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Sindrome dell’intestino irritabile: c’è un ruolo per il glutine?

by luciano

Uno studio molto importante che evidenzia la sovrapposizione dei sintomi della sindrome dell’intestino irritabile con quelli generati dalla sensibilità al glutine non celiaca dalle ATI e da Fodmaps.

“A tight link exists between dietary factors and irritable bowel syndrome (IBS), one of the most common functional syndromes, characterized by abdominal pain/discomfort, bloating and alternating bowel habits. Amongst the variety of foods potentially evoking “food sensitivity”, gluten and other wheat proteins including amylase trypsin inhibitors represent the culprits that recently have drawn the attention of the scientific community. Therefore, a newly emerging condition termed non-celiac gluten sensitivity (NCGS) or nonceliac wheat sensitivity (NCWS) is now well established in the clinical practice. Notably, patients with NCGS/NCWS have symptoms that mimic those present in IBS. The mechanisms by which gluten or other wheat proteins trigger symptoms are poorly understood and the lack of specific biomarkers hampers diagnosis of this condition. The present review aimed at providing an update to physicians and scientists regarding the following main topics: the experimental and clinical evidence on the role of gluten/wheat in IBS; how to diagnose patients with functional symptoms attributable to gluten/wheat sensitivity; the importance of double-blind placebo controlled cross-over trials as confirmatory assays of gluten/wheat sensitivity; and finally, dietary measures for gluten/wheat sensitive patients. The analysis of current evidence proposes that gluten/wheat sensitivity can indeed represent a subset of the broad spectrum of patients with a clinical presentation of IBS. (J Neurogastroenterol Motil 2016;22:547-557). Umberto Volta, Maria Ines Pinto-Sanchez et al.

Extrac from the study:
…..omissis. Experimental Evidence for a Role of Wheat Components in Irritable Bowel Syndrome. Different mechanisms have been proposed to explain how gluten may trigger gastrointestinal symptoms in the absence of celiac disease (Figure).

In vitro studies have demonstrated that digests of gliadin increase the expression of co-stimulatory molecules and the production of proinflammatory cytokines in monocytes and dendritic cells (40,57,58). Certain “toxic” (that only stimulates the innate immune response) gliadin-derived peptides such as the 31-43mer, may evoke epithelial cell dysfunction, increased IL-15 production and enterocyte apoptosis (59). Recent studies have demonstrated increased expression of TLR-2 in the intestinal mucosa of non-celiac compared to celiac patients, suggesting a role of the innate immune system in the pathogenesis of non-celiac reactions to gluten or other wheat components (49). Other studies have shown that monocytes from HLA-DQ2+ non-celiac individuals spontaneously release 2-3 fold more IL-8 than monocytes from HLA-DQ2 negative patients. This suggests that patients without celiac disease (no enteropathy and negative specific serology), but with positive HLA-DQ2 status, may represent a subpopulation reacting mildly to gluten (60). In terms of gut dysfunction, gluten sensitization in mice has been shown to induce acetylcholine release, one of the main excitatory neurotransmitters in the gut, from the myenteric plexus (57).
This correlates with increased smooth muscle contractility and a hypersecretory status with increased ion transport and water movements (57). These functional effects induced by gluten were not accompanied by mucosal atrophy, and were not observed after sensitization with non-gluten proteins. Interestingly gluten-induced gut dysfunction was particularly notable in mice transgenic for the human celiac gene HLA-DQ8 (57).
ATIs, a group of wheat proteins that confer resistance of the grain to pests, are strong inducers of innate immune responses via TLR4 and via the myeloid differentiation factor 88-dependent and -independent pathway (40). This activation occurs both in vitro and in vivo after oral ingestion of purified ATIs or gluten, while gluten-free cereals display no or minimal activities (61). The role of ATIs in IBS is not yet known, however there is clear description of a mechanism that could be involved in the generation of gut dysfunction and symptoms. These mechanisms are different from those proposed for gluten and thus it is conceivable that they could co-exist in given patients or have a synergistic effect.

Glutine: aminoacidi, digestione, peptidi tossici e immunogenici

by luciano

Gliadina e Glutenina
Sono le proteine del grano (la gliadina, solubile in alcol e la glutenina, insolubile in alcol.) e sono composte da catene di aminoacidi (1). La gliadina è costituita dall’unione di circa 100-200 amminoacidi (principale responsabile della celiachia), e la glutenina, costituita dalla combinazione di circa 2.000-20.000 amminoacidi. Il legame covalente che unisce due amminoacidi prende anche il nome in biochimica di “legame peptidico”. Una catena di più amminoacidi legati attraverso legami peptidici prende il nome generico di peptide o polipeptide o di oligopeptide se il numero di amminoacidi coinvolti è limitato; uno o più polipeptidi, a volte accompagnati da altre strutture ausiliarie o ioni dette cofattori o gruppi prostetici, costituiscono una proteina. Gli aminoacidi (o amminoacidi) sono l’unità strutturale primaria delle proteine. Possiamo quindi immaginare gli aminoacidi come mattoncini che, uniti da un collante chiamato legame peptidico, formano una lunga sequenza che dà origine ad una proteina.
Le proteine dei cereali solubili in alcol sono denominate: prolammine.
La prolamina del grano è la gliadina, dell’orzo l’ordeina, della segale la secalina, dell’avena l’avenina. I diversi tipi di prolamine contengono diversi aminoacidi e quanto più alto è il contenuto di prolina e glutamina (che sono alcuni degli aminoacidi che la compongo) tanto più quella prolamina, e quindi i peptidi di quel cereale saranno tossici (2) per il paziente affetto da malattia celiachia. I livelli più elevati di prolina e glutamina sono nel grano, orzo e segale. Anche le glutenine hanno alcune sequenze tossiche per i celiaci ma risultano essere molto meno attive nel sollecitare la risposta avversa del sistema umanitario dell’uomo.

Importanza delle subunità HMM del glutine (aggiornamento 21-01-2020)

by luciano

Estratto dallo studio: The structure and properties of gluten

“….omissis. Un gruppo di proteine ​​del glutine, le subunità HMM della glutenina, è particolarmente importante nel conferire alti livelli di elasticità (ovvero la resistenza della pasta). Queste proteine ​​sono presenti nei polimeri HMM che sono stabilizzati dai legami disolfuro e sono formano “l’ossatura elastica” del glutine. Tuttavia, le sequenze ripetitive ricche di glutammina che comprendono le parti centrali delle subunità HMM formano anche estese matrici di legami idrogeno tra di loro legati che possono contribuire alle proprietà elastiche attraverso un meccanismo “loop and train*”. L’ingegneria genetica può essere utilizzata per manipolare la quantità e la composizione delle subunità HMM, portando a un aumento della forza dell’impasto o a cambiamenti più drastici nella struttura e nelle proprietà del glutine.

….omissis … Queste proprietà sono generalmente descritte come viscoelasticità, con l’equilibrio tra estensibilità ed elasticità che determina la qualità dell’uso finale. Ad esempio, per la panificazione sono necessari impasti altamente elastici (“forti”) ma impasti più estensibili per preparare torte e biscotti. Omissis … Le proteine ​​del grano determinano le proprietà viscoelastiche dell’impasto, in particolare le proteine ​​di conservazione che formano una rete nell’impasto chiamata glutine (Schofield 1994). Di conseguenza, le proteine ​​del glutine sono state ampiamente studiate per un periodo superiore a 250 anni, al fine di determinare le loro strutture e proprietà e fornire una base per manipolare e migliorare la qualità dell’uso finale.”

*

…omissis. As a result of the formation of a protein matrix, individual cells of wheat flour contain networks of gluten proteins, which are brought together during dough mix ing. The precise changes that occur in the dough during mixing are still not completely understood, but an increase in dough stiffness occurs that is generally considered to result from ‘optimization’ of protein–protein interactions within the gluten network. In molecular terms, this ‘optimization’ may include some exchange of disulphide bonds as mixing in air, oxygen and nitrogen result in different effects on the sulphydryl and disulphide contents of dough (Tsen & Bushuk 1963; Mecham & Knapp 1966).

Glutine ed intestino

by luciano

Digestione di peptidi del glutine nell’intestino crasso e benefici che apporta.

È stato dimostrato che l’eliminazione del glutine dalla dieta influisce sulla composizione della comunità batterica nell’intestino crasso dove il cibo non digerito nell’intestino tenue e potrebbe essere idrolizzato dal metabolismo microbico, generando composti benefici per l’ospite.

“Alimentary protein digestion followed by amino acid and peptide absorption in the small intestinal epithelium is considered an efficient process. Nevertheless, unabsorbed dietary proteins enter the human large intestine as a complex mixture of protein and peptides.53,63 The incomplete assimilation of some dietary proteins in the small intestine has been previously demonstrated, even with proteins that are known to be easily digested (e.g., egg protein).64,65 The high proline content of wheat gluten and related proteins renders these proteins resistant to complete digestion in the small intestine. As a result, many high molecular weight gluten oligopeptides arrive in the lower gastrointestinal tract.66 While gluten peptides pass through the large intestine, proteolytic bacteria could participate in the hydrolysis of these peptides. A recent study from our group has shown that some of the gluten ingested in the diet is not completely digested while passing through the gastrointestinal tract, and is consequently eliminated in feces.

Moreover, it has been shown that the amount of gluten peptides present in feces is proportional to the amount of gluten consumed in the diet. Therefore, several gluten peptides are resistant to both human and bacterial proteases in the gastrointestinal tract.66,67

The large intestine is the natural habitat for a large and dynamic bacterial community. Although the small intestine contains a significant density of living bacteria, the density in the large intestine is much higher. The large intestine has as many as 1011–1012 cells per gram of luminal content that belong to thousands of bacterial taxa. Furthermore, the large intestinal microbiota is extremely complex and performs specific tasks that are beneficial to the host.68–71 Among the important functions that the intestinal microbiota performs for the host are several metabolic functions.72 In contrast to the rapid passage of dietetic components through the small intestine, the transit of the luminal material through the large intestine is considerably slower. The longer transit time in the large intestine has been associated with important bacterial metabolic activity.53 Therefore, undigested food in the upper gut could be hydrolyzed by microbial metabolism in the large intestine, generating beneficial compounds for the host.

The resistance of gluten peptides to pancreatic and brush border enzymes allows large amounts of high molecular weight peptides to enter the lower gastrointestinal tract. Therefore, gluten peptides are available for microbial metabolism in the large intestine and could be important to the composition of the intestinal microbiota. It has been shown that removing gluten from the diet affects the composition of the bacterial community in the large bowel.78,79 De Palma et al.78 observed that healthy subjects who followed a gluten-free diet for 1 month had reduced fecal populations of Lactobacillus and Bifidobacterium, but the population of Enterobacteriae such as E. coli appeared to increase. Similar results were obtained in studies with CD patients. Treated CD patients also showed a reduction in the diversity of Lactobacillus and Bifidobacterium species.80,81Gluten Metabolism in Humans. Alberto Caminero, … Javier Casqueiro, in Wheat and Rice in Disease Prevention and Health, 2014”