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      Does a Gluten-free Diet Improve Metabolic Syndrome Parameters? A Systematic Review

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          Abstract

          Abstract To review scientific evidence on the effects of a gluten-free diet on body composition and improvement of clinical and biochemical parameters of metabolic syndrome. The Preferred Reporting Items for Systematic Reviews and Meta-Analyzes - PRISMA guidelines were followed. A literature search was performed in the PubMed, ScienceDirect, Trip Database, Bireme and Scielo databases, without language restriction, until March 2021. The terms “gluten-free diet”, “obesity”, “metabolic syndrome”, and “weight loss”, and Boolean operators (AND/OR) were used. The clinical hypothesis was structured according to the acronym PICOT. Randomized clinical trials with adult and elderly humans without a diagnosis of celiac disease, consuming a gluten-free diet, evaluating associations of the effects of this diet on weight loss and metabolic syndrome components were considered eligible. To assess the risk of bias, the RoB2 was used. A total of 3,198 articles were identified and, after the screening and evaluation of pre-defined eligibility criteria, four studies were included in the qualitative analysis. Weight loss was not associated with a gluten-free diet. However, individuals under a gluten-free diet had lower mean waist circumference, fat percentage (-2.3%) and serum triglyceride levels. The impact of a gluten-free diet on metabolic syndrome parameters is still controversial. In individuals without gluten sensitivity or celiac disease, the consumption of a gluten-free diet appears to provide no nutritional benefit.

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          Most cited references28

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          Executive Summary of the Third Report of the National Cholesterol Education Program (NCEP) Expert Panel on Detection, Evaluation, and Treatment of High Blood Cholesterol in Adults (Adult Treatment Panel III)

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            Chemistry of gluten proteins.

            Gluten proteins play a key role in determining the unique baking quality of wheat by conferring water absorption capacity, cohesivity, viscosity and elasticity on dough. Gluten proteins can be divided into two main fractions according to their solubility in aqueous alcohols: the soluble gliadins and the insoluble glutenins. Both fractions consist of numerous, partially closely related protein components characterized by high glutamine and proline contents. Gliadins are mainly monomeric proteins with molecular weights (MWs) around 28,000-55,000 and can be classified according to their different primary structures into the alpha/beta-, gamma- and omega-type. Disulphide bonds are either absent or present as intrachain crosslinks. The glutenin fraction comprises aggregated proteins linked by interchain disulphide bonds; they have a varying size ranging from about 500,000 to more than 10 million. After reduction of disulphide bonds, the resulting glutenin subunits show a solubility in aqueous alcohols similar to gliadins. Based on primary structure, glutenin subunits have been divided into the high-molecular-weight (HMW) subunits (MW=67,000-88,000) and low-molecular-weight (LMW) subunits (MW=32,000-35,000). Each gluten protein type consists or two or three different structural domains; one of them contains unique repetitive sequences rich in glutamine and proline. Native glutenins are composed of a backbone formed by HMW subunit polymers and of LMW subunit polymers branched off from HMW subunits. Non-covalent bonds such as hydrogen bonds, ionic bonds and hydrophobic bonds are important for the aggregation of gliadins and glutenins and implicate structure and physical properties of dough.
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              Gliadin induces an increase in intestinal permeability and zonulin release by binding to the chemokine receptor CXCR3.

              Celiac disease is an immune-mediated enteropathy triggered by gliadin, a component of the grain protein gluten. Gliadin induces an MyD88-dependent zonulin release that leads to increased intestinal permeability, a postulated early element in the pathogenesis of celiac disease. We aimed to establish the molecular basis of gliadin interaction with intestinal mucosa leading to intestinal barrier impairment. Alpha-gliadin affinity column was loaded with intestinal mucosal membrane lysates to identify the putative gliadin-binding moiety. In vitro experiments with chemokine receptor CXCR3 transfectants were performed to confirm binding of gliadin and/or 26 overlapping 20mer alpha-gliadin synthetic peptides to the receptor. CXCR3 protein and gene expression were studied in intestinal epithelial cell lines and human biopsy specimens. Gliadin-CXCR3 interaction was further analyzed by immunofluorescence microscopy, laser capture microscopy, real-time reverse-transcription polymerase chain reaction, and immunoprecipitation/Western blot analysis. Ex vivo experiments were performed using C57BL/6 wild-type and CXCR3(-/-) mouse small intestines to measure intestinal permeability and zonulin release. Affinity column and colocalization experiments showed that gliadin binds to CXCR3 and that at least 2 alpha-gliadin 20mer synthetic peptides are involved in this binding. CXCR3 is expressed in mouse and human intestinal epithelia and lamina propria. Mucosal CXCR3 expression was elevated in active celiac disease but returned to baseline levels following implementation of a gluten-free diet. Gliadin induced physical association between CXCR3 and MyD88 in enterocytes. Gliadin increased zonulin release and intestinal permeability in wild-type but not CXCR3(-/-) mouse small intestine. Gliadin binds to CXCR3 and leads to MyD88-dependent zonulin release and increased intestinal permeability.
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                Author and article information

                Journal
                ijcs
                International Journal of Cardiovascular Sciences
                Int. J. Cardiovasc. Sci.
                Sociedade Brasileira de Cardiologia (Rio de Janeiro, RJ, Brazil )
                2359-4802
                2359-5647
                December 2022
                : 35
                : 6
                : 803-813
                Affiliations
                [2] Maceió orgnameUniversidade Federal de Alagoas Brazil
                [1] Vitória de Santo Antão Pernambuco orgnameUniversidade Federal de Pernambuco Brazil
                [3] Recife Pernambuco orgnameUniversidade Federal Rural de Pernambuco Brazil
                Article
                S2359-56472022000600803 S2359-5647(22)03500600803
                10.36660/ijcs.20200291
                94c2a963-a425-4a67-8e83-088829432e4d

                This work is licensed under a Creative Commons Attribution 4.0 International License.

                History
                : 05 January 2022
                : 17 September 2020
                Page count
                Figures: 0, Tables: 0, Equations: 0, References: 28, Pages: 11
                Product

                SciELO Brazil

                Categories
                Review Article

                Gluten-free diet,Weight loss,Metabolic syndrome,Obesity
                Gluten-free diet, Weight loss, Metabolic syndrome, Obesity

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