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At least 703 records · Page 39Linked to original sources
PubMed1985

Changes in food consumption and its nutritional quality when on a gluten-free diet for dermatitis herpetiformis.

Dietary intakes of energy and nutrients were calculated from diet history interviews in 30 patients with dermatitis herpetiformis, before and after 18 months on a gluten-free diet. In spite of great changes in the intake of different foods, the mean intake of dietary fibre did not decrease. There was only a small decrease in the intake of iron in women, while the intake in men did not change. Patients with a previous high intake of gluten had indirect evidence of malabsorption.

Adult↗
PubMed1987

Organ culture of fetal rat small intestine for testing gluten toxicity: a reappraisal.

Jejunal segments from fetal rats of 18 days gestation were maintained in an organ culture system for up to 72 h. During this period, villi developed within the intestinal lumen and the epithelium changed from stratified to simple columnar. Peristaltic activity was observed during in-vitro culture. Alkaline phosphatase specific activity of the bowel segments fell after 48 hours culture, compared with pre-culture values (P less than 0.05), but that of alpha-glucosidase increased. The addition of Frazer's gluten fraction III to the culture medium caused slowing in the rate of morphological maturation of the jejunal explants, but there was no additional effect on enzyme specific activities compared with segments cultured in gluten-free medium. The place of organ culture of fetal rat intestine as an animal model for testing cereal toxicity in the study of coeliac disease remains unclear.

Animals↗
PubMed1974

Cellular infiltrate of jejunal biopsies in adult coeliac disease in relation to gluten withdrawal.

A comparison has been made of inflammatory cell counts in the lamina propria and epithelium of jejunal biopsies in 11 patients with adult coeliac disease with those found in 12 control subjects. In the coeliac patients, there were significant increases in the numbers of total cells, plasma cells, and intraepithelial lymphocytes, but a significant reduction in lamina propria lymphocytes. Following clinical improvement on a strict gluten-free diet, significant changes in cell counts occurred, but with the exception of lymphocytes in the lamina propria, the counts were still abnormal. Analysis of five patients in whom the biopsy improved to near normal morphology and of six in whom there was no such improvement showed that significant falls in plasma cells and rises in lymphocytes in the lamina propria could occur without improvement in other morphological appearances. These results seem relevant to the problem of diagnosing coeliac disease in patients who, on gluten withdrawal, show an unequivocal clinical response, but no gross morphological improvement in the jejunal biopsy. On the basis of the observed changes in cell counts, there seems little justification in questioning the diagnosis of coeliac disease in such patients.

Adult↗
PubMedDate not supplied

[Amino acid composition of triticale gluten].

The study of the amino acid composition of tritikale gluten has demonstrated that in comparison with that of grain protein it contains much less aspartic acid (by 28.1%) and lysine (by 19.4%), less alanine and arginine but more tyrosine (by 39.7%), glutamic acid (by 31.4%), phenylalanine (by 23.6%) and leucine (by 14.4%) and slightly more threonine and valine. The study has shown no significant differences in the amino acid composition of grain protein and tritikale gluten of different varieties and cultivation regions.

Amino Acids↗
PubMed1984

[Acquired hypogammaglobulinemia and malabsorption with villous atrophy sensitive to a gluten-free diet].

The observation of a 21 year-old man with primary common variable hypogammaglobulinemia and total villous atrophy is reported. Gluten withdrawal induced considerable improvement in malabsorption and mucosal damage. However, protein-losing enteropathy, nodular lymphoid hyperplasia and immunoglobulin deficiency were persistent. To our knowledge, improvement on gluten-free diet has been reported until now in 18 previous cases. This report illustrates the links between immunodeficiency and malabsorption, which are discussed.

Adult↗
PubMedDate not supplied

[Casein and gluten utilization by the body].

The time-course of changes in casein and gluten utilization was elucidated in rats in 2 experiments lasting 52 and 84 days by means of determining the protein effectiveness coefficient (PEC). The PEC was measured every other 4 days. Casein utilization decreased continuously and almost rectilinearly, whereas gluten utilization first rose (adaptation) and then descended (deadaptation). It is concluded that the time-course of changes in utilization of unbalanced wheat protein is linked not only with restitution of the enzymatic systems but also with mobilization and depletion of the reserve possibilities of the body.

Animals↗
PubMedDate not supplied

[Celiac disease (celiac sprue, gluten-sensitive enteropathy)].

In spite of the remarkable progress made in the last years, the perspectives in coeliac disease is still an enigma that has maintained this clinical entity a subject open to investigation. However, particular attention is deserved to the recent contributions related to the role of the histocompatibility antigens (HLA system), which is basically controlled by inherited transmission but can behave, in certain cases as gluten-sensitive "receptors" at the level of brush-border membrane. The coupling of these receptors with antigenic fractions of gluten in a sensitive person should be a starting point for a sequence of immunological events, with its several intestinal and general implications.

Adolescent↗
PubMed1982

Villus atrophy and crypt elongation in the small intestine of preruminant calves fed with heated soyabean flour or wheat gluten.

Serial biopsies were removed from the jejunal mucosa of preruminant calves given single or multiple feeds containing heated soyabean flour or wheat gluten. Morphometric investigation using a microdissection technique revealed partial villus atrophy and crypt elongation. The first exposure to soyabean protein caused slight shortening of villi but after a succession of experimental feeds of heated soyabean flour or gluten, animals developed marked mucosal abnormalities and severe diarrhoea. Villus atrophy and crypt elongation were seen 24 hours after challenge with an experimental feed and restoration of normal morphology on a diet of milk alone took about 10 days. The data are discussed in relation to coeliac disease of man and the use of soya products in milk replacers for calves.

Animals↗
PubMed1982

Gluten-free diet in chronic active hepatitis associated with intestinal villous atrophy.

Three patients out of 16 with chronic active hepatitis exhibited villous atrophy in biopsy specimens from the upper jejunum. These patients were put on a gluten-free diet for one year, and the intestinal changes normalized in two of the patients, but did not heal in the third patient. The levels of alanine aminotransferase and IgG, did not decrease under the gluten-free diet. The liver disease of the patients with intestinal changes ran a serious course: one patient died in hepatic coma, and one patient developed portal hypertension with recurring hematemesis. These complications did not appear in the patients with healthy intestine. It is suggested that the three patients suffered from both chronic active hepatitis and coeliac disease, which appeared concomitantly on the basis of a genetic disposition for both diseases.

Adolescent↗
PubMed1980

Gluten enteropathy occurring in chronic hepatitis.

Steatorrhoea and subtotal villus atrophy due to gluten enteropathy was found to occur in a 27 year old female, who had histologically proven chronic active hepatitis six years ago. She had abnormal elevation of immunoglobulins IgG, IgM, and IgA, decreased level of complement C4 and a positive test for HLA-B8. The SGOT was persistently mildly elevated, but her latest liver biopsy (6 years after onset) showed only changes of chronic persistent hepatitis. She had good symptomatic and histological (jejunal biopsy) improvement with gluten-free diet.

Adult↗
PubMed1981

The timing of histological damage following a single challenge with gluten in treated coeliac disease.

Two treated subjects and one healthy volunteer have been challenged with a single dose of fraction B of gluten administered intraduodenally. Serial biopsy specimens were obtained by means of a Quinton hydraulically operated biopsy instrument immediately before challenge and repeatedly thereafter. The biopsy specimens were studied by light microscopy, electron microscopy, immunofluorescence, immunoperoxidase staining and disaccharidase assay. The two coeliac subjects showed pronounced mucosal changes which developed a few hours after challenge and which showed the features of an Arthus-type reaction. The healthy volunteer was unaffected. It is concluded that the lesion of coeliac disease is the result of an Arthus-type reaction induced by ingested gluten in susceptible subjects.

Aged↗
PubMed1980

Scanning electron microscopy of small intestinal repair following treatment for gluten sensitive enteropathy.

Sequential small intestinal biopsies from patients with gluten sensitive enteropathy were studied by scanning electron microscopy before and after dietary treatment. Compared with patients without evidence of villus atrophy, there were marked architectural changes. Before treatment, villi were absent and crypts were prominent. After treatment, the intestinal repair could be divided into stages. The first stage consisted of circular ridges surrounding the crypts. Unequal cellular repletion around the crypts resulted in the formation of horseshoe shaped ridges. Elongation of the arms of the horseshoes led to the formation of cerebriform ridges. Mitten-like villi were formed in the last stage by the development of furrows and septation of the ridges. The scanning electron microscope is a useful adjunct to the light microscopic and dissecting microscopic assessment of small intestinal biopsies. It can detect changes not possible with either light microscopy or the dissecting microscope and may be a more sensitive technique for the morphological assessment of patient response to treatment for gluten sensitive enteropathy.

Biopsy↗
PubMed1994

Celiac disease and the spectrum of gluten sensitivity.

Celiac disease is a well-known entity in which intolerance to wheat gluten and related proteins from barley, rye, and oats (collectively known as prolamins) damage intestinal mucosa. New insights into the pathology of the celiac intestinal lesion point to a wider spectrum of gluten sensitivity than previously thought. Recent advances in immunology and genetics have shed light on the underlying mechanisms and risks associated with the disease. Although the classical manifestations are well known, the wide variety of clinical presentations make celiac disease often difficult to diagnose, and the ubiquitous presence of prolamins in the Western diet make treatment challenging.

Celiac Disease↗
PubMed1997

[Gluten as food additive in The Netherlands: cheese forbidden for celiac patients?].

A new coating for cheese, to be introduced in May, consists entirely of natural degradable components. The coating is based on wheat gluten. This increase in the amount of gluten in the Dutch diet may lead to overt coeliac disease in people with a subclinical form of it, and will limit the dietary choices of patients already suffering from the disease.

Celiac Disease↗
PubMed1985

Dermatitis herpetiformis in monozygous twins: discordance for dermatitis herpetiformis and concordance for gluten-sensitive enteropathy.

A monozygous female twin pair discordant for dermatitis herpetiformis and concordant for gluten-sensitive enteropathy is reported. The diagnosis of dermatitis herpetiformis was verified by demonstrating granular IgA deposits in the uninvolved skin. Gluten-sensitive enteropathy was confirmed according to the ESPGAN criteria. Monozygosity was proved by the standard genetic characteristics.

Celiac Disease↗
PubMed1981

[Tissue gluten with special considerations of fibrin glue (author's transl)].

Tissue glues can be divided into two groups: synthetic and biogenic. The use of the first is limited by poor tissue tolerance. Biogenic glue consists of fibrinogen, factor XIII, and thrombin, which form a fibrin clot in the presence of calcium. In our experiments we were able to prove an advantageous effect on hemostasis and healing. A new dried gluten developed on the basis of collagen represents a new type of biogenic gluten.

Animals↗
PubMed2006

Increased protein expression of matrix metalloproteinases -1, -3, and -9 and TIMP-1 in patients with gluten-sensitive enteropathy.

Gluten-sensitive enteropathy is characterized by small intestinal damage. The pathogenic mechanisms involved are not precisely understood. There is recent interest in the possibility that matrix metalloproteinases might play a pathogenic role. Using immunohistochemistry technique, we examined the protein expression of matrix metalloproteinases-1, -3, and -9 and the tissue inhibitor metalloproteinase-1 in duodenal biopsies from 30 patients with celiac disease and dermatitis herpetiformis. We demonstrated that the percentage of cells expressing these enzymes and their inhibitor in all patients was significantly greater than in the normal controls (P < 0.0001). This was evident even in patients with a minimal lesion but was most marked in patients with severe damage, mirroring the degree of inflammation in the small intestinal tissue. The increased expression of these enzymes and their inhibitor in the duodenal mucosa of patients with gluten-sensitive enteropathy suggests a role for these enzymes in the tissue remodeling which is a feature of these disorders.

Adult↗
PubMed1991

Modulation of protease specificity by a change in the enzyme microenvironment. Selectivity modification on a model substrate, purified soluble proteins and gluten.

Subtilisin BPN' activity on a synthetic substrate is found to decrease with the concentration of soluble additives such as sugars and polyols, the catalytic efficiency of the enzyme being related to the water activity in the reaction medium. Limited hydrolysis of B chain of insulin is followed and the cleavage priority determined. When carried out in glycerol-containing medium, both enzyme catalytic behaviour and specificity are perturbed; a different cleavage order and a selectivity restriction are observed. The experiments were generalised to purified proteins and to an insoluble protein complex. The hydrolysis kinetics of purified gliadins by pepsin and of gluten by a Bacillus neutral protease are modulated in presence of water activity depressors. Glycerol is able to increase both pepsin efficiency and gluten protein solubility. The hydrolysis order is affected by water-structuring molecules in the enzyme microenvironment and new peptides appear whatever the size and initial solubility of the substrate.

Amino Acid Sequence↗