Celiac Disease Can Affect More Than Just CREDIT the Gastrointestinal System GURSIMRAN SINGH KOCHHAR, MD, TAVANKIT SINGH, MD ANANT GILL, MBBS DONALD F

Total Page:16

File Type:pdf, Size:1020Kb

Celiac Disease Can Affect More Than Just CREDIT the Gastrointestinal System GURSIMRAN SINGH KOCHHAR, MD, TAVANKIT SINGH, MD ANANT GILL, MBBS DONALD F REVIEW CME EDUCATIONAL OBJECTIVE: Readers will recognize that celiac disease can affect more than just CREDIT the gastrointestinal system GURSIMRAN SINGH KOCHHAR, MD, TAVANKIT SINGH, MD ANANT GILL, MBBS DONALD F. KIRBY, MD, FACP, FACN, CNSC, FACP Department of Internal Medicine, Saraswathi Institute of Medical FACG, AGAF, CNSC, CPNS Department of Gastroenterology and Hepatology, Cleveland Clinic Sciences, Anwarpur, Center for Human Nutrition, Digestive Disease Digestive Disease Institute, Cleveland Clinic Uttar Pradesh, India Institute, Cleveland Clinic; Professor, Cleveland Clinic Lerner College of Medicine of Case Western Reserve University, Cleveland, OH Celiac disease: Managing a multisystem disorder ABSTRACT eliac disease is an autoimmune disorder C that occurs in genetically predisposed in- Celiac disease is a multisystem autoimmune disorder that dividuals in response to ingestion of gluten. Its can cause symptoms involving the gastrointestinal tract prevalence is about 0.7% of the US population.1 and other organ systems such as the skin and bones. This paper reviews the pathogenesis, diagnosis, and manage- See related editorial, page 228 ment of celiac disease and associated diseases. The gold standard for diagnosis is duode- KEY POINTS nal biopsy, in which the histologic features may include varying gradations of flattening Besides gastrointestinal symptoms, celiac disease is as- of intestinal villi, crypt hyperplasia, and infil- sociated with a variety of diseases, including dermatitis tration of the lamina propria by lymphocytes. herpetiformis, malabsorption of several nutrients (poten- Many patients have no symptoms at the time tially leading to osteoporosis, iron deficiency anemia, and of diagnosis, but presenting symptoms can other disorders), and intestinal malignancies. include diarrhea along with features of mal- absorption,2 and, in about 25% of patients (mainly adults), a bullous cutaneous disorder While serologic testing for immunoglobulin A antibod- 3,4 ies to tissue transglutaminase can be used as an initial called dermatitis herpetiformis. The patho- screening test for this condition, the confirmatory tests genesis of celiac disease and that of dermati- tis herpetiformis are similar in that in both, are invasive, involving upper endoscopy for duodenal ingestion of gluten induces an inflammatory biopsy in celiac disease and skin biopsy in dermatitis reaction leading to the clinical manifesta- herpetiformis. tions. The mainstay of treatment of celiac disease The only effective treatment is lifelong adherence to a remains avoidance of gluten in the diet. gluten-free diet, and nonadherence is a common cause of refractory disease. ■ GENETIC PREDISPOSITION AND DIETARY TRIGGER Concomitant conditions such as anemia and vitamin The pathogenesis of celiac disease has been deficiency often require nutritional supplements. In addi- well studied in both humans and animals. The tion, patients with dermatitis herpetiformis often require disease is thought to develop by an interplay of treatment with dapsone. genetic and autoimmune factors and the inges- tion of gluten (ie, an environmental factor). Celiac disease occurs in genetically pre- disposed individuals, ie, those who carry the HLA alleles DQ2 (DQA1*05, DQB1*02), DQ8 (DQA1*03, DQB1*0302), or both.5 Ingestion of gluten is necessary for the disease doi:10.3949/ccjm.83a.14158 to develop. Gluten, the protein component of CLEVELAND CLINIC JOURNAL OF MEDICINE VOLUME 83 • NUMBER 3 MARCH 2016 217 CELIAC DISEASE TABLE 1 by both the innate and adaptive immune sys- tems that can ultimately result in flattening of Diseases associated villi and crypt hyperplasia (Figure 1).7 with celiac disease Tissue transglutaminase also plays a cen- tral role in the pathogenesis, as it further Endocrine deaminates gliadin and increases its immu- Hashimoto thyroiditis Type 1 diabetes mellitus nogenicity by causing it to bind to receptors Addison disease on antigen-presenting cells with stronger af- Osteoporosis finity. Furthermore, gliadin-tissue transgluta- Osteopenia minase complexes formed by protein cross- linkages generate an autoantibody response Dermatologic Dermatitis herpetiformis (predominantly immunoglobulin A [IgA] Alopecia areata type) that can exacerbate the inflammatory process.8,9 Hepatic Certain viral infections during childhood, Autoimmune hepatitis such as rotavirus and adenovirus infection, Primary biliary cirrhosis 10–13 Primary sclerosing cholangitis can increase the risk of celiac disease. Nonalcoholic fatty liver disease Although earlier studies reported that breast- feeding seemed to have a protective effect,14 as Obstetric and gynecologic did introducing grains in the diet in the 4th to Amenorrhea 6th months of life as opposed to earlier or lat- Delayed menarche er,15 more recent studies have not confirmed Early menopause 16,17 Recurrent spontaneous abortion these benefits. Infertility Loss of libido ■ CLINICAL FEATURES Neurologic Most adults diagnosed with celiac disease are Celiac disease Cerebellar ataxia in their 30s, 40s, or 50s, and most are women. Peripheral neuropathy Diarrhea remains a common presenting occurs in Epilepsy symptom, although the percentage of patients carriers of Dementia with celiac disease who present with diarrhea 18,19 HLA-DQ2, Psychiatric has decreased over time. Depression Abdominal pain and weight loss are also HLA-DQ8, Schizophrenia common.20 or both Oncologic Pallor or decreased exercise tolerance can Intestinal T-cell lymphoma develop due to anemia from iron malabsorp- Adenocarcinoma of small intestine tion, and some patients have easy bruising due to vitamin K malabsorption. Cardiac Autoimmune myocarditis Gynecologic and obstetric complications associated with celiac disease include delayed menarche, amenorrhea, spontaneous abor- tion, intrauterine growth retardation, preterm delivery, and low-birth-weight babies.21,22 Pa- wheat, barley, and rye, contains proteins called tients who follow a gluten-free diet tend to prolamins, which vary among the different have a lower incidence of intrauterine growth types of grain. In wheat, the prolamin is gliadin, retardation, preterm delivery, and low-birth- which is alcohol-soluble. In barley the prolamin weight babies compared with untreated pa- is hordein, and in rye it is secalin.4 The prolamin tients.21,22 content in gluten makes it resistant to degrada- Osteoporosis and osteopenia due to mal- tion by gastric, pancreatic, and intestinal brush absorption of vitamin D are common and are border proteases.6 Gluten crosses the epithelial seen in two-thirds of patients presenting with barrier and promotes an inflammatory reaction celiac disease.23 A meta-analysis and position 218 CLEVELAND CLINIC JOURNAL OF MEDICINE VOLUME 83 • NUMBER 3 MARCH 2016 KOCHHAR AND COLLEAGUES Pathogenesis of celiac disease Gluten Villi flattening Crypt hyperplasia Gliadin Apoptosis of enterocytes Transcytosis Inflammatory Lamina propria response Deamination Secretion of Fibroblast tTG proinflammatory activation cytokines Deaminated gliadin IgA Presentation of Activated T cell autoantibody deaminated peptides response by antigen-presenting cell to T cell Antigen- presenting B cell cell T cell CCF ©2016 Medical Illustrator: David Schumick FIGURE 1. Celiac disease is an autoimmune disorder that, in genetically susceptible individuals, is triggered by ingestion of foods containing gluten. IgA = immunoglobulin A; tTG = tissue transglutaminase. CLEVELAND CLINIC JOURNAL OF MEDICINE VOLUME 83 • NUMBER 3 MARCH 2016 219 CELIAC DISEASE Dermatitis herpetiformis Dermatitis herpetiformis is one of the most common cutaneous manifestations of celiac disease. It presents between ages 10 and 50, and unlike celiac disease, it is more common in males.30 The characteristic lesions are pruritic, grouped erythematous papules surmounted by vesicles distributed symmetrically over the ex- tensor surfaces of the upper and lower extremi- ties, elbows, knees, scalp, nuchal area, and but- tocks31 (Figures 2 and 3). In addition, some patients also present with vesicles, erythematous macules, and erosions in the oral mucosa32 or purpura on the palms and soles.33–35 The pathogenesis of dermatitis herpetifor- mis in the skin is related to the pathogenesis of celiac disease in the gut. Like celiac disease, dermatitis herpetiformis is more common in genetically predisposed individuals carrying either the HLA-DQ2 or the HLA-DQ8 haplo- type. In the skin, there is an analogue of tissue transglutaminase called epidermal transgluta- minase, which helps in maintaining the integ- rity of cornified epithelium.36 In patients with celiac disease, along with formation of IgA antibodies to tissue transglutaminase, there is also formation of IgA antibodies to epidermal transglutaminase. IgA antibodies are deposit- ed in the tips of dermal papillae and along the FIGURE 2. Eroded and crusted erythematous plaques with basement membrane.37–39 These deposits then scalloped borders on the elbow of a patient with dermati- initiate an inflammatory response that is pre- tis herpetiformis. dominantly neutrophilic and results in forma- 40 Photo courtesy of Alok Vij, Department of Dermatology, Cleveland Clinic. tion of vesicles and bullae in the skin. Also supporting the linkage between celiac disease statement from Canada concluded that dual- and dermatitis herpetiformis, if patients ad- energy x-ray absorptiometry should be done at here to a gluten-free diet, the deposits of im- the time of diagnosis of celiac disease if the mune complexes in the skin disappear.41 patient
Recommended publications
  • Protein Fractions of Oats and Possibilities of Oat Utilisation for Patients with Coeliac Disease
    Czech J. Food Sci. Vol. 22, No. 4: 151–162 Protein Fractions of Oats and Possibilities of Oat Utilisation for Patients with Coeliac Disease I���� CAPOUCHOVÁ1, J��� PETR1, H����� TLASKALOVÁ-HOGENOVÁ2, I��� MICHALÍK3, O������ FAMĚRA1, D��� URMINSKÁ3, L������ TUČKOVÁ2, H������� KNOBLOCHOVÁ3 and D��� BOROVSKÁ2 1Czech University of Agriculture in Prague, Prague, Czech Republic; 2Microbiological Institute of the Academy of Sciences of the Czech Republic, Prague, Czech Republic; 3Slovak University of Agriculture, Nitra, Slovak Republic Abstract C��������� I., P��� J., T���������-H������� H., M������� I., F����� O., U������� D., T������ L., K���������� H., B������� D. (2004): Protein fractions of oats and possibilities of oat utilisation for patients with coeliac disease. Czech J. Food Sci., 22: 151–162. The applicability was evaluated of 16 different oats species and varieties of different provenance in the coeliac diet in view of the composition of the protein complex and immunological testing during two-year experiments (2001 and 2002). Determination was carried out of total nitrogen content (average of evaluated oats collection in 2001 was 2.21%, in 2002 2.78%), protein nitrogen content (average 2001 1.94%, 2002 2.28%), and crude protein (N × 6.25) content (average 2001 13.80%, 2002 17.37%). The proportions of different protein fractions play a decisive role for the aims of this study because, based on the existing knowledge, coeliacally active protein components are present particularly in the prolamin fraction. The percentage of prolamins (determined by discontinual fractionation after Osborne) in the author’s evaluated collection of oats species and varieties under the conditions of Central Bohemia reached on average 17.68% of the total protein in 2001, and 15.36% in 2002.
    [Show full text]
  • Prolamin Degradation in Sourdoughs
    Prolamin degradation in sourdoughs Jussi Loponen University of Helsinki EKT-sarja 1372 EKT series 1372 Helsinki 2006 Helsingin yliopisto Elintarviketeknologian laitos University of Helsinki Department of Food Technology EKT-SARJA 1372 EKT SERIES 1372 PROLAMIN DEGRADATION IN SOURDOUGHS JUSSI LOPONEN ACADEMIC DISSERTATION To be presented with the permission of the Faculty of Agriculture and Forestry of the University of Helsinki, for public criticism in the Walter-hall, Viikki on December 20th, 2006 at 12 o’clock noon. HELSINKI 2006 Custos Professor Hannu Salovaara Department of Food Technology University of Helsinki Helsinki, Finland Supervisors Professor Hannu Salovaara Department of Food Technology University of Helsinki Helsinki, Finland University Lecturer Tuula Sontag-Strohm Department of Food Technology University of Helsinki Helsinki, Finland Reviewers Dr. Berne Jones, Supervisory Research Chemist (retired) USDA, ARS, Cereal Crops Research Unit Madison, WI, USA Dr. Michael Gänzle, Assistant Professor Department of Agricultural, Food and Nutritional Science University of Alberta Edmonton, Canada Opponent Dr. Peter Weegels, Lead Technologist Unilever Research & Development Vlaardingen, the Netherlands ISBN 952-10-3581-1 (paperback) ISBN 952-10-3582-X (PDF) ISSN 0355-1180 Yliopistopaino Helsinki 2006 2 CONTENTS ABSTRACT 4 PREFACE 5 LIST OF ORIGINAL PUBLICATIONS AND AUTHORSHIPS 6 ABBREVIATIONS 7 1 INTRODUCTION 8 2 LITERATURE REVIEW 10 2.1 The Proteolytic systems of cereal grains 10 2.1.1 The Prolamins of the Triticeae cereals (wheat,
    [Show full text]
  • Barley C-Hordein As the Calibrant for Wheat Gluten Quantification
    foods Article Barley C-Hordein as the Calibrant for Wheat Gluten Quantification Xin Huang * , Kaiyue Ma, Sara Leinonen and Tuula Sontag-Strohm Department of Food and Nutrition, Faculty of Agriculture and Forestry, University of Helsinki, Agnes Sjöberginkatu 2, PL66, FI-00014 Helsinki, Finland; kaiyue.ma@helsinki.fi (K.M.); [email protected] (S.L.); tuula.sontag-strohm@helsinki.fi (T.S.-S.) * Correspondence: xin.huang@helsinki.fi Received: 8 October 2020; Accepted: 5 November 2020; Published: 10 November 2020 Abstract: The lack of certified reference materials has been one major challenge for gluten quantification in gluten-free products. In this study, the feasibility of using barley C-hordein as the calibrant for wheat gluten in R5 sandwich enzyme-linked immunosorbent assay (ELISA) was investigated. The gluten composition and total gluten R5 reactivity ranged largely depending on the genotypes and the growing environment. The conversion factor of gliadin to gluten averaged 1.31 for common wheat, which is smaller than the theoretical factor of 2. Each gluten group had varying reactivity against the R5 antibody, where !1.2-, γ- and α-gliadins were the main reactive groups from wheat gluten. A mixture of wheat cultivars or one single cultivar as the reference material can be difficult to keep current. Based on the average R5 reactivity of total gluten from the 27 common wheat cultivars, here we proposed 10% C-hordein mixed with an inert protein as the calibrant for wheat gluten quantification. In spiking tests of gluten-free oat flour and biscuits, calibration using 10% C-hordein achieved the same recovery as the gliadin standard with its cultivar-specific conversion factor.
    [Show full text]
  • Recent Progress and Recommendations on Celiac Disease from the Working Group on Prolamin Analysis and Toxicity
    REVIEW published: 17 March 2020 doi: 10.3389/fnut.2020.00029 Recent Progress and Recommendations on Celiac Disease From the Working Group on Prolamin Analysis and Toxicity Katharina A. Scherf 1, Carlo Catassi 2, Fernando Chirdo 3, Paul J. Ciclitira 4, Conleth Feighery 5, Carmen Gianfrani 6, Frits Koning 7, Knut E. A. Lundin 8, Detlef Schuppan 9, Marinus J. M. Smulders 10, Olivier Tranquet 11, Riccardo Troncone 12 and Peter Koehler 13* Edited by: 1 Department of Bioactive and Functional Food Chemistry, Institute of Applied Biosciences, Karlsruhe Institute of Technology Jun Lu, (KIT), Karlsruhe, Germany, 2 Department of Pediatrics, Polytechnic University of Marche, Ancona, Italy, 3 Instituto de Estudios Auckland University of Technology, Inmunologicos y Fisiopatologicos- IIFP (UNLP-CONICET), Universidad Nacional de La Plata, La Plata, Argentina, 4 Norwich New Zealand Medical School, University of East Anglia, Norwich, United Kingdom, 5 St. James’s Hospital, University of Dublin, Dublin, 6 7 Reviewed by: Ireland, Institute of Biochemistry and Cell Biology, Italian National Council of Research, Naples, Italy, Leiden University 8 Sachin Rustgi, Medical Centre, Leiden, Netherlands, Department of Gastroenterology, Oslo University Hospital Rikshospitalet and Stiftelsen 9 Clemson University, United States KG Jebsen Coeliac Disease Research Centre, University of Oslo, Oslo, Norway, Institute for Translational Medicine, 10 Govind K. Makharia, University Medical Center of the Johannes Gutenberg University Mainz, Mainz, Germany, Plant Breeding, Wageningen 11 12 All India Institute of Medical University & Research, Wageningen, Netherlands, INRAE, UR BIA, Nantes, France, European Laboratory for the Sciences, India Investigation of Food Induced Diseases (ELFID), Department of Medical Translational Sciences, University Federico II, Naples, 13 Emanuele Zannini, Italy, biotask AG, Esslingen, Germany University College Cork, Ireland Luis Rodrigo, Celiac disease (CD) affects a growing number of individuals worldwide.
    [Show full text]
  • Composition, Physicochemical Properties of Pea Protein and Its Application in Functional Foods
    Critical Reviews in Food Science and Nutrition ISSN: 1040-8398 (Print) 1549-7852 (Online) Journal homepage: https://www.tandfonline.com/loi/bfsn20 Composition, physicochemical properties of pea protein and its application in functional foods Z. X. Lu, J. F. He, Y. C. Zhang & D. J. Bing To cite this article: Z. X. Lu, J. F. He, Y. C. Zhang & D. J. Bing (2019): Composition, physicochemical properties of pea protein and its application in functional foods, Critical Reviews in Food Science and Nutrition, DOI: 10.1080/10408398.2019.1651248 To link to this article: https://doi.org/10.1080/10408398.2019.1651248 Published online: 20 Aug 2019. Submit your article to this journal Article views: 286 View related articles View Crossmark data Full Terms & Conditions of access and use can be found at https://www.tandfonline.com/action/journalInformation?journalCode=bfsn20 CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION https://doi.org/10.1080/10408398.2019.1651248 REVIEW Composition, physicochemical properties of pea protein and its application in functional foods Z. X. Lua,J.F.Heb, Y. C. Zhanga, and D. J. Bingc aLethbridge Research and Development Centre, Agriculture and Agri-Food Canada, Lethbridge, Alberta, Canada; bInner Mongolia Academy of Agriculture and Animal Husbandry Sciences, Hohhot, Inner Mongolia, P.R. China; cLacombe Research and Development Centre, Agriculture and Agri-Food Canada, Lacombe, Alberta, Canada ABSTRACT KEYWORDS Field pea is one of the most important leguminous crops over the world. Pea protein is a rela- Pea; protein; composition; tively new type of plant proteins and has been used as a functional ingredient in global food physicochemical property; industry.
    [Show full text]
  • Divergent Properties of Prolamins in Wheat and Maize Wei Zhang Rutgers University - New Brunswick/Piscataway
    Agronomy Publications Agronomy 6-2013 Divergent properties of prolamins in wheat and maize Wei Zhang Rutgers University - New Brunswick/Piscataway Vavaporn Sangtong United States Department of Agriculture Joan Peterson United States Department of Agriculture M. Paul Scott Iowa State University, [email protected] Follow this and additional works at: http://lib.dr.iastate.edu/agron_pubs Part of the Agricultural Science Commons, Agronomy and Crop Sciences Commons, and the Plant Breeding and Genetics Commons The ompc lete bibliographic information for this item can be found at http://lib.dr.iastate.edu/ agron_pubs/173. For information on how to cite this item, please visit http://lib.dr.iastate.edu/ howtocite.html. This Article is brought to you for free and open access by the Agronomy at Iowa State University Digital Repository. It has been accepted for inclusion in Agronomy Publications by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. Planta (2013) 237:1465–1473 DOI 10.1007/s00425-013-1857-5 ORIGINAL ARTICLE Divergent properties of prolamins in wheat and maize Wei Zhang • Vavaporn Sangtong • Joan Peterson • M. Paul Scott • Joachim Messing Received: 14 December 2012 / Accepted: 8 February 2013 / Published online: 23 February 2013 Ó Springer-Verlag Berlin Heidelberg 2013 Abstract Cereal grains are an important nutritional Abbreviations source of amino acids for humans and livestock worldwide. RNAi RNA interference Wheat, barley, and oats belong to a different subfamily of DAP Days after pollination the grasses than rice and in addition to maize, millets, HMW High-molecular weight sugarcane, and sorghum. All their seeds, however, are largely devoid of free amino acids because they are stored during dormancy in specialized storage proteins.
    [Show full text]
  • All About Gluten & Celiac Disease
    College of Agricultural, Consumer and Environmental Sciences All About Discovery! ™ New Mexico State University aces.nmsu.edu All about Gluten? Celiac disease, gluten sensitivity, wheat sensitivity, and other Dr. Raquel Garzon, RDN NMSU Cooperative Extension Services considerations Nutrition and Wellness State Specialist About the College: The College of Agricultural, Consumer and Environmental Sciences is an engine for economic and community development in New Mexico, improving the lives of New Mexicans through academic, research, and extension programs. All About Discovery! ™ New Mexico State University aces.nmsu.edu All About Discovery! ™ New Mexico State University aces.nmsu.edu Definitions Gluten: A heterogenous mix of water-insoluble storage proteins in cereal grains, wheat, rye, and barley, that gives dough its elastic properties; it consists of two fractions: prolamins and glutelins; the fractions of wheat are gliadins and glutenins Prolamins: Difficult to digest; the high content of proline and glutamine content in gluten that prevents complete breakdown by digestive enzymes; this is the component that causes issues in celiac disease Gliadin: The prolamin in wheat Secalin: The prolamin in rye Hordein: The prolamin in barley Avenin: The prolamin in oats FODMAPs: Fermentable Oligo-, Di-, and Mono-saccharides And Polyols; short chain carbohydrates poorly absorbed in the small intestine; osmotically active and highly fermentable by gut bacteria 2016 REVITALIZE PROJECT, INC. All About Discovery! ™ New Mexico State University aces.nmsu.edu
    [Show full text]
  • Immunochemical Analysis of Prolamins in Gluten-Free Foods
    Department of Food and Environmental Sciences University of Helsinki Finland Immunochemical analysis of prolamins in gluten-free foods Päivi Kanerva ACADEMIC DISSERTATION To be presented, with the permission of the Faculty of Agriculture and Forestry of the University of Helsinki, for public examination in the B2 hall, Viikki, on 4 November 2011, at 12 noon. Helsinki 2011 Kanerva, P. 2011. Immunochemical analysis of prolamins in gluten-free foods (dissertation). EKT series 1530. University of Helsinki. Department of Food and Environmental Sciences, 94 pp. ABSTRACT People with coeliac disease have to maintain a gluten-free diet, which means excluding wheat, barley and rye prolamin proteins from their diet. Immunochemical methods are used to analyse the harmful proteins and to control the purity of gluten-free foods. In this thesis, the behaviour of prolamins in immunological gluten assays and with different prolamin-specific antibodies was examined. The immunoassays were also used to detect residual rye prolamins in sourdough systems after enzymatic hydrolysis and wheat prolamins after deamidation. The aim was to characterize the ability of the gluten analysis assays to quantify different prolamins in varying matrices in order to improve the accuracy of the assays. Prolamin groups of cereals consist of a complex mixture of proteins that vary in their size and amino acid sequences. Two common characteristics distinguish prolamins from other cereal proteins. Firstly, they are soluble in aqueous alcohols, and secondly, most of the prolamins are mainly formed from repetitive amino acid sequences containing high amounts of proline and glutamine. The diversity among prolamin proteins sets high requirements for their quantification.
    [Show full text]
  • Improved Extraction of Prolamins for Gluten Detection in Processed Foods
    AGRICULTURAL AND FOOD SCIENCE AGRICULTURAL AND FOOD SCIENCE Kanerva,Vol. P. et 20(2011): al. Extraction 206–216. of prolamins Improved extraction of prolamins for gluten detection in processed foods Päivi Kanerva*, Tuula Sontag-Strohm, Outi Brinck and Hannu Salovaara Department of Food and Environmental Sciences, PO Box 66, FI-00014 University of Helsinki, Finland e-mail:[email protected] A problem in gluten analysis has been inconsistent extractability of prolamins, particularly from processed foods consisting of unknown portions of prolamins from wheat, barley, and rye. This study aimed at im- proving the extraction of prolamins for immunological analysis, regardless of the cereal species and the production process. The prolamins were extracted with varying concentrations of ethanol, 1-propanol, and 2-propanol. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis and Western blotting were applied to study the protein composition of the extracts and the antibody recognition of the prolamin subgroups. We characterized the affinities of prolamin-specific antibodies that are used in gluten analysis against the prolamin groups that were soluble in 40% 1-propanol. The antibody R5 recognized more abundantly the medium-molecular weight groups, including polymeric proteins, and less the high-molecular weight groups than the anti-ω-gliadin antibody. In the present study, the prolamins were most efficiently extracted by 40% 1-propanol with 1% dithiothreitol at 50 °C . The prolamins were extracted from processed bread samples with efficiency similar to that from untreated meal samples. Key-words: barley; celiac disease; gluten; prolamin; rye; wheat Introduction which means excluding wheat, barley, or rye protein- containing products from the diet.
    [Show full text]
  • Protein Complex of Wheat, Buckwheat and Maize in Relation to Celiac Disease
    PROTEIN COMPLEX OF WHEAT, BUCKWHEAT AND MAIZE IN RELATION TO CELIAC DISEASE Milan Chňapek*, Marián Tomka, Želmíra Balážová, Zdenka Gálová Address(es): Ing., Phd., Milan Chňapek, Slovak University of Agriculture, Faculty of Biotechnology and Food Sciences, Department of Biochemistry and Biotechnology, Tr. A.. Hlinku 2, 949 76 Nitra, Slovak Republic, +421 37 6414277. *Corresponding author: [email protected] ARTICLE INFO ABSTRACT Received 12. 11. 2013 Cereals are the most wide spread and very important plants utilized as a food source for mankind and for animals where they play role in Revised 2. 12. 2013 energetical metabolism and proteosynthesis. Cereals contain proteins with unique properties. These properties allow us to produce Accepted 16. 12. 2013 leavened bread. Technological characteristic of cereal grain is determined by quantity and quality of storage proteins which represent Published 1. 2. 2014 alcohol soluble prolamins and glutenins soluble in acids and basis solutions. Celiac disease is one of the most frequent food intolerance caused by cereal storage proteins. Therapy consists of strict diet without consumptions of cereals or gluten. Pseudocereals are very perspective groups of plants in gluten free diet, due to absence of celiac active proteins, but on the other hand, flour from pseudocereals Regular article is not very suitable for baking. There are a lot of analytical methods applicable for detection of celiac active proteins in cereal and pseudocereal grain. Electrophoretical and immunochemical methods are the most utilized. Genotypes of wheat and maize were homogeneous and singlelined in contrast with genotypes of buckwheat. Average content of HMW-GS was highest in genotypes of bread wheat and lowest in buckwheat varieties.
    [Show full text]
  • The Prolamin Storage Proteins of Sorghum and Millets
    THE PROLAMIN STORAGE PROTEINS OF SORGHUM AND MILLETS P R Shewry1 and N G. Halford2 1Long Ashton Research Station, Long Ashton, Bristol BS41 9AF, UK, E-mail: [email protected] 2Rothamsted Research, Harpenden, Herts AL5 2JQ, UK Most millets are classified with maize, sorghum and Coix (Job's tears) in the grass sub-family Panicoideae, but two species, tef and ragi (finger millet) are placed in a separate sub-family, the Chloridoideae. In all species the major storage proteins are alcohol-soluble prolamins, but their properties vary. For example, although the kafirins of sorghum are closely related to the zeins of maize, they differ in their solubility properties, being more efficiently extracted with 60% (v/v) tertiary butanol, a less polar solvent than propan-2-ol. Maize prolamins are classified into four groups, termed alpha-, beta-, gamma- and delta-zeins. Of these, the alpha-zeins are the major fraction but have low nutritional quality, with low contents of cysteine and methionine and no lysine or tryptophan. In contrast, the beta-zeins and delta-zeins contain about 11 mol% and over 20 mol% methionine, respectively. Alpha-type prolamins appear to be the major components in sorghum, Coix and all millet species which have been analysed in detail (pearl millet, foxtail millet, kodo millet, tef, ragi), with the exception of fonio (Digitaria exilis). Sorghum and Coix also contain homologues of the beta-and gamma-zeins of maize and sorghum homologues of delta-zein. Less well-characterized methionine-rich components have also been reported in foxtail millet and fonio, forming the major prolamin group in the latter species.
    [Show full text]
  • Celiac Disease-Specific Prolamin Peptide Content of Wheat Relatives and Wild Species Determined by ELISA Assays and Bioinformatics Analyses
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Repository of the Academy's Library Cereal Research Communications 43(1), pp. 133–143 (2015) DOI: 10.1556/CRC.43.2015.1.13 Celiac Disease-specific Prolamin Peptide Content of Wheat Relatives and Wild Species Determined by ELISA Assays and Bioinformatics Analyses GY.GELL1,K.KOVÁCS1,I.MOLNÁR2,ZS.BUGYI3,S.TÖMÖSKÖZI3 and A. JUHÁSZ1* 1Applied Genomics Department, Agricultural Institute, Centre for Agricultural Research, HAS, Martonvásár, Hungary 2Department of Plant Genetic Resources and Organic Breeding, Agricultural Institute, Centre for Agricultural Research, HAS, Martonvásár, Hungary 3Department of Applied Biotechnology and Food Science, Budapest University of Technology and Economics, Budapest, Hungary (Received 8 September 2014; Accepted 10 November 2014; Communicated by F. Békés) Enzyme-linked immunosorbent assays (ELISAs) are widely used to determine gluten con- tamination in gluten-free and low gluten food samples. ELISA assays developed using monoclonal antibodies against known toxic peptides have an advantage in the identification of toxic prolamin content in protein extracts of different food samples, as well as raw materials. R5 and G12 monoclonal antibodies specific for two known toxic peptides used in commer- cially available gluten ELISA assays were applied to test toxic peptide contents in wheat rela- tives and wild wheat species with different genome composition and complexity. Although the R5 peptide content showed some correlation with ploidy levels in Triticum species, there was a high variance among Aegilops species. Some of the analysed diploid Aegilops species showed extremely high R5 peptide contents. Based on the bioinformatics analyses, the R5 peptide was present in most of the sulphur rich prolamins in all the analysed species, whereas the G12 epitope was exclusively present in alpha gliadins.
    [Show full text]