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PubMed1987

In vitro cross-linking of gluten into high-molecular-weight polymers with transglutaminase.

From the amino acid composition of gluten proteins and the substrate specificity of transglutaminases (TGase) we concluded that gluten proteins can be favourable substrates for TGases due to their high glutamine content. By use of sodium dodecyl sulfate polyacrylamide gel-electrophoresis it was demonstrated that from gluten-ES and gluten-TS high-molecular-weight proteins developed in the presence of Ca2+ and red blood cell lysate containing TGase. When ovalbumin or deamidated gluten were applied as substrates no high-molecular-weight products were formed. Upon spectrophotometric measurements we found that covalent cross-links (isopeptide bonds) formed under the effect of TGases presumably cause a change in the position of chromophore groups in the substrates. Absorption decrease was detected between 274-276 nm as a result in the case of gluten-TS and gluten-ES used as substrates for TGase. No such change occurred in ovalbumin and deamidated gluten, applied as controls, under the influence of TGase. On the basis of our experiments it is postulated that the first step in gluten toxicity is presumably the binding of gluten to the intestine mucosa. In this binding the high transglutaminase activity in the intestines of coeliac patients and the high glutamine content of gluten may have an important role.

Celiac Disease↗
PubMed1985

Isolation and physicochemical and functional properties of a calcium binding gluten fraction.

Each milligram gluten protein isolated from bread contains 0.03-0.06 mumol calcium. On theoretical grounds we have concluded that this calcium quantity is bound to the free carboxyl groups not participating in peptide bonds of dicarbonic aminoacids, especially glutaminic acid, making up a large proportion within the aminoacids of gluten. After treatment with EGTA, a well-known calcium complex forming compound, two gluten fractions can be distinguished: water-soluble gluten-ES, and gluten-EP soluble in acetic acid. The aminoacid composition of gluten-ES is similar to that of unfractionated gluten. It is rich in aminodicarbonic acid (glu), aminodicarbonic acid amide (gln) and proline. Further properties of gluten-ES are: immunological similarity to gluten; a molecular mass of 36 000 dalton; an absorption maximum at 275.6 nm; a Ca2+-binding capacity of 0.72 mumol Ca2+/mg protein as measured by atomic absorption spectrophotometry and by Ca2+ ion selective electrode; inhibitory effect of a small quantity (25-30 micrograms) of the compound on the Ca2+-Mg2+ dependent ATPase and Ca2+-uptake of fragmented sarcoplasmatic reticulum. Preliminary experiments have demonstrated that gluten-ES has an influence on other calcium ion mediated systems like actomyosin superprecipitation. We put forward the hypothesis that by its Ca2+-binding capacity, gluten-ES is capable of influencing the level of free calcium and may thus play a part in the pathomechanism of coeliac disease.

Amino Acids↗
PubMed1983

[Gluten-sensitive enteropathy--in the light of new clinical and pathogenetic aspects].

The corn protein gluten causes the gluten-sensitive enteropathy in susceptible persons (HLA-antigens). The diagnosis is made on the basis of the morphological criteria of villous atrophy of the jejunal mucosa and the clinical observation that the malabsorption can be healed by a gluten-free diet. The disease, which occurs in children and adults, is a distinct entity. Life-long adherence to a gluten-free diet is difficult. Intentional or unintentional reintroduction of gluten often causes masked disease states. These are best classified on the basis of electron-microscopy study of the jejunal biopsy. We propose a new classification of the phases of remission. A group of diseases exist which are closely related to gluten-sensitive enteropathy. Frequently villous atrophy is detectable. However, the disease does not respond to a gluten-free diet. The pathophysiology of these diseases is at present unclear. Diseases involving autoimmune processes also appear to be associated with gluten-sensitive enteropathy. The common factor is probably an immuno-genetic defect. This is supported by the existence of common HLA-antigen constellations. Gluten has been characterised in vitro as a lectin with oligomannose specificity. This provides a new pathomechanism for the gluten induced enterocytic destruction.

Celiac Disease↗
PubMed2005

Microfiltration of gluten processing streams from corn wet milling.

In corn wet milling, dry matter can be separated from liquids in process streams with centrifuges or vacuum belt filtration (VBF). Because separations usually are not complete, dry matter can be lost in the liquid streams (overflow from the gluten thickener centrifuge and filtrate from VBF). This represents a loss of nutrients, especially protein, to low valued coproducts and reduces quality of water for recycling within the process. The objective was to compare microfiltration of light and heavy gluten process streams to conventional separation methods. Batches of light and heavy gluten were obtained from a wet mill plant and processed by microfiltration. Samples of permeate and concentrate from microfiltration were analyzed and compared to corresponding streams from wet milling. Microfiltration of light gluten resulted in concentrate and permeate streams similar in composition to conventionally processed light gluten using a centrifuge, suggesting that microfiltration is as effective as centrifugation in partitioning solids and water in light gluten. Dewatering of heavy gluten found that conventional VBF caused dry matter concentrations in gluten cake to be higher than concentrate from microfiltration. Permeate from microfiltration of heavy gluten had higher concentrations of ash and lower soluble nitrogen than filtrate from VBF. Microfiltration was able to remove more ash from concentrate, which may improve the value of wet milling coproducts. These data demonstrated microfiltration has potential for separation of light and heavy gluten streams, but more data are needed on effectiveness and practicality.

Centrifugation↗
PubMed1988

Aggressive gluten challenge of dermatitis herpetiformis cases converts them from seronegative to seropositive for IgA-class endomysial antibodies.

The responses to aggressive gluten challenge of two dermatitis herpetiformis patients with normal gut mucosa and negative serum findings for IgA endomysial antibodies while on normal diets indicate that these patients have a latent gluten-sensitive enteropathy. This was shown further by the control of skin lesions in both cases and in one case by the clearance of the induced gut lesions with a gluten-free diet. Specifically, for 12 to 20 weeks, aggressive gluten challenge (1 to 2 gm/kg/day) of these two patients was followed by both the appearance of and a rise in titer of IgA endomysial antibodies with an exacerbation of skin lesions. After 27 weeks of gluten challenge, histologic studies of the gut showed grade III flattening of the jejunal mucosa in the patient who developed IgA endomysial antibodies 19 weeks before biopsy was performed but not in the patient in whom IgA endomysial antibodies appeared 7 weeks before biopsy was performed. When both patients were placed on a gluten-free diet, IgA endomysial antibodies titers showed negative findings and the skin lesions subsided. It was possible to discontinue dapsone treatment after 30 weeks on a gluten-free diet in one patient and after 33 weeks in the other. It is important to note in the patient who developed grade III (significant) gut pathology after gluten challenge that a third biopsy taken 59 weeks after starting a gluten-free diet revealed a return to a grade II (insignificant) level of villus atrophy. Thus if sulfones are contraindicated in such cases, patients can be treated successfully with a gluten-free diet.

Child↗
PubMed2005

Low-dose gluten challenge in celiac sprue: malabsorptive and antibody responses.

BACKGROUND & AIMS: Undiagnosed patients with symptoms of celiac sprue often present to physicians after establishing dietary gluten exclusion. Although they must resume a gluten-containing diet for evaluation, there are no guidelines regarding duration of the gluten challenge, gluten dose, or monitoring parameters. We investigated the effects of a short-term gluten challenge in asymptomatic treated adult celiac patients on intestinal absorption and celiac antibody tests. METHODS: Eight adult asymptomatic celiac patients consumed either 5 or 10 g of partially hydrolyzed gluten per day in an orange juice mixture for 21 days while maintaining their usual gluten-free diet. A symptom questionnaire, serum antibodies (antigliadin immunoglobulin [Ig]A and antitransglutaminase IgA and IgG), D-xylose urine excretion test, and 72-hour quantitative fecal fat test were monitored. RESULTS: Two patients (25%) had at least 1 abnormal celiac antibody test at baseline. There was no increase in antibodies during gluten exposure compared with baseline for any of the patients (P > .05). At baseline, 1 patient had abnormal urine xylose excretion, and 3 patients had abnormal fecal fat values. At day 15 of gluten challenge, all patients had reduced xylose absorption compared with baseline (P = .0019), and 5 of 8 participants (63%) reduced their xylose excretion to the abnormal range. Seven of 8 patients (88%) had increased fecal fat excretion at day 15 (P = .026), and 6 of these (75%) had steatorrhea by day 15. CONCLUSIONS: Short-term gluten challenge in asymptomatic adult celiac patients produces carbohydrate and fat malabsorption but does not increase transglutaminase and antigliadin antibody titers.

Aged↗
PubMed1998

T-cell reactivity to wheat gluten in patients with insulin-dependent diabetes mellitus.

Dietary wheat gluten has been associated with the risk of diabetes in animal models of human insulin-dependent diabetes mellitus (IDDM). To evaluate the role of wheat gluten as a T cell antigen in human IDDM, we studied the cell-mediated immune response to wheat gluten in patients with IDDM and in control subjects. The cellular response to gluten was measured by the peripheral blood mononuclear cell (PBMC) proliferation test, and the results were expressed as a stimulation index (SI). We observed an enhanced cellular immune response to gluten (SI > or = 3) in seven of 29 patients with newly diagnosed IDDM (24.1%), in six of 39 patients with a longer duration of IDDM (15.4%), and in two of 37 non-diabetic controls (5.4%). Reactivity of T cells to gluten was associated with IDDM at diagnosis (P = 0.03), whereas patients with longer duration of IDDM did not differ from controls (P = 0.16). Responses of T cells to gluten were low in general: the median SI (range) was 2.0 (1-8.6) in patients with newly diagnosed IDDM and 1.5 (1-5.8) in control subjects (P = 0.03). Cellular responsiveness to gluten was not associated with HLA-DQB1 risk alleles for IDDM in patients. Although T cell responses to gluten were slightly increased in newly diagnosed patients the responsiveness was rare, and thus our results do not support a major role of gluten in the pathogenesis of human IDDM.

Adolescent↗
PubMed2007

A prospective, double-blind, placebo-controlled trial to establish a safe gluten threshold for patients with celiac disease.

BACKGROUND: Treatment of celiac disease (CD) is based on the avoidance of gluten-containing food. However, it is not known whether trace amounts of gluten are harmful to treated patients. OBJECTIVE: The objective was to establish the safety threshold of prolonged exposure to trace amounts of gluten (ie, contaminating gluten). DESIGN: This was a multicenter, double-blind, placebo-controlled, randomized trial in 49 adults with biopsy-proven CD who were being treated with a gluten-free diet (GFD) for > or =2 y. The background daily gluten intake was maintained at < 5 mg. After a baseline evaluation (t0), patients were assigned to ingest daily for 90 d a capsule containing 0, 10, or 50 mg gluten. Clinical, serologic, and histologic evaluations of the small intestine were performed at t0 and after the gluten microchallenge (t1). RESULTS: At t0, the median villous height/crypt depth (Vh/Cd) in the small-intestinal mucosa was significantly lower and the intraepithelial lymphocyte (IEL) count (x 100 enterocytes) significantly higher in the CD patients (Vh/Cd: 2.20; 95% CI: 2.11, 2.89; IEL: 27; 95% CI: 23, 34) than in 20 non-CD control subjects (Vh/Cd: 2.87; 95% CI: 2.50, 3.09; IEL: 22; 95% CI: 18, 24). One patient (challenged with 10 mg gluten) developed a clinical relapse. At t(1), the percentage change in Vh/Cd was 9% (95% CI: 3%, 15%) in the placebo group (n = 13), -1% (-18%, 68%) in the 10-mg group (n = 13), and -20% (-22%, -13%) in the 50-mg group (n = 13). No significant differences in the IEL count were found between the 3 groups. CONCLUSIONS: The ingestion of contaminating gluten should be kept lower than 50 mg/d in the treatment of CD.

Adult↗
PubMed1991

The effect of an elemental diet with and without gluten on disease activity in dermatitis herpetiformis.

Elemental diets are reported to decrease activity of patients with dermatitis herpetiformis. We tested the hypothesis that gluten, given in addition to an elemental diet, is responsible for the intestinal abnormalities, cutaneous immunoreactant deposition, and skin disease activity in dermatitis herpetiformis. At entry eight patients with dermatitis herpetiformis, who were consuming unrestricted diets, were stabilized on their suppressive medications at dosage levels that allowed individual lesions to erupt. Six patients were then given an elemental diet plus 30 of gluten for 2 weeks, followed by the elemental diet alone for 2 weeks. Conversely, two patients received an elemental diet alone for 2 weeks followed by an elemental diet plus gluten during the final 2 weeks. Small bowel biopsies, skin biopsies, and clinical assessments were done at 0, 2, and 4 weeks. Suppressive medication dose requirement decreased over the 4 weeks by a mean of 66%. Six of eight subjects significantly improved clinically during the gluten-challenge phase of the elemental diet and all were improved at the end of the study. The amount of IgA in perilesional skin did not change significantly, but the amount of C3 increased in five of seven evaluable subjects after gluten challenge. Circulating anti-gluten and anti-endomysial antibodies were not significantly affected by the diets. All subjects completing evaluable small bowel biopsies (seven of seven) demonstrated worsening of their villus architecture (by scanning electron microscopy and intraepithelial lymphocyte counts) during gluten challenge and improvement (six of six subjects) after 2 weeks of elemental dietary intake. We conclude that 1) there is a significant improvement in clinical disease activity on an elemental diet, independent of gluten administration, 2) small bowel morphology improves rapidly on an elemental diet, and 3) complement deposition but neither IgA deposition nor circulating antibody levels correlate with gluten intake. It seems likely that dietary factors other than gluten are important in the pathogenesis of the skin lesions in dermatitis herpetiformis.

Adult↗
PubMed2001

Linear IgA bullous dermatosis responsive to a gluten-free diet.

Dermatitis herpetiformis is associated with a gluten-sensitive enteropathy in >85% of cases. Both the skin lesions and the enteropathy respond to gluten restriction. Linear IgA bullous dermatosis has a much lower prevalence of histological small bowel abnormalities, and lesions are not known to respond to gluten restriction. We report a patient with linear IgA bullous dermatosis and gluten-sensitive enteropathy. This report addresses the issue of whether linear IgA bullous dermatosis can be associated with gluten-sensitive enteropathy. We evaluated the response to gluten restriction and normal diet by following the status of the patient's jejunal biopsies and skin lesions. The patient responded to gluten restriction, as shown by resolution of jejunal abnormalities and skin lesions and subsequently by recurrence of jejunal abnormalities and skin lesions with reinstitution of a gluten-containing diet. This report demonstrates that linear IgA bullous dermatosis can respond to gluten restriction if an underlying gluten-sensitive enteropathy is present.

Adult↗
PubMed2000

Behavioral and pharmacological studies on gluten exorphin A5, a newly isolated bioactive food protein fragment, in mice.

Central effects of gluten exorphin A5 (Gly-Tyr-Tyr-Pro-Thr), a fragment from wheat gluten, were studied on the pain-inhibitory system, emotionality and learning/memory processes in mice. Orally administered gluten exorphin A5 produced neither an antinociceptive effect nor an effect on morphine analgesia. Intracerebroventricularly (i.c.v.) administered gluten exorphin A5 produced mild but significant antinociception in a dose-depepndent manner, while not affecting the morphine analgesia. On the other hand, oral gluten exorphin A5 suppressed the endogenous pain-inhibitory system, i.e., antinociception induced by socio-psychological- (PSY-) stress (SIA) using a communication box; intraperitoneal gluten exorphin A5 abolished both footshock- (FS-) stress-induced antinociception (SIA) and PSY-SIA; and i.c.v. gluten exorphin A5 suppressed FS-SIA, but rather potentiated PSY-SIA. This peptide given by these routes was without effect on forced swim-SIA. In addition, oral gluten exorphin A5 tended to prolong the retention time on open arms in the elevated plus-maze test. Finally, oral gluten exorphin A5 when given during the post-training period of learning/memory processes significantly increased the latency into the dark compartment in the one-trail step-though type passive avoidance test, indicating that the peptide also facilitates the acquire/consolidation process of learning/memory. Thus, gluten exorphin A5 has been found to produce various effects not only in the peripheral nervous systems but also in the central nervous system.

Analgesics, Opioid↗
PubMed2004

Wheat gluten causes dendritic cell maturation and chemokine secretion.

Wheat gluten causes gut inflammation in genetically predisposed individuals. We tested the hypothesis that wheat gluten is not only a target of adaptive immunity, but also modulates the function of APC. Dendritic cells (DC) derived from the bone marrow of BALB/c mice were exposed to chymotrypsin-treated wheat gluten. This induced DC maturation as estimated by all surface markers tested (MHC class II, CD40, CD54, and CD86). The effect was dose dependent, and, at 100 microg/ml gluten matched that caused by 10 ng/ml LPS. A role of endotoxin contamination was ruled out by demonstrating the resistance of wheat gluten effects to LPS antagonist polymyxin B. DC from LPS nonresponder strain C3H/HeJ were affected by wheat gluten, but not by LPS. Proteinase K-digested wheat gluten was unable to stimulate DC maturation. Wheat gluten induced a unique secretion pattern of selected cytokines and chemokines in DC. Classic pro- or anti-inflammatory mediators were not produced, in contrast to LPS. Rather, chemokines MIP-2 and keratinocyte-derived cytokine were secreted in large amounts. We conclude that wheat gluten lowers the threshold for immune responses by causing maturation of APC, by attracting leukocytes and increasing their reactivity state. In the presence of an appropriate genetic predisposition, this is expected to increase the risk of adverse immune reactions to wheat gluten or to other Ags presented.

Animals↗
PubMed1989

Humoral and cellular immune response in growing rats fed a 10% gluten diet.

The effect of protein malnutrition, induced by a diet containing 10% plant wheat gluten, on the immune response system was studied in growing rats. The rats were fed wheat gluten or casein (control) diets, and were the offspring of mothers fed a commercial stock rat diet, a gluten diet, or a casein diet during pregnancy and lactation. Rats fed dietary wheat gluten showed a depressed humoral immune response to antigenic stimulation with sheep red blood cells, regardless of the mother's diet. Both IgG and IgM antibody titers were depressed by the gluten diet, but the effect on IgG was more pronounced. Total hemolysin titers of gluten-fed rats were 41% that of the casein-fed rats. Hemolysin antibodies resistant to 2-mercaptoethanol appeared in the gluten-fed rats 5 days later than in the control rats, and their titers were 38% that of the controls. The number of spleen plaque-forming cells in the experimental rats at the peak of response was lower and delayed by 1 day. An impairment in the cellular immune response, measured by in vitro stimulation of lymphocytes with concanavalin A, was found in the gluten-fed rats. The amount of [3H]methylthymidine incorporated into newly synthesized DNA of lymphocytes taken from lymph nodes of rats fed gluten was 11% that of the control rats. These findings may suggest that a gluten diet, which induces protein malnutrition, affects thymus-dependent immune responses.

Animals↗
PubMed1983

Isolation and physiochemical properties of an adenosine-rich gluten fraction.

Gluten proteins were isolated from the 0.01 mol acetic acid extract of bread. It was observed that precipitation of gluten provoked by 200 mM NaCl could partly be inhibited by adenosine. Based on this finding a method for isolation of the gluten fraction resisting saline precipitation in the presence of adenosine was elaborated. This fraction termed by us gluten-A-S, was found to have a lower glutamine + glutaminic acid and a higher proline and phenylalanine content than gluten. By sodium dodecylsulphate polyacrylamide gel electrophoresis gluten-A-S was shown to contain components of 58 000 and 34 000 dalton molecular weight after mercaptoethanol treatment while without the latter it contained a component of 74 000 dalton. The absorption maximum of the compound is at 260 mm; E280nm/E260nm = 0.5. In accordance with previous findings, gluten-A-S was found to contain 50-100 nmol adenosine per mg protein in a strong binding. It seems that in addition to the small amount of tightly bound adenosine, gluten-A-S contains a larger quantity of adenosine loosely bound to the protein. The physiological effects of dissociable adenosine bound to gluten and its possible role in the pathomechanism of gluten sensitive enteropathy is discussed in detail.

Adenosine↗
PubMed2002

Sorbitol H2-breath test versus anti-endomysium antibodies to assess histological recovery after gluten-free diet in coeliac disease.

BACKGROUND: Gluten-free diet plays a key role in treatment of coeliac disease, but it is difficult to evaluate its effect on improvement of villous architecture using sensitive non-invasive tests. AIMS: To compare sorbitol H2-Breath Test with antiendomysial antibodies in the follow-up of coeliac disease to detect histological recovery METHODS: A total of 38 consecutive patients with coeliac disease were studied. All underwent Sorbitol H2-Breath Test, antiendomysial and oesophagogastroduodenoscopy with multiple bioptic samples before diet and then 6, 12 and 18 months after gluten-free diet. Expiratory samples were collected before patients drank the test solution (5 g sorbitol in 150 ml tap water) and thereafter every 30 min for 4 hours. An increase in H2 concentration of > or = 20 ppm above fasting baseline was considered positive for sorbitol malabsorption. Antiendomysial antibodies were evaluated by the indirect immunofluorescent method. RESULTS: Antiendomysial antibodies were positive in 32/38 patients before gluten-free diet (84.21%), while they were positive in 20/34 (54.82%), 2/16 (12.5%) and 0/2 (0%) cases after 6, 12 and 18 months of gluten-free diet, respectively, no correlation being found with improvement of histological lesions (p = ns). As far as concerns sorbitol H2-Breath Test, maximal cut-off value (in ppm) decreased progressively and parallel to histological recovery during follow-up. Indeed, it decreased from a mean 63 ppm before diet to 35, 19 and 12 ppm, after 6, 12 and 18 months of gluten-free diet, with a stetistical difference being found before and after (p < 0.001). Likewise, the peak value (in minutes) appeared progressively later during follow-up, parallel to histological recovery. In fact, it appeared at a mean of 119 minutes before gluten-free diet, while it appears at a mean of 164, 195 and 219 minutes after 6, 12 and 18 months on gluten-free diet. A statistical difference before and after start of gluten-free diet was found also in this case (p < 0.001). CONCLUSIONS: Sorbitol H2-Breath Test is better than antiendomysial antibodies in revealing histological recovery in the follow-up of coeliac patients after the start of gluten-free diet due to its good correlation with histological damage. Moreover, it also appears to be able to detect dietary mistakes of the patients on gluten-free diet.

Adolescent↗
PubMed2000

Degradation behavior of soy protein-wheat gluten films in simulated soil conditions.

Films containing soy protein and wheat gluten were exposed to simulated farmland soil mix over a period of 30 days and monitored for degradation. The simulated farmland soil mix (topsoil/sand/Sunshine compost/vermiculite, 59:6:25:10, wt %) was mixed and stored at ambient humidity (48-55%) and temperature (20-24 degrees C); the soil mix was constantly maintained at 15% moisture by weight. Research focused on evaluating the effectiveness of gluten and cysteine additions on biodegradable behavior in the simulated farmland soil conditions. The four types of films, soy protein (S:G 1:0); soy protein with cysteine addition (S:G 1:0 + CYS); soy protein-wheat gluten (S:G 4:1); and soy protein-wheat gluten with cysteine addition (S:G 4:1 + CYS), were prepared at pH 7. 0 for degradation studies. Soy protein-gluten film rapidly degraded with 50% weight loss in about 10 days and with up to 95% weight loss in 30 days. Tensile strength and elongation of all soy protein-gluten films significantly decreased in 3 days. However, cysteine addition delayed the degradation rate of soy protein-gluten films. Soy protein-wheat gluten film disintegrated after 20 days in the simulated farmland soil environment. These results suggest that wheat gluten and cysteine addition to soy protein-based films could delay degradation rates due to their high disulfide contents.

Glutens↗
PubMed1999

Wheat starch-containing gluten-free flour products in the treatment of coeliac disease and dermatitis herpetiformis. A long-term follow-up study.

BACKGROUND: We investigated whether wheat starch-based gluten-free products are safe in the treatment of gluten intolerance. METHODS: The study involved 41 children and adults with coeliac disease and 11 adults with dermatitis herpetiformis adhering to a gluten-free diet for 8 years on average. Thirty-five newly diagnosed coeliac patients at diagnosis and 6 to 24 months after the start of a gluten-free diet and 27 non-coeliac patients with dyspepsia were investigated for comparison. Daily dietary gluten and wheat starch intake were calculated. Small-bowel mucosal villous architecture, CD3+, alphabeta+, and gammadelta+ intraepithelial lymphocytes, mucosal HLA-DR expression, and serum endomysial, reticulin, and gliadin antibodies were investigated. RESULTS: Forty of 52 long-term-treated patients adhered to a strict wheat starch-based diet and 6 to a strict naturally gluten-free diet; 6 patients had dietary lapses. In the 46 patients on a strict diet the villous architecture, enterocyte height, and density of alphabeta+ intraepithelial lymphocytes were similar to those in non-coeliac subjects and better than in short-term-treated coeliac patients. The density of gammadelta(+)cells was higher, but they seemed to decrease over time with the gluten-free diet. Wheat starch-based gluten-free flour products did not cause aberrant upregulation of mucosal HLA-DR. The mucosal integrity was not dependent on the daily intake of wheat starch in all patients on a strict diet, whereas two of the six patients with dietary lapses had villous atrophy and positive serology. CONCLUSION: Wheat starch-based gluten-free flour products were not harmful in the treatment of coeliac disease and dermatitis herpetiformis.

Adolescent↗
PubMed2002

Even small amounts of gluten cause relapse in children with celiac disease.

BACKGROUND: Previously, a gluten challenge was customary to establish the diagnosis of celiac disease in children. There are no clear recommendations on how to perform this challenge or what markers to rely on for timing the biopsy after the challenge. The authors' aim was to monitor gluten intake, clinical symptoms, and antibody kinetics to evaluate the influence of gluten exposure during the challenge. METHODS: Twenty-five children under investigation for suspected celiac disease were challenged. One child was excluded because blood samples, food records, or biopsy was lacking. Median age at the postchallenge biopsy was 3.8 (2.7-8.8) years. The families kept daily records of the children's gluten intake and of symptoms that occurred. Blood samples were taken monthly for analysis of antigliadin and endomysium antibodies and total immunoglobulin A (IgA). A third biopsy was performed when clinical symptoms suggested a relapse. RESULTS: All 24 children showed deterioration of the mucosa or elevated antibodies during gluten challenge. Median duration of the challenge was 13 (5-51) weeks, and mean gluten intake was 1.7 (0.2-4.3) g/d and 0.1 (0.02-0.26) g/kg daily. CONCLUSIONS: Gluten intake during the challenge varied widely, and the parents were unable to give their children the recommended amount. Despite the small amounts given, all children showed signs of relapse at a clinical, laboratory, or histologic level. Much smaller amounts of gluten than previously suggested seem sufficient to cause relapse during gluten challenge in children.

Biopsy↗