein and gluten but amino acid release was a little less for the gluten. With sodium phytate, the release of peptides was quite similar for casein but was less for gluten. The release of amino acids was diminished in both cases. Thus, gluten was more resistant than casein to the action of pancreatic enzymes. Nevertheless, this was not necessarily observed when those enzymes were used for proteolysis at a high enzyme/substrate ratio or following a high peptic proteolysis. The differences between casein and gluten proteolyses have been discussed according to the specific action of the pancreatic enzymes. In conclusion, in comparing the proteolyses of various foods, it is important to use various enzyme/substrate ratios.

Amino Acids↗
PubMed2007

Myopathy associated with gluten sensitivity.

Ataxia and peripheral neuropathy are the most common neurological manifestations of gluten sensitivity. Myopathy is a less common and poorly characterized additional neurological manifestation of gluten sensitivity. We present our experience with 13 patients who presented with symptoms and signs suggestive of a myopathy and in whom investigation led to the diagnosis of gluten sensitivity. Three of these patients had a neuropathy with or without ataxia in addition to the myopathy. The mean age at onset of the myopathic symptoms was 54 years. Ten patients had neurophysiological evidence of myopathy. Inflammatory myopathy was the most common finding on neuropathological examination. One patient had basophilic rimmed vacuoles suggestive of inclusion-body myositis. Six patients received immunosuppressive treatment in addition to starting on a gluten-free diet; five improved and one remained unchanged. Among seven patients not on immunosuppressive treatment, four showed clinical improvement of the myopathy with a gluten-free diet. The improvement was also associated with reduction or normalization of serum creatine kinase level. The myopathy progressed in one patient who refused the gluten-free diet. Myopathy may be another manifestation of gluten sensitivity and is likely to have an immune-mediated pathogenesis. A gluten-free diet may be a useful therapeutic intervention.

Adolescent↗
PubMed1995

Absence of gluten-specific T lymphocytes in the skin of patients with dermatitis herpetiformis.

Dermatitis Herpetiformis (DH) is an immunobullous skin disease with an associated gluten-sensitive enteropathy. Withdrawal of gluten from the diet leads to the resolution of both the skin lesions and the enteropathy. A T cell-mediated immune response to gluten has been implicated in the damage to the gut; the possible gluten specificity of the T cell infiltrate in DH skin lesions has not, however, been investigated. T cell lines (TCL) were therefore established from the skin lesions of eight patients with DH by culturing skin fragments for 11-17 days with a medium supplemented with 20 U/ml of IL-2. In three cases, gliadin (fraction of gluten toxic to the DH gut) and irradiated, autologous peripheral blood mononuclear cells were also added. The TCL were stained for CD3, CD4, CD8, TCR alpha beta and gamma delta expression by indirect immunofluorescence, and their proliferative responses to mitogens and gluten fraction III (a peptic-tryptic digest of gluten) investigated. Of the eight CD3+ TCL, four were predominantly CD4+ (82.1-98.8%), three predominantly CD8+ (92.6-98.6%) and one TCL contained both 87.6% CD4+ and 95.2% CD8+ T cells, a substantial proportion of which were presumably double-labelled CD4+, CD8+ T cells. All eight TCL, which were almost exclusively TCR alpha beta +, proliferated in response to PHA whilst six out of the eight were stimulated by Concanavalin A. None of the TCL proliferated to gluten fraction III alone; however, two TCL showed increased proliferation to the antigen in the presence of exogenous IL-2 or IL-4 (10 U/ml) compared to cytokine alone.(ABSTRACT TRUNCATED AT 250 WORDS)

CD3 Complex↗
PubMed1993

Studies on the aetiology of coeliac disease: no evidence for lectin-like components in wheat gluten.

In an approach to examine the lectin-hypothesis in the pathogenesis of coeliac disease, the presence of lectin-like components in three wheat gluten preparations known to induce coeliac disease, gliadin, Frazer fraction III and an acetic acid/ethanol extract of gluten, was investigated. Lectin-like components in these wheat gluten preparations were traced in binding studies employing a variety of model glycoproteins glycosylated with the different types of N-linked oligosaccharides, i.e., those of the high mannose-, complex- and hybrid-type. Binding affinity of wheat proteins to these glycoproteins was analyzed by affinity dotting and blotting techniques and was compared to that of the well characterized lectins Galanthus nivalis agglutinin, Concanavalin A and wheat germ agglutinin. Though the three wheat gluten preparations exhibited binding reactivity for distinct model glycoproteins, no correlation was found between the type of N-glycosylation of the model glycoproteins and their binding capability to the different wheat gluten preparations. Moreover, binding of the three gluten preparations to the model glycoproteins could not be inhibited by competitive saccharides (methyl-alpha-D-mannopyranoside, N-acetyl-D-glucosamine, mannan). Enzymatic deglycosylation of the ligand glycoproteins with endo-beta-N-acetylglucosaminidase H (Endo H, EC 3.2.1.96) or peptide N-glycosidase F (PNGase F, EC 3.5.1.52) abolished their binding reactivity for the plant lectins, but did not affect binding of the wheat gluten preparations. These results give no evidence for the presence of lectin-like components in wheat gluten preparations and do question the 'lectin hypothesis' of coeliac disease.

Amidohydrolases↗
PubMed1997

Release of opioid peptides, gluten exorphins by the action of pancreatic elastase.

The release of opioid peptides, gluten exorphins A, which have been isolated from the pepsin-thermolysin digest of wheat gluten, with gastrointestinal proteases was examined. High levels of gluten exorphin A5 (Gly-Tyr-Tyr-Pro-Thr) immunoreactive materials were detected in the pepsin-pancreatic elastase digest by a competitive ELISA. From this digest, gluten exorphin A5, B5 and B4 were isolated. This means that these peptides are released in the gastrointestinal tracts after ingestion of wheat gluten. The yield of gluten exorphin A5 in the pepsin-elastase digest was larger than that in the pepsin-thermolysin digest. The gluten exorphin A5 sequence is found 15 times in the primary structure of the high molecular weight glutenin. The region from which gluten exorphin A5 was released by the action of pancreatic elastase was identified using synthetic fragment peptides.

Cross Reactions↗
PubMed2003

Characterization of gluten processing streams.

Corn gluten meal (CGM) is a major coproduct of corn wet milling; it has value because of high protein. However, variation in composition and high P content reduce market value. Data that characterize gluten streams would be helpful in identifying key processing steps that could be modified to improve the quality of CGM and increase processing efficiency. Few data are published in the literature on the detailed composition of gluten processing streams. The objective was to characterize the gluten process streams in a corn wet milling plant. Samples were obtained from one plant over a six month period and analyzed for dry matter (DM), total N (protein), ash and elements. DM and macroelement content of the streams were increased significantly during processing. Ash, priority pollutant elements and microelement concentrations were low and of little concern. About 38% of the N (protein) in light gluten was not recovered in the CGM; most of this was lost at the gluten thickener step into the gluten thickener overflow. Much of the P also was removed at this step. Modification of the gluten thickener overflow to increase N and reduce P could make CGM a more valuable coproduct and improve processing efficiency.

Conservation of Natural Resources↗
PubMed2003

Dynamic viscoelastic and tensile properties of gluten and glutenin gels of common wheats of different strength.

Dynamic viscoelastic properties at 25 degrees C of gluten and glutenin gels were obtained from Canadian common wheats of different strengths. The relaxation spectra showed a maximum intensity at a characteristic relaxation time (tau). The relaxation modulus associated with this maximum was taken as the strength of the glutenin or gluten gel transient network (G(tau)). The ratio of G(tau) for glutenin and gluten gels from the same cultivar ranged from 5.6 for an extra strong cultivar to 51.1 for a soft wheat. This gives indirect evidence that the gliadin fraction weakens the glutenin gel network more in weaker cultivars. In addition, the fact that both glutenin and gluten gels showed extensive stress relaxation coupled with the fact that addition of l-cysteine to a gluten gel eliminated the network structure at 25 degrees C and resulted in a power law stress relaxation spectrum suggests that the transient network in gluten is a reversible network. This power law relaxation pattern was not seen here for an entangled polymer melt (poly(dimethylsiloxane)). It was also found here that the viscosity of the gluten gel (G(tau) x tau) trended best with the tensile stress build-up in a uniaxial tensile test of gluten gels. Together, these results indicate that both network strength and relaxation times should be considered in characterizing the linear viscoelastic properties of hydrated cereal proteins.

Cysteine↗
PubMed2006

Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten.

Protein-glutaminase (PG) purified from Chryseobacterium proteolyticum was used to investigate its deamidation effects on wheat gluten. Water-insoluble gluten was able to be deamidated to the extent of deamidation degree (DD) 72% in 200 mM sodium phosphate buffer (pH 7) at 40 degrees C for 30 h. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis exhibited an upper shift of gluten bands with only deamidation for 1.5-2.0 h (DD 35-45%) compared to the bands of nondeamidated gluten. Results of Fourier transform infrared analysis revealed alterations in secondary structure of gluten by PG deamidation. The assignment within amide I region showed decreases in both inter- (around 1695 cm(-1)) and intramolecular beta-sheets (around 1680 cm(-1)) by deamidation suggesting the deterioration of the aggregation ability of gluten molecules. Solubility and emulsification properties of gluten at pH 7 were improved by deamidation, while both properties at pH 3 were deteriorated by deamidation. Enzyme-linked immunosorbent assay identified that allergenicity of deamidated gluten as compared to the nondeamidated cohorts was decreased remarkably as the deamidation time was prolonged.

Allergens↗