Białka glutenu a alergenność mąki pszennej

Łącka, A.; Leszczyńska, J.

Artykuł - szczegóły

Tytuł artykułu

Białka glutenu a alergenność mąki pszennej

Autorzy

Łącka A. , Leszczyńska J.

Wybrane pełne teksty z tego czasopisma

Identyfikatory

Warianty tytułu

Proteins of wheat gluten and the allergenity of wheat flour

Języki publikacji

Abstrakty

W artykule opisane są, na podstawie najnowszej literatury, struktury gliadyn i glutenin, białek glutenu pszennego oraz różnice pomiędzy tymi frakcjami; zawarty jest również przegląd danych literaturowych na temat alergii na pszenicę, związanej z nieprawidłową reakcją na różne typy związków zawartych w ziarnie, przede wszystkim na cztery grupy białek: albuminy, globuliny, gliadyny i gluteniny. Alergia pokarmowa związana jest jednak prawie wyłącznie z nieprawidłowymi reakcjami wywoływanymi przez gluten.

This paper presents structures of gliadins and glutenins, which are proteins of wheat gluten, and the differences between them on the basis of the most recent literature. The second part of this work contains a review of the literature data about allergy to wheat, which is connected to an incorrect reaction to different types of compounds contained in grain, especially for four groups of proteins: albumins, globulins, gliadins and glutenins. Food allergy is almost exclusively connected with adverse reactions induced by gluten.

Słowa kluczowe

alergia pokarmowa alergen pszenny białka glutenu pszennego alergenność mąki pszennej gliadyna glutenina

food allergy wheat allergen wheat gluten proteins allergenity of wheat flour gliadin glutenin

Wydawca

Wydawnictwo Politechniki Łódzkiej

Czasopismo

Zeszyty Naukowe. Chemia Spożywcza i Biotechnologia / Politechnika Łódzka

Rocznik

2005

Tom

Z. 69

Strony

77--89

Opis fizyczny

Bibliogr. 75 poz.

Twórcy

autor

Łącka A.

Instytut Podstaw Chemii Żywności, Politechnika Łódzka

autor

Leszczyńska J.

Instytut Podstaw Chemii Żywności, Politechnika Łódzka

Bibliografia

[1] Osborne T.B.: The proteins of the wheat kernel, Carnegie Institute, Washington DC, Publ. No. 84, 1907.
[2] Osborne T.B.: The vegetable proteins, Longmans, Green and Co., London, 1924.
[3] Cole E.W., Fullington J.G., Kasarda D.D.: Grain protein variability among species of Triticum and Aegilops: quantative SDS-PAGE studies, Theor. Appl. Genet., 60, 17,(1981).
[4] Wieser H., Antes S., Seilmeier W.: Quantative determination of gluten protein types in wheat flour by reversed-phase high-performance liquid chromatography, Cereal Chem., 75, 644, (1998).
[5] Shewry P.R.: Plant storage proteins, Biol. Rev., 70, 375, (1995).
[6] Eliasson A. C., Larsson K.: Cereals in breadmaking, Dekker, New York, 1993.
[7] Autran J.C., Lew E.J., Nimmo C.C., Kasarda D.D.: N-terminal amino acid sequencing of prolamins from wheat and related species, Nature, 282, 527, (1979).
[8] Kasarda D.D. et al.: Nucleic acid (cDNA) and amino acid sequences of alpha-type gliadins from wheat (Triticum aestivum), Proc. Natl. Acad. Sei. USA, 81, 4712, (1984).
[9] Wieser H.: The precipitating factor in coeliac disease, Bailliere’s Clin. Gastroenterol., 9, 191, (1995).
[10] Shewry P., Tatham A.S., Kasarda D.: [W:] Coeliac disease, M. Marsh (red.), Blackwell, Oxford, 1992.
[11] Woychick J.H., Boundy J.A., Dimler R.J.: Arch. Biochem. Biophys., 91, 477, (1961).
[12] Kasarda D.D., Autran J.C., Lew E.J., Nimmo C.C., Shewry P.R.: Biochim. Biophys. Acta, 747, 138, (1983).
[13] Shewry P.R., Tatham A.S.: The prolamin storage proteins of cereal seeds: structure and evolution, Biochem. J., 267, 1, (1990).
[14] Shewry P.R., Tatham A.S.: Disulphide bonds in wheat gluten proteins, J. Cereal Sei., 25, 207, (1997).
[15] Belton P.S.: On the elasticity of wheat gluten, J. Cereal Sei., 29, 103, (1999).
[16] Simonato B. et al.: IgE binding to soluble and insoluble wheat flour proteins in atopic and non-atopic patients suffering from gastrointestinal symptoms after wheat ingestion, Clin. Exp. Allergy, 31, 1771, (2001).
[17] Shewry P.R., Tatham A.S., Forde J., Kreis M., Miflin B.J.: The classification and nomenclature of wheat gluten proteins. A reassessment, J. Cereal Sei., 4, 97, (1986).
[18] Skerritt J.H., Hill A.S., Andrews J.L.: Antigenicity of wheat prolamins: detailed epitope analysis using a panel of monoclonal antibodies, J. Cereal Sei., 32, 259, (2000).
[19] Sumner-Smith M., Rafalski J.A., Sugiyama T., Stoll M., Soll D.: Conservation and variability of wheat alpha/beta gliadin genes, Nucl. Acids Res., 13, 3905, (1985).
[20] Rafalski J.A. et al.: Developmentally regulated plant genes: the nucleotide sequence of a wheat gliadin genomic clone, EMBO J., 3, 1409, (1984).
[21] Sugiyama T., Rafalski J. A., Soll D.: The nucleotide sequence of a wheat gamma- gliadin genomic clone, Plant Sei., 44, 205, (1986).
[22] Tatham A.S., Shewry P.R.: The S-poor prolamins of wheat, barley and rye, J. Cereal Sei., 22, 1, (1995).
[23] Belton P.S., Gil A.M., Grant A., Alberti E., Tatham A.S.: Proton and carbon NMR measurements of the effects of hydratation on the wheat protein ω-gliadin, Spectrochim. Acta A, 54, 955, (1998).
[24] Anderson O.D. et al.: Identification of several new classes of low-molecular- weight wheat gliadin-related proteins and genes, Theor. Appl. Genet., 103, 307, (2001).
[25] Miles M.J., Morris V.J., Carroll V., Wright D.J., Bacon J.J.: Int. J. Biol. Macromol., 6, 291, (1984).
[26] Belton P.S. et al.: FTIR and NMR studies on the hydration of a high Mr subunit of glutenin, Int. J. Biol. Macromol., 17, 74, (1995).
[27] Kasarda D.D.: Wheat kernel proteins: molecular and functional aspects, Viterbo, 1994.
[28] Gilbert S.M. et al.: Expression and characterisation of a highly repetitive peptide derived from a wheat seed storage protein, Biochim. Biophys. Acta, 1479, 135, (2000).
[29] Bekkers A.C.A. P.A., De Boef E., Van Dijk A.A., Hamer R.J .: The central domain of high molecular weight glutenin subunits is water-soluble,J. Cereal Sei., 29, 109, (1999).
[30] Miles M. J. et al.: Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure, Proc. Natl. Acad. Sei. USA, 88, 68,(1991).
[31] Tatham A.S., Shewry P.R.: Elastomeric proteins: biological roles, structures and mechanisms, Trends Biochem. Sei., 25, 567, (2000).
[32] Thomson N.H. et al.: Small angle X-ray scattering of wheat seed-storage proteins: α-, γ- and ω-gliadins and the high molecular weight (HMW) subunits of glutenin, Biochim. Biophys. Acta, 1430, 359, (1999).
[33] Nakamura M., Kurata T.: Effect of α-ascorbic acid and superoxide anion radical on the polymerization of wheat flour protein, Food Sei. Technol. Inf., 4, 264, (1998).
[34] Larré C. et al.: Biochemical analysis and rheological properties of gluten modified by transglutaminase, Cereal Chem., 77, 121, (2000).
[35] Valero Santiago A. et al.: Hypersensitivity to wheat flour in bakers, Allergol. Immunopathol., 16, 309, (1988).
[36] Baur X., Posch A.: Characterised allergens causing bakers’ asthma, Allergy, 53, 562 (1998).
[37] Pfeil T., Schwabl U., Ulmer W. T., Konig W.: Western blot analysis for water- soluble wheat flour (Triticum vulgaris) allergens, Int. Arch. Allergy Appl. Immunol., 91, 224, (1990).
[38] Weiss W. et al.: Identification and characterisation of wheat grain albumin/globulin allergens, Electrophoresis, 18, 826, (1997).
[39] Sandiford C.P. et al.: Identification of the major water/salt insoluble wheat proteins involved in cereal hypersensitivity, Clin. Exp. Allergy, 27, 1120, (1997).
[40] Sanchez-Monge R. et al.: Wheat and barley allergens associated with baker’s asthma. Glycosylated subunits of the alpha-amylase-inhibitor family have enhanced IgE-binding capacity, Biochem. J., 281, 401 (1992).
[41] Armentia A., Sanchez-Monge R., Gomez L., Barber D., Salcedo G.: In vivo allergenic activities of eleven purified members of a major allergen family from wheat and barley flour, Clin. Exp. Allergy, 23, 410, (1993).
[42] Posh A., Weiss W., Wheeler C., Dunn M. J., Görg A.: Sequence analysis of wheat grain allergens separated by two-dimensional electrophoresis with immobilized pH gradients, Electrophoresis, 16, 1115, (1995).
[43] Fränken J., Stephan U., Meyer H. E.: Identification of alpha-amylase inhibitor as a major allergen of wheat flour, Int. Arch. Allergy Immunol., 104, 171 (1994).
[44] Amano M. et al.: Identification of the major allergens in wheat flour responsible for baker’s asthma, Biochem. J., 330, 1229, (1998).
[45] Sanchez-Monge R., Garcia-Casado G., Lopez-Otin C., Armentia A., Salcedo G.: Wheat flour peroxidase is a prominent allergen associated with baker’s asthma, Clin. Exp. Allergy, 27, 1130, (1997).
[46] Sander I. et al.: Identification of wheat flour allergens by means of 2-dimensional immunoblotting, J. Allergy Clin. Immunol., 107, 907, (2001).
[47] Varjonen E., Vainio E., Kalimo K.: Life-threatening, recurrent anaphylaxis caused by allergy to gliadin and exercise, Clin. Exp. Allergy, 27, 162, (1997).
[48] Varjonen E., Vainio E., Kalimo K.: Antigliadin IgE - indicator of wheat allergy in atopic dermatitis, Allergy, 55, 386, (2000).
[49] Rasanen L., Lehto M., Turjanmaa K., Savolainen J., Reunala T.: Allergy to ingested cereals in atopic children, Allergy, 49, 871, (1994).
[50] Lorentz K.: Cereal allergies and intolerances, [W:] Food poisoning, A.T. Tu (red.), Marcel Dekker Inc., New York, 1992.
[51] Ciclitira P.J., Hellis H.J., Evans D.J.: J. Immunol. Methods, 62, 231, (1983).
[52] Bufe A., Gehlhar K., Schramm G., Schlaak M., Becker W.M.: Allergenic activity of a major grass pollen allergen is elevated in the presence of nasal secretion, Am. J. Respir. Crit. Care Med., 157, 1269, (1998).
[53] Kimoto M. et al.: Identification of allergens in cereals and their hypoallergenisation. I. Screening of allergens in wheat and identification of an allergen, Tri a Bd 17 K, Ann. Report Interdisipl. Res. Inst. Environ. Sei., 17, 53, (1998).
[54] Walsh B.J., Howden M.E.: A method for the detection of IgE binding sequences of allergens based on a modification of epitope mapping, J. Immunol. Methods, 121,275,(1989).
[55] Weiss W., Vogelmeier C., Görg A.: Electrophoretic characterization of wheat grain allergens from different cultivars involved in baker’s asthma, Electrophoresis, 14, 805,(1993).
[56] Sutton R., Hill D.H., Baldo B.A., Wrigley C.W.: Immunoglobulin E antibodies to ingested cereal flour components: studies from subjects with asthma and eczema, Clin. Allergy, 12, 63, (1982).
[57] Maruyama N. et al.: Identification of major wheat allergens by means of the Escherichia coli expression system, Eur. J. Biochem., 255, 739, (1998).
[58] Tanabe S. et al.: A major wheat allergen has a Gln-Gln-Gln-Pro-Pro motif identified as an IgE-binding epitope, Biochem. Biophys. Res. Commun., 219, 290, (1996).
[59] Hansen L.P., Millington R.J.: Blockage of protein enzymatic digestion (carboxypeptidase-B) by heat-induced sugar-lysine reactions, J. Food Sei., 44, 1173, (1979).
[60] Palosuo K. et al.: A novel wheat gliadin as a cause of exercise-induced anaphylaxis, J. Allergy Clin. Immunol., 103, 912, (1999).
[61] Palosuo K., Alenius H., Varjonen E., Kalkkinen N., Reunala T.: Rye γ-70 and γ- 35 secalins and barley γ-3 hordein cross-react with ω-5 gliadin, a major allergen in wheat-dependent, exercise-induced anaphylaxis, Clin. Exp. Allergy, 31, 466, (2001).
[62] Morita E., Kameyoshi Y., Mihara S., Hiragun T., Yamamoto S.: γ-gliadin: a presumptive allergen causing wheat-dependent exercise-induced anaphylaxis, Brit. J. Dermatol., 145, 182, (2001).
[63] Hansen L., Johnston P.: Heat-moisture effects on wheat flour. II. An evaluation study of heat-processing effects on flour proteins by digestive enzymes - pepsin, trypsin, and trypsin-carboxypeptidase-B, Cereal Chem., 53, 656, (1976).
[64] Kushimoto H., Aoki T.: Wheat allergy. Relation to exercise-induced anaphylaxis, Arch. Dermatol., 121, 355, (1985).
[65] Molberg O. et al.: Tissue transglutaminase selectively modifies gliadin peptides that are recognised by gut-derived T-cells in celiac disease, Nat. Med., 4, 713, (1998).
[66] van der Wal Y., Kooy Y.M.C., Drijfhout J.W., Amons R., Koning F.: Peptide binding of the coeliac disease-associated DQ (alpha 1*0501, beta 1*0201) molecule, Immunogenetics, 44, 246, (1996).
[67] Terreaux C. et al.: Increased HLA-DQ2-affmity of a synthetic gliadin peptide by acid-induced deamidation of glutamine residues, Bioorg. Med. Chem. Lett., 8, 2039 (1998).
[68] Osman A.A., Uhlig H., Thamm B., Schneider-Mergener J., Mothes T.: Use of
the phage display technique for detection of epitopes recognized by polyclonal rabbit gliadin antibodies, FEBS Lett., 433, 103, (1998).
[69] Sissons M.J., Blundell M.J., Hill A.S., Skerritt J.H.: Antibodies to N-terminal peptides of low Mr subunits of wheat glutenin. I. Characterisation of the antibody responce, J. Cereal Sei., 30, 283, (1999).
[70] Tatham A.S., Marsh M.N., Wieser H., Shewry P.R.: Conformational studies of peptides corresponding to the coeliac-activating regions of wheat alpha-gliadin, Biochem. J., 270,313,(1990).
[71] Alfonso P. et al.: ß-structure motif recognition by anti-gliadin antibodies in coeliac disease, FEBS Lett., 427, 36, (1998).
[72] Tanabe S. et al.: Isolation and characterization of a novel polysaccharide as a possible allergen occuring in wheat flour, Biosci. Biotechnol. Biochem., 64, 1675, (2000).
[73] Kaukinen K. et al.: Intolerance to cereals is not specific for coeliac disease, Scand. J. Gastroenterol., 35, 942, (2000).
[74] Protein Sequence Database, Protein Information Resource of the National Biomedical Research Foundation, http://www-nbrf.georgetown.edu/
[75] Brett G.M. et al.: Epitope mapping studies of broad specificity monoclonal antibodies to cereal prolamins, J. Cereal Sei., 29, 117, (1999).

Typ dokumentu

Bibliografia

Identyfikator YADDA

bwmeta1.element.baztech-article-LOD3-0010-0004