This review is intended to focus on the composition of oat and its therapeutic potential in the pharmacology that supports its use to cure various maladies. Oat (Avena sativa) is distinct among the cereals due to its multifunctional characteristics and nutritional profile. Recent advancement in food and nutrition has revealed the importance of its various components. It is a good source of dietary fiber especially β-glucan, minerals and other nutrients. Oat and oat by products have been proven to be helpful in the treatment of diabetes and cardiovascular disorders. Oat bran in particular, is good source of B complex vitamins, protein, fat, minerals besides heart healthy soluble fiber β-glucan. The β-glucan has outstanding functional properties and is of immense importance in human nutrition. Different physiological effects of β-glucan are related to its viscosity, attenuation of postprandial plasma glucose and insulin responses, high transport of bile acids towards lower parts of the intestinal tract and high excretion of bile acids thereby lowering of serum cholesterol levels. Moreover, it is helpful against coeliac disease. The incorporation of oat grains and oat bran in the food products improves not only the nutrition but also a therapy against various maladies.

Oat: unique among the cereals

As shown by R5 antibody-based sandwich and competitive enzyme-linked immunosorbent assay (ELISA), selected sourdough lactobacilli, in combination with fungal proteases, hydrolyzed gluten (72 h at 37°C) of various cultivars of Triticum turgidum L. var. durum to less than 20 ppm. Complementary electrophoretic, chromatography, and mass spectrometry techniques were used to characterize the gluten and epitope hydrolysis. Nine peptidases were partially purified from the pooled cytoplasmic extract of the sourdough lactobacilli and used to hydrolyze the 33-mer epitope, the most immunogenic peptide generated during digestion of Triticum species. At least three peptidases (general aminopeptidase type N [PepN], X-prolyl dipeptidyl aminopeptidase [PepX], and endopeptidase PepO) were necessary to detoxify the 33-mer without generation of related immunogenic epitopes. After 14 h of incubation, the combination of all or at least six different peptidases totally hydrolyzed the 33-mer (200 mM) into free amino acids. The same results were found for other immunogenic epitopes, such as fragments 57-68 of α9-gliadin, 62-75 of A-gliadin, and 134-153 of γ-gliadin. When peptidases were used for fermentation of durum wheat semolina, they caused the hydrolysis of gluten to ca. 2 ppm. The in vivo digestion was simulated, and proteins/peptides extracted from pepsin-trypsin (PT) digestion of durum wheat semolina fermented with selected sourdough lactobacilli induced the expression of gamma interferon and interleukin 2 at levels comparable to those of the negative control. Durum wheat semolina fermented with sourdough lactobacilli was freeze-dried and used for making Italian-type pasta. The scores for cooking and sensory properties for this pasta were higher that those of conventional gluten-free pasta.

https://aem.asm.org/content/aem/76/2/508.full.pdf

Mechanism of degradation of immunogenic gluten epitopes from Triticum turgidum L. var. durum by sourdough lactobacilli and fungal proteases.

Real-time PCR methods, using melting curve analysis for product identification, were established for the specific discrimination of wheat, rye, barley and oats in food samples. Specific primers targeting cereal prolamin genes were chosen for the amplification. The lengths of the amplicons varied between 104 and 181 base pairs and the melting point between 81.2 and 85.0 °C. The specificity of the wheat PCR was shown for spring and autumn wheat but also for durum wheat, spelt wheat and kamut. The methods were applied for final food products and for detection of toxic cereal contamination in oat samples. The results of the analysis were compared with those obtained with an established enzyme immuno assay for gluten analysis. The PCR methods give a good correlation with the protein assay and are rapid and sensitive. The PCR methods can thus be used as confirmatory methods in food analysis of gluten-free and naturally gluten-free foods.

Real Time PCR for the detection and discrimination of cereal contamination in gluten free foods

Celiac disease (CD) is an inflammatory small intestinal disorder that can lead to severe villous atrophy, malabsorption, and malignancy. It is triggered by the gluten proteins of wheat, barley, and rye. All patients express the antigen-presenting molecules human leukocyte antigen-DQ2 (HLA-DQ2) and/or HLA-DQ8, which bind gluten peptides and thus activate destructive intestinal T cells. Patients with untreated CD have circulating IgA autoantibodies to the enzyme tissue transglutaminase (tTG), a component of endomysium. Testing for serum IgA tTG has a high predictive value. Therapy of CD is a lifelong gluten-free diet. Counseling by an expert dietitian and association with a celiac support group are important in helping the patient embark on a healthy gluten-free diet. Current research focuses on non-dietary therapies and treatment of refractory (diet-unresponsive) CD.

/pdf/celiac-disease-epidemiology-pathogenesis-diagnosis-and-1tmrygdu79.pdf

Celiac disease: epidemiology, pathogenesis, diagnosis, and nutritional management.

Purpose of reviewIncreasing numbers of atypical or asymptomatic cases of celiac disease are being diagnosed. This review aims to summarize recent critical research in celiac disease.Recent findingsAlternative candidate genes outside of the human leukocyte antigen complex continue to be identified, w

Advances in celiac disease

Background: It is well established that the wheat protein gliadin triggers inflammation in coeliac patients. However, the potential toxicity of avenin, the equivalent protein in oats, is debated.

Aim: To investigate the immunogenicity of avenin using the cytokines interferon γ (IFN-γ) and interleukin (IL)-2 as markers of immunological activity.

Methods: Duodenal biopsies from coeliac patients were cultured with 5 mg/ml of peptic tryptic (PT) gliadin (n=9) or 5 mg/ml of PT avenin (n=8) for four hours. Biopsies cultured with RPMI 1640 alone served as controls. Non-coeliac biopsies were also cultured with PT gliadin (n=8) and PT avenin (n=8). Total RNA was extracted from the tissue after culture. Cytokine mRNA was quantified by TaqMan polymerase chain reaction. Secreted cytokine protein was measured in the culture supernatant by enzyme linked immunosorbent assay.

Results: After culture with PT gliadin, an increase in IFN-γ mRNA was observed in all nine patients with coeliac disease. Increased IFN-γ protein was also found in four of these patients. Smaller increases in IL-2 mRNA were detected in six subjects with increased IL-2 protein found in two patients. In contrast with PT gliadin, there was no significant IFN-γ or IL-2 response when coeliac biopsies were cultured with PT avenin. Similarly, biopsies from normal controls did not respond to PT gliadin or PT avenin stimulation.

Conclusions: The findings of this study suggest that the immunogenic sequences in gliadin are not present in avenin. Moreover, they are in keeping with in vivo studies which report that oats are safe for consumption by coeliac patients.

https://gut.bmj.com/content/gutjnl/52/1/47.full.pdf

Avenin fails to induce a Th1 response in coeliac tissue following in vitro culture

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Avenin fails to induce a Th1 response in coeliac tissue following in vitro culture