Maillard reaction in food allergy: Pros and cons

References

• Ahmed, N. (2005). Advanced glycation endproducts–role in pathology of diabetic complications. Diabetes Res. Clin. Pract. 67(1):3–21.
   PubMed Web of Science ®Google Scholar
• Alison, G., Joshua, A. B., Ann, M. S. and Mark, A. C. (2006). Advanced glycation end products: sparking the development of diabetic. Circulation. 114:597–605.
   PubMed Web of Science ®Google Scholar
• Ames, J. M. (1992). The Maillard reaction. In: Progress in Food Proteins-Biochemistry, pp. 99–153. Hudson, B. J. F., Ed., Elsevier Applied Science, London.
   Google Scholar
• Ames, J. M. (2003). Nonenzymatic browning. In: Encyclopedia of Food Sciences and Nutrition, pp. 665–672. Caballero, B., Trugo, L. and Finglas, P., Eds., Academic Press, London.
   Google Scholar
• Araki, N., Higashi, T., Mori, T., Shibayama, R., Kawabe, Y., Kodama, T., Takahashi, K., Shichiri, M. and Horiuchi, S. (1995). Macrophage scavenger receptor mediates the endocytic uptake and degradation of advanced glycation end products of the Maillard reaction. Eur. J. Biochem. 230(2):408–415.
   PubMedGoogle Scholar
• Arena, S., Salzano, A. M., Renzone, G., D'Ambrosio, C. and Scaloni, A. (2014). Non-enzymatic glycation and glycoxidation protein products in foods and diseases: an interconnected, complex scenario fully open to innovative proteomic studies. Mass Spectrom. Rev. 33(1):49–77.
   PubMed Web of Science ®Google Scholar
• Arfat, M. Y., Jalaluddin, M., Ashraf, Z., Arif, M. and Khursheed, A. (2014). Fine characterization of glucosylated human IgG by biochemical andbiophysical methods. Int. J. Biol. Macromolecules. 69:408–415.
   PubMed Web of Science ®Google Scholar
• Ashkenas, J., Penman, M., Vasile, E., Acton, S., Freeman, M. and Krieger, M. (1993). Structures and high and low affinity ligand binding properties of murine type I and type II macrophage scavenger receptors. J. Lipid Res. 34(6):983–1000.
   PubMed Web of Science ®Google Scholar
• Ashraf, J. M., Shahab, U., Tabrez, S., Lee, E. J., Choi, l. and Ahmad, S. Quercetin as a finer substitute to aminoguanidine in the inhibition of glycation products. Int. J. Biol. Macromolecules. 77:188–192.
   PubMed Web of Science ®Google Scholar
• Autenrieth, S. E., Soldanova, I., Rösemann, R., Gunst, D., Zahir, N., Kracht, M., Ruckdeschel, K., Wagner, H., Borgmann, S. and Autenrieth, I. B. (2007). Yersinia enterocolitica YopP inhibits MAP kinase-mediated antigen uptake in dendritic cells. Cell Microbiol. 9(2):425–437.
   PubMed Web of Science ®Google Scholar
• Baker, J. R., Zyzak, D. V., Thorpe, S. R. and Baynes, J. W. (1994). Chemistry of the fructosamine assay: D-glucosone is the product of oxidation of Amadori compounds. Clin. Chem. 40(10):1950–1955.
   PubMed Web of Science ®Google Scholar
• Barlovic, D. P., Thomas, M. C. and Jandeleit-Dahm, K. (2010). Cardiovascular disease: What's all the AGE/RAGE about?. Cardiovasc Hematol Disord Drug Targets. 10(1):7–15.
   PubMedGoogle Scholar
• Barondes, S. H., Cooper, D. N., Gitt, M. A. and Leffler, H. (1994). Galectins. Structure and function of a large family of animal lectins. J. Biol. Chem. 269(33):20807–20810.
   PubMed Web of Science ®Google Scholar
• Barth, H., Schnober, E. K., Neumann-Haefelin, C., Thumann, C., Zeisel, M. B., Diepolder, H. M., Hu, Z., Liang, T. J., Blum, H. E., Thimme, R. and Lambotin, M. (2008). Scavenger receptor class B is required for hepatitis C virus uptake and cross-presentation by human dendritic cells. J. Virol. 82:3466–79.
   PubMed Web of Science ®Google Scholar
• Beal, M. F. (2002). Oxidatively modified proteins in aging and disease. Free Rad. Biol. Med. 32:797803. 106.
   Web of Science ®Google Scholar
• Berrens, L. (1996). Neoallergens in heated pecan nut: Products of Maillard-type degradation?. Allergy. 51(4):277–278.
   PubMed Web of Science ®Google Scholar
• Berrens, P. (1996). Neoallergens in heated pecan nut: Products of Maillard‐type degradation?. Allergy. 51(4):277–278.
   PubMed Web of Science ®Google Scholar
• Beyer, K., Morrow, E., Li, X. M., Bardina, L., Bannon, G. A., Burks, A. W. and Sampson, H. A. (2001). Effects of cooking methods on peanut allergenicity. J. Allergy Clin. Immunol. 107(6):1077–1081.
   PubMed Web of Science ®Google Scholar
• Biemel, K. M., Conrad, J. and Lederer, M. O. (2002a). Unexpected carbonyl mobility in aminoketoses: The key to major Maillard crosslinks. Angew Chem. Int. Ed Engl. 4:801–814.
   Web of Science ®Google Scholar
• Biemel, K. M., Friedl, D. A. and Lederer, M. O. (2002b). Identification and quantification of major Maillard cross-links in human serum albumin and lens protein. Evidence for glucosepane as the dominant compound. J. Biol. Chem. 277:24907–24915.
   PubMed Web of Science ®Google Scholar
• Biemel, K. M. and Lederer, M. O. (2003). Site-specific quantitative evaluation of the protein glycation product N6-(2,3-dihydroxy-5,6-dioxohexyl)-L-lysinate by LC-(ESI) MS peptide mapping: evidence for its key role in AGE formation. Bioconjug Chem. 14:619–628.
   PubMed Web of Science ®Google Scholar
• Bierhaus, A., Humpert, P. M., Morcos, M., Wendt, T., Chavakis, T., Arnold, B. et al. (2005). Understanding RAGE, the receptor for advanced glycation end products. J. Mol. Med. (Berl). 83(11):876–886.
   PubMed Web of Science ®Google Scholar
• Booth, A. A., Khalifah, R. G., Todd, P. and Hudson, B. G. (1997). In vitro kinetic studies of formation of antigenic advanced glycation end products (AGEs). Novel inhibition of post-Amadori glycation pathways. J. Biol. Chem. 272(9):5430–5437.
   PubMed Web of Science ®Google Scholar
• Bublin, M. and Breiteneder, H. (2014). Cross-reactivity of peanut allergens. Curr. Allergy Asthma Rep. 14(4):426.
   PubMed Web of Science ®Google Scholar
• Bucala, R., Makita, Z., Koschinsky, T., Cerami, A. and Vlassara, H. (1993). Lipid advanced glycosylation: pathway for lipid oxidation in vivo. Proc. Natl. Acad. Sci. USA. 90:6434.
   PubMed Web of Science ®Google Scholar
• Bucciarelli, L. G., Ananthakrishnan, R., Hwang, Y. C. et al. (2008). RAGE and modulation of ischemic injury in the diabetic myocardium. Diabetes 57:1941–1951.
   PubMed Web of Science ®Google Scholar
• Buckley, S. and Ehrhardt, C. (2010). The receptor for advanced glycation end products (RAGE) and the lung. J. Biomed. Biotechnol. Article ID 917108.
   PubMedGoogle Scholar
• Bunn, H. F. and Higgins, P. J. (1981). Reaction of monosaccharides with proteins: possible evolutionary significance. Science 213(4504):222–224.
   PubMed Web of Science ®Google Scholar
• Burgdorf, S., Lukacs-Kornek, V. and Kurts, C. (2006). The mannose receptor mediates uptake of soluble but not of cell-associated antigen for cross-presentation. J. Immunol. 176(11):6770–6776.
   PubMed Web of Science ®Google Scholar
• Burks, A. W., Williams, L. W., Connaughton, C., Cockrell, G. O., Brien, T. J. and Helm, R. M. (1992). Identification and characterization of asecond major peanut allergen, Ara h II, with use of the sera ofpatients with atopic dermatitis and positive peanut challenge. J. Allergy Clin. Immunol. 90:962–969.
   PubMed Web of Science ®Google Scholar
• Cai, W., He, J. C., Zhu, L., Chen, X., Striker, G. E. and Vlassara, H. (2008). AGE-receptor-1Counteracts cellular oxidantstress induced by AGEs vianegative regulation of p66shc-dependent FKHRL1 phosphorylation. Am. J. Physiol. Cell. Physiol. 294:C145–C152.
   PubMed Web of Science ®Google Scholar
• Calvano, C. D., Monopoli, A., Loizzo, P., Faccia, M. and Zambonin, C. (2013). Proteomic approach based on MALDI-TOF MS to detect powdered milk in fresh cow's milk. J. Agric. Food Chem. 61:1609.
   PubMed Web of Science ®Google Scholar
• Cataldegirmen, G., Zeng, S., Feirt, N., Ippagunta, N., Dun, H., Qu, W., Lu, Y., Rong, L. L., Hofmann, M. A., Kislinger, T. and Pachydaki, S. I. (2005). RAGE limits regeneration after massive liver injury by coordinated suppression of TNF-alpha and NF-kappaB. J. Exp. Med. 201:473–484.
   PubMed Web of Science ®Google Scholar
• Chavakis, T., Bierhaus, A., Al-Fakhri, N., Schneider, D., Witte, S., Linn, T. and Nawroth, P. P. (2003). The pattern recognition receptor (RAGE) Is a counterreceptor for leukocyte integrins a novel pathway for inflammatory cell recruitment. J. Exp. Med. 198(10):1507–1515.
   PubMed Web of Science ®Google Scholar
• Chayaratanasin, P., Barbieri, M. A., Suanpairintr, N. and Adisakwattana, S. (2015). Inhibitory effect of Clitoria ternatea flower petal extract on fructose-induced protein glycation and oxidation-dependent damages to albumin in vitro. BMC Complement Altern Med. 18:15–27.
   Google Scholar
• Choi, Y. G. and Lim, S. (2009). Characterization of anti-advanced glycation end product antibodies to nonenzymatically lysine-derived and arginine-derived glycated products. J. Immunoassay Immunochem. 30(4):386–399.
   PubMed Web of Science ®Google Scholar
• Codina, R., Oehling, A. G. Jr and Lockey, R. F. (1998). Neoallergens in heated soybean hull. Int. Arch. Allergy Immunol. 117(2):120–125.
   PubMed Web of Science ®Google Scholar
• Cortizo, A. M., Lettieri, M. G., Barrio, D. A., Mercer, N., Etcheverry, S. B. and McCarthy, A. D. (2003). Advanced glycation end-products (AGEs) induce concerted changes in the osteoblastic expression of their receptor RAGE and in the activation of extracellular signal-regulated kinases (ERK). Mol. Cell. Biochem. 250(1–2):1–10.
   PubMed Web of Science ®Google Scholar
• Corzo-Martínez, M., Moreno, F. J., Olano, A. and Villamiel, M. (2010). Role of pyridoxamine in the formation of the Amadori/Heyns compounds and aggregates during the glycation of beta-lactoglobulin with galactose and tagatose. J. Agric. Food Chem. 58(1):500–506.
   PubMed Web of Science ®Google Scholar
• Cuadrado, C., Cabanillas, B., Pedrosa, M. M., Varela, A., Guillamón, E., Muzquiz, M., Crespo, J. F., Rodriguez, J. and Burbano, C. (2009). Influence of thermal processing on IgE reactivity to lentil and chickpea proteins. Mol. Nutr. Food Res. 53(11):1462–1468.
   PubMed Web of Science ®Google Scholar
• Cucu, T., De Meulenaer, B. and Devreese, B. (2012). MALDI-based identification of stable hazelnut protein derived tryptic marker peptides. Food Addit. Contam. Part A Chem. Anal. Control Expo Risk Assess. 29(12):1821–1831.
   PubMed Web of Science ®Google Scholar
• David, A. A. (1987). Fructosamine: structure, analysis, and clinical usefulness. Clin. Chem. 33(12):2153–2163.
   PubMed Web of Science ®Google Scholar
• Davis, P. J., Smales, C. M. and James, D. C. (2001). How can thermal processing modify the antigenicity of proteins?. Allergy. 67:56–60.
   Google Scholar
• Davis, P. J. and Williams, S. C. (1998). Protein modification by thermal processing. Allergy. 53:102–105.
   PubMed Web of Science ®Google Scholar
• De Jongh, H. H., Robles, C. L., Timmerman, E., Nordlee, J. A., Lee, P. W., Baumert, J. L., Hamilton, R. G., Taylor, S. L. and Koppelman, S. J. (2013). Digestibility and IgE-binding of glycosylated codfish parvalbumin. Biomed. Res. Int. 2013:756789.
   PubMedGoogle Scholar
• del Castillo, M. D., Sanz, M. L., Vicente-Arana, M. J. and Corzo, N. (2002). Study of 2-furoylmethyl amino acids in processed foods by HPLC–mass spectrometry. Food Chem. 79(2):261–266.
   Web of Science ®Google Scholar
• Del Val, G., Yee, B. C., Lozano, R. M., Buchanan, B. B., Ermel, R. W., Lee, Y. M. and Frick, O. L. (1999). Thioredoxin treatment increases digestibility and lowers allergenicity of milk. J. Allergy Clin. Immunol. 103(4):690–697.
   PubMed Web of Science ®Google Scholar
• Demling, N., Ehrhardt, C., Kasper, M., Laue, M., Knels, L. and Rieber, E. (2006). Promotion of cell adherence and spreading: a novel function of RAGE, the highly selective differentiation marker of human alveolar epithelial type I cells. Cell Tissue Res. 323:475–488.
   PubMed Web of Science ®Google Scholar
• Dumic, J., Dabelic, S. and Flogel, M. (2006). Galectin-3: An open-ended story. Biochim. Biophys. Acta 1760:616–635.
   PubMed Web of Science ®Google Scholar
• Ehn, B. M., Ekstrand, B., Bengtsson, U. and Ahlstedt, S. (2004). Modification of IgE binding during heat processing of the cow's milk allergen β-lactoglobulin. J. Agric. Food Chem. 52:1398–1403.
   PubMed Web of Science ®Google Scholar
• Emara, M., Royer, P. J., Abbas, Z., Sewell, H. F., Mohamed, G. G., Singh, S. and Ghaemmaghami, A. M. (2011). Recognition of the major cat allergen Fel d 1 through the cysteine-rich domain of the mannose receptor determines its allergenicity. J. Biol. Chem. 286(15):13033–13040.
   PubMed Web of Science ®Google Scholar
• Erbersdobler, H. F. and Somoza, V. (2007). Forty years of furosine—Forty years of using Maillard reaction products as indicators of the nutritional quality of foods. Mol. Nutr. Food Res. 51:423–430.
   PubMed Web of Science ®Google Scholar
• Ezekowitz, R. A., Sastry, K., Bailly, P. and Warner, A. (1990). Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells. J. Exp. Med. 172:1785–1794.
   PubMed Web of Science ®Google Scholar
• Faigerc, R., Lappalainenc, J., Schneider, W. J., Kovanen, P. and Levi-Schaffer, F. (2012). Allergic models of inflammation: 28 potential role of scavenger receptors in human mast cell cytokine response to oxidized ldl. The World Allergy Organ. J. 5(Suppl 2):S27.
   Google Scholar
• Figdor, C. G., Van Kooyk, Y. and Adema, G. Y. (2002). C-type lectin receptors on dendritic cells and Langerhans cells. Nat. Rev. Immunol. 2:77–84.
   PubMed Web of Science ®Google Scholar
• Fioravanti, J., Medina-Echeverz, J. and Berraondo, P. (2011). Scavenger receptor class B, type I: A promising immunotherapy target. Immunotherapy 3:395–406.
   PubMed Web of Science ®Google Scholar
• Fountain, C. W., Requena, J. R., Jenkins, A. J., Lions, T. J., Smith, B., Baynes, J. W. and Thorpe, S. R. (1999). Quantification of N-(glucitol)ethanolamine and N-(carboxymethyl)serine: Two products of nonenzymatic modification of aminophospholipids formed in vivo. Anal. Biochem. 272:48.
   PubMed Web of Science ®Google Scholar
• Gary, E. M. and Min, K. C. (1982). Nonenzymatic glycosylation of proteins structure and function changes. Diabetes 31(Supplement_3).
   Google Scholar
• Goh, K. C., Lim, Y. P., Ong, S. H., Siak, C. B., Cao, X., Tan, Y. H. and Guy, G. R. (1996). Identification of p90, aprominenttyrosine-phosphorylatedproteinin fibroblast growth factor-stimulatedcells, as80K-H. J. Biol. Chem. 271:5832–5838.
   PubMed Web of Science ®Google Scholar
• Gough, P. J., Greaves, D. R. and Gordon, S. (1998). A naturally occurring isoform of the human macrophage scavenger receptor (SR-A) gene generated by alternative splicing blocks modified LDL uptake. J. Lipid. Res. 39(3):531–543.
   PubMed Web of Science ®Google Scholar
• Greenfield, N. J. (2006). Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc. 1(6):2876–2890.
   PubMed Web of Science ®Google Scholar
• Greenwalt, D. E., Lipsky, R. H., Ockenhouse, C. F., Ikeda, H., Tandon, N. N. and Jamieson, G. A. (1992). Membrane glycoprotein CD36: A review of its roles in adherence, signal transduction, and transfusion medicine. Blood. 80(5):1105–1115.
   PubMed Web of Science ®Google Scholar
• Gruber, P., Becker, W. M. and Hofmann, T. (2005). Influence of the Maillard reaction on the allergenicity of rAra h 2, a recombinant major allergen from peanut (Arachis hypogaea), its major epitopes, and peanut agglutinin. J. Agric. Food Chem. 53:2289–2296.
   PubMed Web of Science ®Google Scholar
• Gruber, P., Vieths, S., Wangorsch, A., Nerkamp, J. and Hofmann, T. (2004). Maillard reaction and enzymatic browning affect the allergenicity of Pru av 1, the major allergen from cherry (Prunus avium). J. Agric. Food Chem. 52:4002–4007.
   PubMed Web of Science ®Google Scholar
• Guanhao, B., Zhu, T., Chen, F., Zhang, N., Liu, K., Zhang, L. and Yang, H. (2015). Effects of saccharide on the structure and antigenicity of β-conglycinin in soybean protein isolate by glycation. Eur. Food Res. Technol. February. 240:285–293.
   Web of Science ®Google Scholar
• Halford, N. G., Muttucumaru, N., Powers, S. J., Gillatt, P. N., Hartley, L., Elmore, J. S. and Mottram, D. S. (2012). Concentrations of free amino acids and sugars in nine potato varieties: effects of storage and relationship with acrylamide formation. J. Agric. Food Chem. 60(48):12044–12055.
   PubMed Web of Science ®Google Scholar
• Hansen, K. S., Ballmer-Weber, B. K., Luttkopf, D., Wuthrich, B., Bindslev-Jensen, C., Vieths, S. and Poulsen, L. K. (2003). Roasted hazelnutsallergenic activity evaluated by double-blind placebo-controlled food challenge. Allergy. 58:132–138.
   PubMed Web of Science ®Google Scholar
• Harris, N., Super, M., Rits, M., Chang, G. and Ezekowitz, R. A. (1992). Characterization of the murine macrophage mannose receptor: demonstration that the down-regulation of receptor expression mediated by interferon- occurs at the level of transcription. Blood. 80:2363–2373.
   PubMed Web of Science ®Google Scholar
• Hebling, C. M., McFarland, M. A., Callahan, J. H. and Ross, M. M. (2013). Global proteomic screening of protein allergens and advanced glycation endproducts in thermally processed peanuts. J. Agric. Food Chem. 19; 61(24):5638–5648.
   PubMed Web of Science ®Google Scholar
• Heilmann, M., Wellner, A., Gadermaier, G., Ilchmann, A., Briza, P., Krause, M. and Henle, T. (2014). Ovalbumin modified with pyrraline, a Maillard reaction product, shows enhanced T-cell immunogenicity. J. Biol. Chem. 289(11):7919–7928.
   PubMed Web of Science ®Google Scholar
• Henle, T. (2005). Protein-bound advanced glycation endproducts (AGEs) as bioactive amino acid derivatives in foods. Amino. Acids. 29:313–322.
   PubMed Web of Science ®Google Scholar
• Herberth, G., Daegelmann, C., Röder, S., Behrendt, H., Krämer, U., Borte, M., Heinrich, J., Herbarth, O. and Lehmann, I. (2010). IL-17E but not IL-17A is associated with allergic sensitization: Results from the LISA study. Pediatr Allergy Immunol. 21:1086–1090.
   PubMed Web of Science ®Google Scholar
• Hilmenyuk, T., Bellinghausen, I., Heydenreich, B., Ilchmann, A., Toda, M., Grabbe, S. and Saloga, J. (2010). Effects of glycation of the model food allergen ovalbumin on antigen uptake and presentation by human dendritic cells. Immunology. 3:437–445.
   Web of Science ®Google Scholar
• Hirai, M. and Shimizu, N. (1990). Purification of two distinct proteins of approximate Mr 80,000 from human epithelial cells and identification as proper substrates for protein kinase C. Biochem. J. 270:583–589.
   PubMed Web of Science ®Google Scholar
• Ho, M. K. and Springer, T. A. (1982). Mac-2, a novel 32,000 Mr mouse macrophage subpopulationspecific antigen defined by monoclonal antibodies. J. Immunol. 128:1221–1228.
   PubMed Web of Science ®Google Scholar
• Hofmann, M. A., Drury, S., Fu, C., Qu, W., Taguchi, A., Lu, Y., Avila, C., Kambham, N., Bierhaus, A., Nawroth, P. and Neurath, M. F. (1999). RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides. Cell 97(7):889–901.
   PubMed Web of Science ®Google Scholar
• Hofmann, T. (1998). Characterization of chemical structure of novel coloured Maillard reaction products from furan-2-carboxaldehyde and amino acids. J. Agric. Food Chem. 46:932–940.
   Web of Science ®Google Scholar
• Horvai, A., Palinski, W., Wu, H., Moulton, K. S., Kalla, K. and Glass, C. K. (1995). Scavenger receptor, a gene regulatory elements target gene expression to macrophages and to foam cells of atherosclerotic lesions. Proc. Natl. Acad. Sci. USA. 92(12):5391–5395.
   PubMed Web of Science ®Google Scholar
• Hsu, H. Y., Chiu, S. L., Wen, M. H., Chen, K. Y. and Hua, K. F. (2001). Ligands of macrophage scavenger receptor induce cytokine expression via differential modulation of protein kinase signaling pathways. J. Biol. Chem. 276(31):28719–28730. Epub 2001 Jun 4.
   PubMed Web of Science ®Google Scholar
• Hugh, A. S. (2003). Anaphylaxis and emergency treatment. Pediatrics. 111:6.
   PubMed Web of Science ®Google Scholar
• Hughes, D. A., Fraser, I. P. and Gordon, S. (1995). Murine macrophage scavenger receptor: in vivo expression and function as receptor for macrophage adhesion in lymphoid and non-lymphoid organs. Eur. J. Immunol. 25(2):466–473.
   PubMed Web of Science ®Google Scholar
• Hunt, V. J., Bottoms, A. M. and Mitchinson, J. M. (1993). Oxidative alterations in the experimental glycation model of diabetes mellitus are due to protein-glucose adduct oxidation. Biochem. J. 291:529–535.
   PubMed Web of Science ®Google Scholar
• Huntington, J. A. and Stein, P. E. (2001). Structure and properties of Ovalbumin. J. Chromatography B. 756:189–198.
   PubMed Web of Science ®Google Scholar
• Ilchmann, A., Burgdorf, S., Scheurer, S., Waibler, Z., Nagai, R., Wellner, A., Yamamoto, Y., Yamamoto, H., Henle, T., Kurts, C. and Kalinke, U. (2010). Glycation of a food allergen by the Maillard reaction enhances its T-cell immunogenicity: role of macrophage scavenger receptor class A type I and II. J. Allergy Clin. Immunol. 125(1):175-83.e1-11.
   PubMed Web of Science ®Google Scholar
• Iwan, M., Vissers, Y. M., Fiedorowicz, E., Kostyra, H., Kostyra, E., Savelkoul, H. F. and Wichers, H. J. (2011). Impact of Maillard reaction on immunoreactivity and allergenicity of the hazelnut allergen Cor a 11. J. Agric. Food Chem. 59:7163–7171.
   PubMed Web of Science ®Google Scholar
• Jimenez, S. R., Belloque, J., Molina, E. and Lopez, F. R. (2011). Human immunoglobulin E (IgE) binding to heated and glycated ovalbumin and ovomucoid before and after in vitro digestion. J. Agric. Food Chem. 59:10044–10051.
   PubMed Web of Science ®Google Scholar
• Joe, A. and Vinson, B. (1996). Inhibition of protein glycation and advanced glycation end products by ascorbic acid and other vitamins and nutrients. J. Nutr. Biochem. 7:659–663.
   Web of Science ®Google Scholar
• Jung, H. A., Yoon, N. Y., Kang, S. S., Kim, Y. S. and Choi, J. S. (2008). Inhibitory activities of prenylated flavonoids from Sophora flavescens against aldose reductase and generation of advanced glycation endproducts. J. Pharm. Pharmacol. 60(9):1227–1236.
   PubMed Web of Science ®Google Scholar
• Kanai, M., Göke, M., Tsunekawa, S. and Podolsky, D. K. (1997). Signal transduction pathway of human fibroblast growthfactorreceptor3.Identification ofanovel66- kDa phosphoprotein. J. Biol. Chem. 272:6621–6628.
   PubMed Web of Science ®Google Scholar
• Kanjarawi, R., Dercamp, C., Etchart, N., Adel-Patient, K., Nicolas, J. F., Dubois, B. and Kaiserlian, D. (2011). Regulatory T cells control type I food allergy to beta-lactoglobulin in mice. Int. Arch. Allergy Immunol. 156:387–396.
   PubMed Web of Science ®Google Scholar
• Kislinger, T., Humeny, A., Peich, C. C., Becker, C. M. and Pischetsrieder, M. (2005). Analysis of protein glycation products by MALDI-TOF/MS. Ann N Y Acad Sci. 1043:249–259.
   PubMed Web of Science ®Google Scholar
• Kremer, K. N., Kumar, A. and Hedin, K. E. (2007). Haplotype-independent costimulation of IL-10 secretion by SDF-1/CXCL12 proceeds via AP-1 binding to the human IL-10 promoter. J. Immunol. 178(3):1581–1588.
   PubMed Web of Science ®Google Scholar
• Kroghsbo, S., Rigby, N. M., Johnson, P. E., Adel-Patient, K., Bøgh, K. L., Salt, L. J., Mills, E. C. and Madsen, C. B. (2014). Assessment of the sensitizing potential of processed peanut proteins in Brown Norway rats: roasting does not enhance allergenicity. PLoS One. 7, 9(5):e96475. doi: 10.131471/journal.pone.0096475.
   PubMed Web of Science ®Google Scholar
• Kumar, S., Verma, A. K., Das, M. and Dwivedi, P. D. (2012). Molecular mechanisms of IgE mediated food allergy. Int. Immunopharmacology 13:432–439.
   PubMed Web of Science ®Google Scholar
• Kyte, J. and Doolittle, R. F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157(1):105–132.
   PubMed Web of Science ®Google Scholar
• Kzhyshkowska, J., Neyen, C. and Gordon, S. (2012). Role of macrophage scavenger receptors in atherosclerosis. Immunobiology. 217(5):492–502.
   PubMed Web of Science ®Google Scholar
• Largent, B. L., Walton, K. M., Hoppe, C. A., Lee, Y. C. and Schnaar, R. L. (1984). Carbohydrate-specific adhesion of alveolar macrophages to mannose-derivatized surfaces. J. Biol. Chem. 259:1764–1769.
   PubMed Web of Science ®Google Scholar
• Led, F. and Schleicher, E. (1990). New aspects of the Maillard reaction in foods and in the human-body. Angew Chem. Int. Ed. 29:565–594.
   Web of Science ®Google Scholar
• Leduc, V., Moneret, V. D. A., Guerin, L., Morisset, M. and Kanny, G. (2003). Anaphylaxis to wheat isolates: immunochemical study of a case proved by means of double-blind, placebo-controlled food challenge. J. Allergy Clin. Immunol. 111(4):897–899.
   PubMed Web of Science ®Google Scholar
• Lertsiri, S., Shiraishi, M. and Miyazawa, T. (1998). Identification of deoxy-Dfructosyl phosphatidylethanolamine as a non-enzymic glycation product of phosphatidylethanolamine and its occurrence in human blood plasma and red blood cells. Biosci. Biotechnol. Biochem. 62:893.
   PubMed Web of Science ®Google Scholar
• Li, H., Chehade, M., Liu, W., Xiong, H., Mayer, L. and Berin, M. C. (2007). Allergen-IgE complexes trigger CD23-dependent CCL20 release from human intestinal epithelial cells. Gastroenterology. 133:1905–1915.
   PubMed Web of Science ®Google Scholar
• Li, Y. M., Mitsuhashi, T., Wojciechowicz, D., Shimizu, N., Li, J., Stitt, A., He, C., Banerjee, D. and Vlassara, H. (1996). Molecular identity and cellular distribution of advanced glycation end product receptors:relationshipof p60toOST-48 and p90to80K- membrane proteins. Proc. Natl. Acad. Sci. USA. 93:11047–11052.
   Web of Science ®Google Scholar
• Lin, L., Park, S. and Lakatta, E. G. (2009). RAGE signaling in inflammation and arterial aging. Front Biosci. 14:1403–1413.
   PubMed Web of Science ®Google Scholar
• Lu, C., He, J. C., Cai, W., Liu, H., Zhu, L. and Vlassara, H. Advanced glycation end product (AGE) receptor1 is a negative regulator of the inflammatory response to AGE in mesangialcells. Proc. Natl. Acad. Sci. USA. 101:11767–11772.
   PubMed Web of Science ®Google Scholar
• Ma, X. J., Gao, J. Y. and Chen, H. B. (2013). Combined effect of glycation and sodium carbonate-bicarbonate buffer concentration on IgG binding, IgE binding and conformation of ovalbumin. J. Sci. Food Agric. 93(13):3209–3215.
   PubMed Web of Science ®Google Scholar
• Malanin, K., Lundberg, M. and Johansson, S. G. (1995). Anaphylactic reaction caused by neoallergens in heated pecan nut. Allergy. 50(12):988–991.
   PubMed Web of Science ®Google Scholar
• Maleki, S. J., Chung, S. Y., Champagne, E. T. and Raufman, J. P. (2000). The effects of roasting on the allergenic properties of peanut proteins. J. Allergy Clin. Immunol. 106(4):763–768.
   PubMed Web of Science ®Google Scholar
• Malgorzata, T., Jansen, A. P. H., Roovers, M. H. W. M., Ruinemans-Koerts, J., Wichers, H. J. and Savelkoul, H. F. J. (2015). Maillard-type neoallergens present in processed soy extract may cause an allergic reaction in soy allergic patients. Clin. Translational Allergy. 5(3):P21.
   PubMed Web of Science ®Google Scholar
• Martínez-Flórez, S., González-Gallego, J., Culebras, J. M. and Tuñón, M. J. Flavonoids: Properties and anti-oxidizing action. Nutr Hosp. 17(6):271–278.
   PubMedGoogle Scholar
• Martins, S. I., Marcelis, A. T. and Van, B. M. A. (2003). Kinetic modelling of Amadori N-(1-deoxy-D-fructos-1-yl)-glycine degradation pathways. Part I—Reaction mechanism. Carbohydr Res. 338:1651–1663.
   PubMed Web of Science ®Google Scholar
• Matsumoto, A., Naito, M., Itakura, H., Ikemoto, S., Asaoka, H., Hayakawa, I., Kanamori, H., Aburatani, H., Takaku, F. and Suzuki, H. (1990). Human macrophage scavenger receptors: primary structure, expression, and localization in atherosclerotic lesions. Proc. Natl. Acad. Sci. USA. 87(23):9133–9137.
   PubMed Web of Science ®Google Scholar
• Mills, E. N. C., Sancho, A. I., Rigby, N. M., Jenkins, J. A. and Mackie, A. R. (2009). Impact of food processing on the structure and allergenic properties of food allergens. Mol. Nutr. Res. 53:963–969.
   PubMed Web of Science ®Google Scholar
• Miyata, T., Hori, O., Zhang, J., Yan, S. D., Ferran, L., Iida, Y. and Schmidt, A. M. (1996). The receptor for advanced glycation end products (RAGE) is a central mediator of the interaction of AGE-beta2microglobulin with human mononuclear phagocytes via an oxidant-sensitive pathway. Implications for the pathogenesis of dialysis-related amyloidosis. J. Clin. Invest. 98(5):1088–1094.
   PubMed Web of Science ®Google Scholar
• Miyazaki, A., Nakayama, H. and Horiuchi, S. (2002). Scavenger receptors that recognize advanced glycation end products. Trends Cardiovasc Med. 12(6):258–262.
   PubMed Web of Science ®Google Scholar
• Moreaux, V. and Birlouez-Aragon, I. (1997). Degradation of tryptophan in heated β-lactoglobulin-lactose mixtures is associated with intense Maillard reaction. J. Agric. Food Chem. 45(5):1905–1910.
   Web of Science ®Google Scholar
• Morelli, A. E., Larregina, A. T., Shufesky, W. J., Sullivan, M. L., Stolz, D. B., Papworth, G. D., Zahorchak, A. F., Logar, A. J., Wang, Z., Watkins, S. C. and Falo, L. D. (2004). Endocytosis, intracellular sorting, and processing of exosomes by dendritic cells. Blood. 104(10):3257–3266.
   PubMed Web of Science ®Google Scholar
• Mueller, G. A., Maleki, S. J., Johnson, K., Hurlburt, B. K., Cheng, H., Ruan, S., Nesbit, J. B., Pomés, A., Edwards, L. L., Schorzman, A. and Deterding, L. J. (2013). Identification of Maillard reaction products on peanut allergens that influence binding to the receptor for advanced glycation end products. Allergy. 68(12):1546–1554.
   PubMed Web of Science ®Google Scholar
• Murphy, J. E., Tedbury, P. R., Homer-Vanniasinkam, S., Walker, J. H. and Ponnambalam, S. (2005). Biochemistry and cell biology of mammalian scavenger receptors. Atherosclerosis. 182(1):1–15.
   PubMed Web of Science ®Google Scholar
• Muttucumaru, N., Powers, S., Elmore, J., Briddon, A., Mottram, D. and Halford, N. (2014). Evidence for the complex relationship between free amino acid and sugar concentrations and acrylamide-forming potential in potato. Ann. Appl. Biol. Jan; 164(2):286–300.
   PubMed Web of Science ®Google Scholar
• Nadeem, A., Ansari, M. and Rashid, A. (2011). Glycated lysine residues: a marker for non-enzymatic protein glycation in age-related diseases. Disease Markers 30:317–324.
   PubMed Web of Science ®Google Scholar
• Nagai, R., Matsumoto, K., Ling, X., Suzuki, H., Araki, T., Horiuchi, S. (2000). Glycolaldehyde, a reactive intermediate for advanced glycation end products, plays an important role in the generation of an active ligand for the macrophage scavenger receptor. Diabetes. 49(10):1714–1723.
   PubMed Web of Science ®Google Scholar
• Nagamatsu, K., Komori, M., Kuroda, S. and Tanaka, K. (1992). Dynamic light scattering studies on hydrodynamic properties of fibrinogen-fibronectin complex. J. Biomol. Struct. Dyn. 9(4):807–820.
   PubMed Web of Science ®Google Scholar
• Naila, R. and Paul, J. T. (2012). Glycation research in amino acids: a place to call home. 42(4):1087–1096.
   Google Scholar
• Nakamura, A., Sasaki, F., Watanabe, K., Ojima, T., Ahn, D. H. and Saeki, H. (2006). Changes in allergenicity and digestibility of squid tropomyosin during the Maillard reaction with ribose. J. Agric. Food Chem. 54:9529–9534.
   PubMed Web of Science ®Google Scholar
• Nakamura, A., Watanabe, K., Ojima, T., Ahn, D. H. and Saeki, H. (2005). Effect of maillard reaction on allergenicity of scallop tropomyosin. J. Agric. Food Chem. 53(19):7559–7564.
   PubMed Web of Science ®Google Scholar
• Nakamura, S., Suzuki, Y., Ishikawa, E., Yakushi, T., Jing, H. and Miyamoto, T. and Hashizume, K. (2008). Reduction of in vitro allergenicity of buckwheat Fag e 1 through the Maillard-type glycosylation with polysaccharides. Food Chem. 109:538–545.
   Web of Science ®Google Scholar
• Neeper, M., Schmidt, A. M., Brett, J., Yan, S. D., Wang, F., Pan, Y. C. E., Elliston, K., Stern, D. and Shaw, A. (1992). Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins. J. Biol. Chem. 267:14998–15004.
   PubMed Web of Science ®Google Scholar
• Nemet, I., Strauch, C. M. and Monnier, V. M. (2011). Favored and disfavored pathways of protein crosslinking by glucose: glucose lysine dimer (GLUCOLD) and crossline versus glucosepane. Amino Acids. 40:167–181.
   PubMed Web of Science ®Google Scholar
• Neyen, C., Plüddemann, A., Mukhopadhyay, S., Maniati, E., Bossard, M., Gordon, S. and Hagemann, T. (2013). Macrophage scavenger receptor a promotes tumor progression in murine models of ovarian and pancreatic cancer. J. Immunol. 190(7):3798–805.
   PubMed Web of Science ®Google Scholar
• Nicoletti, A., Caligiuri, G., Törnberg, I., Kodama, T., Stemme, S. and Hansson, G. K. (1999). The macrophage scavenger receptor type a directs modified proteins to antigen presentation. Eur. J. Immunol. 29(2):512–521.
   PubMed Web of Science ®Google Scholar
• Norikazu, F., Mitsutoshi, H., Hashimotoa, H. and Fumio, O. (1992). Solubilization of a lipophilic compound in highly concentrated saccharide solutions containing protein. Biosci. Biotech. Biochem. 56(1):118–121.
   Web of Science ®Google Scholar
• Oczypok, E. A., Milutinovic, P. S., Alcorn, J. F., Khare, A., Crum, L. T., Manni, M. L., Epperly, M. W., Pawluk, A. M., Ray, A. and Oury, T. D. (2015). Epperly MW4, Pawluk AM1, Ray A3, Oury TD5. Pulmonary receptor for advanced glycation end-products promotes asthma pathogenesis through IL-33 and accumulation of group 2 innate lymphoid cells. J. Allergy Clin. Immunol. 6749(15):00409–00411.
   Google Scholar
• Ohgami, N., Nagai, R., Ikemoto, M., Arai, H., Kuniyasu, A., Horiuchi, S. and Nakayama, H. (2001b). CD36, a member of the class b scavenger receptor family, as a receptor for advanced glycation end products. J. Biol. Chem. 276:3195–202.
   PubMed Web of Science ®Google Scholar
• Ohgami, N., Nagai, R., Miyazaki, A, Ikemoto, M., Arai, H., Horiuchi, S. and Nakayama, H. (2001a). Scavenger receptor class B type I-mediated reverse cholesterol transport is inhibited by advanced glycation end products. J. Biol. Chem. 276:13348–13355.
   PubMed Web of Science ®Google Scholar
• Panel, N. S. E. (2010). Guidelines for the diagnosis and management of food allergy in the United States: report of the NIAID-sponsored expert panel. J. Allergy Clin. Immunol. 126:S1–58.
   PubMed Web of Science ®Google Scholar
• Pamplona, R., Bellmunt, M. J., Portero, M., Riba, D. and Prat, J. (1995). Chromatographic evidence for Amadori product formation in rat liver aminophospholipids. Life Sci. 57:873.
   PubMed Web of Science ®Google Scholar
• Pamplona, R., Requena, J. R., Portero-Otin, M., Prat, J., Thorpe, S. R. and Bellmunt, M. J. (1998). Carboxymethylated phosphatidylethanolamine in mitochondrial membranes of mammals–Evidence for intracellular lipid glycoxidation. Eur. J. Biochem. 255:685.
   PubMedGoogle Scholar
• Pastorello, E. A., Pravettoni, V., Calamari, A. M., Banfi, E. and Robino, A. M. (2002). New plant-origin food allergens. Allergy. 57(72):106–110.
   PubMed Web of Science ®Google Scholar
• Plüddemann, A., Neyen, C. and Gordon, S. (2007). Macrophage scavenger receptors and host-derived ligands. Methods. 43:207–217.
   PubMed Web of Science ®Google Scholar
• Plundrich, N. J., Kulis, M., White, B. L., Grace, M. H., Guo, R., Burks, A. W., Davis, J. P. and Lila, M. A. (2014). Novel strategy to create hypoallergenic peanut protein-polyphenol edible matrices for oral immunotherapy. J. Agric. Food Chem. 62(29):7010–7021.
   PubMed Web of Science ®Google Scholar
• Puente, N., Daviet, L., Ninio, E. and McGregor, J. L. (1996). Identification on human CD36 of a domain (155–183) implicated in bi binding oxidized low-density lipoproteins (Ox-LDL). Arterioscler Thromb Vasc Biol. 16(8):1033–1039.
   PubMed Web of Science ®Google Scholar
• Rahmelow, K. and Hubner, W. (1996). Secondary structure determination of proteins in aqueous solution by infrared spectroscopy: A comparison of multivariate data analysis methods. Anal. Biochem. 241:5–13.
   PubMed Web of Science ®Google Scholar
• Rapin, J. R. and Wiernsperger, N. (2010). Possible links between intestinal permeablity and food processing: A potential therapeutic niche for glutamine. Clinics 65(6):635–643.
   PubMed Web of Science ®Google Scholar
• Ravandi, A., Kuksis, A., Marai, L. and Myher, J. J. (1995). Preparation and characterization of glucosylated aminoglycerophospholipids. Lipids 30:885.
   PubMed Web of Science ®Google Scholar
• Ravandi, A., Kuksis, A., Marai, L., Myher, J. J., Steiner, G., Lewisa, G. and Kamido, H. (1996). Isolation and identification of glycated aminophospholipids from red cells and plasma of diabetic blood. FEBS Lett. 381:77.
   PubMed Web of Science ®Google Scholar
• Rebecca, P., Dearlove, P. G., Diane, K., Hartle, R. B., Swanson, J. L. and Hargrove,   (2008). Inhibition of protein glycation by extracts of culinary herbs and spices. J. Med. Food. 11(2):275–281.
   PubMed Web of Science ®Google Scholar
• Robert, M. C. and David, B. S. (2012). Comparing multiple measures of glycemia: how to transition from biomarker to diagnostic test?. Clin. Chem. 58(12):1615–1617.
   PubMed Web of Science ®Google Scholar
• Roger, N. J., Patricia, A. M. and John, R. B. (1983). Fructosamine: A new approach to the estimation of serum glycosylprotein. An index of diabetic control. Clin. Chim. Acta. 127:87–95.
   PubMed Web of Science ®Google Scholar
• Royer, P. J., Emara, M., Yang, C., Al-Ghouleh, A., Tighe, P., Jones, N. and Ghaemmaghami, A. M. (2010). The mannose receptor mediates the uptake of diverse native allergens by dendritic cells and determines allergen-induced T cell polarization through modulation of IDO activity. J. Immunology 185(3):1522–1531.
   PubMed Web of Science ®Google Scholar
• Rupa, P., Nakamura, S., Katayama, S. and Min, Y. (2014a). Effects of ovalbumin glycoconjugates on alleviation of orally induced egg allergy in mice via dendritic-cell maturation and T-cell activation. Mol. Nutr. Food Res. 58:405–417.
   PubMed Web of Science ®Google Scholar
• Rupa, P., Nakamura, S., Katayama, S. and Mine, Y. (2014b). Attenuation of allergic immune response phenotype by mannosylated egg white in orally induced allergy in BALB/c mice. J. Agric. Food Chem. 62(39):9479–9487.
   PubMed Web of Science ®Google Scholar
• Sancho, A. I., Rigby, N. M., Zuidmeer, L., Asero, R., Mistrello, G., Amato, S., González-Mancebo, E., Fernández-Rivas, M., Ree, R. and Mills, E. N. C. (2005). The effect of thermal processing on the IgE reactivity of the non-specific lipid transfer protein from apple, Mal d 3. Allergy 60:1262–1268.
   PubMed Web of Science ®Google Scholar
• Sathe, S. K. and Sharma, G. M. (2009). Effects of food processing on food allergens. Mol. Nutr. Food Res. 53(8):970–978.
   PubMed Web of Science ®Google Scholar
• Sathe, S. K., Teuber, S. S. and Roux, K. H. (2005). Effects of food processing on the stability of food allergens. Biotechnol. Adv. 23(6):423–429.
   PubMed Web of Science ®Google Scholar
• Sato, S. and Nieminen, J. (2004). Seeing strangers or announcing “danger”: Galectin-3 in two models of innate immunity. Glycoconj. J. 19:583–591.
   PubMed Web of Science ®Google Scholar
• Scheijen, J. L., Clevers, E., Engelen, L., Dagnelie, P. C., Brouns, F., Stehouwer, C. D. and Schalkwijk, C. G. (2016). Analysis of advanced glycation endproducts in selected food items by ultra-performance liquid chromatography tandem mass spectrometry: Presentation of a dietary AGE database. Food Chem. 190:1145–1150.
   PubMed Web of Science ®Google Scholar
• Schmidt, A. M., Hasu, M., Popov, D., Zhang, J. H., Chen, J., Yan, S. D., Brett, J., Cao, R., Kuwabara, K. and Costache, G. (1994). Receptor for advanced glycation end products (AGEs) has a central role in vessel wall interactions and gene activation in response to circulating AGE proteins. Proc. Natl. Acad. Sci. USA. 91(19):8807–8811.
   PubMed Web of Science ®Google Scholar
• Schmidt, A. M., Vianna, M., Gerlach, M., Brett, J., Ryan, J., Kao, J., Esposito, C., Hegarty, H., Hurley, W., Clauss, M. (1992). Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung which are present on the endothelial cell surface. J. Biol. Chem. 267(21):14987–14997.
   PubMed Web of Science ®Google Scholar
• Schmidt, A. M., Yan, S. D., Yan, S. F. and Stern, D. M. (2001). The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses. J. Clin. Invest. 108(7):949–955.
   PubMed Web of Science ®Google Scholar
•  
   Google Scholar
• Seo, S. and Karboune, S. (2014). Investigation of the use of Maillard reaction inhibitors for the production of patatin–carbohydrate conjugates. J. Agric. Food Chem. 62(50):12235–12243.
   PubMed Web of Science ®Google Scholar
• Seo, S., L'Hocine, L. and Karboune, S. (2014). Allergenicity of potato proteins and of their conjugates with galactose, galactooligosaccharides, and galactan in native, heated, and digested forms. J. Agric. Food Chem. 62(16):3591–3598.
   PubMed Web of Science ®Google Scholar
• Shanmugam, N., Kim, Y. S., Lanting, L. and Natarajan, R. (2003). Regulation of cyclooxygenase-2 expression in monocytes by ligation of the receptor for advanced glycation end products. J. Biol. Chem. 278(37):34834–34844.
   PubMed Web of Science ®Google Scholar
• Shi, X. X., Ma, M. H., Wang, L. Y. and Huang, X. (2012). Effect of heat treatment on the allergenicity and microstructure of ovomucoid. Guang Pu Xue Yu Guang Pu Fen Xi. 32(9):2487–2491.
   PubMedGoogle Scholar
• Sick, E., Brehin, S., André, P., Coupin, G., Landry, Y., Takeda, K. and Gies, J. P. (2010). Advanced glycation end products (AGEs) activate mast cells. Br. J. Pharmacol. 161(2):442–455.
   PubMed Web of Science ®Google Scholar
• Siddiqui, A. A., Sohail, A., Bhat, S. A., Rehman, M. T. and Bano, B. (2015). Non-enzymatic glycation of almond cystatin leads to conformational changes and altered activity. Protein Pept Lett. 22(5):449–459.
   PubMed Web of Science ®Google Scholar
• Siemasko, K., Chong, A. S., Jäck, H. M., Gong, H., Williams, J. W. and Finnegan, A. (1998). Inhibition of JAK3 and STAT6 tyrosine phosphorylation by the immunosuppressive drug leflunomide leads to a block in IgG1 production. J. Immunol. 160(4):1581–1588.
   PubMed Web of Science ®Google Scholar
• Simona, A., Anna, M. S., Giovanni, R., Chiara, D. A. and Andrea, S. (2014). Non-enzymatic glycation and glycoxidation protein products in foods and diseases: An interconnected, complex scenario fully open to innovative proteomic studies. Mass Spectr. Rev. 33:49–77.
   PubMed Web of Science ®Google Scholar
• Simonato, B., Pasini, G., Giannattasio, M., Peruffo, A. D., De Lazzari, F. and Curioni, A. (2001). Food allergy to wheat products: the effect of bread baking and in vitro digestion on wheat allergenic proteins. A study with bread dough, crumb, and crust. J. Agric. Food Chem. 49:5668–5673.
   PubMed Web of Science ®Google Scholar
• Smith, A. M. and Chapman, M. D. (1996). Reduction in IgE binding to allergen variants generated by site-directed mutagenesis: contribution of disulfide bonds to the antigenic structure of the major house dust mite allergen Der p 2. Mol. Immunol. 33(4–5):399–405.
   PubMed Web of Science ®Google Scholar
• Sorci, G., Riuzzi, F., Arcuri, C., Giambanco, I. and Donato, R. (2004). Amphoterin stimulates myogenesis and counteracts the antimyogenic factors basic fibroblast growth factor and S100B via RAGE binding. Mol. Cell Biol. 11:4880–4894.
   Web of Science ®Google Scholar
• Spies, J. R. (1974). Allergens. J. Agric. Food Chem. 22:30–36.
   PubMed Web of Science ®Google Scholar
• Suzuki, H., Kurihara, Y., Takeya, M., Kamada, N. (1997). A role for macrophage scavenger receptors in atherosclerosis and susceptibility to infection. Nature. 386(6622):292–296.
   PubMed Web of Science ®Google Scholar
• Tagliani, E., Guermonprez, P., Sepúlveda, J., López-Bravo, M., Ardavín, C., Amigorena, S., Benvenuti, F. and Burrone, O. R. (2008). Selection of an antibody library identifies a pathway to induce immunity by targeting CD36 on steady-state CD8 alpha+ dendritic cells. J. Immunol. 180:3201–3209.
   PubMed Web of Science ®Google Scholar
• Taheri-Kafrani, A., Gaudin, J. C., Rabesona, H., Nioi, C., Agarwal, D., Drouet, M., Chobert, J. M., Bordbar, A. K. and Haertle, T. (2009). Effects of heating and glycation of beta-lactoglobulin on its recognition by IgE of sera from cow milk allergy patients. J. Agric. Food Chem. 57:4974–4982.
   PubMed Web of Science ®Google Scholar
• Tazawa, S., Katayama, S., Hirabayashi, M., Yamaguchi, D. and Nakamura, S. (2014). Improvement of surface functionalities, including allergenicity attenuation, of whole buckwheat protein fraction by maillard-type glycation with dextran. Prev. Nutr. Food Sci. 19:327–332.
   PubMedGoogle Scholar
• Teodorowicz, M., Fiedorowicz, E., Kostyra, H., Wichers, H. and Kostyra, E. (2013). Effect of Maillard reaction on biochemical properties of peanut 7S globulin (Ara h 1) and its interaction with a human colon cancer cell line (Caco-2). Eur. J. Nutr. 52(8):1927–1938.
   PubMed Web of Science ®Google Scholar
• Terpstra, V., Van, A. E. S., Van, V. A. G., Kuiper, J. and Van, B. T. J. (2000). Hepatic and extrahepatic scavenger receptors: function in relation to disease. Arterioscler Thromb. Vasc. Biol. 20(8):1860–1872.
   PubMed Web of Science ®Google Scholar
• Thornalley, P. J., Langborg, A. and Minhas, H. S. (1999). Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem. J. 344:109–116.
   PubMed Web of Science ®Google Scholar
• Toda, M., Heilmann, M., Ilchmann, A. and Vieths, S. (2014). The Maillard reaction and food allergies: Is there a link?. Clin. Chem. Lab Med. 52(1):61–67.
   PubMed Web of Science ®Google Scholar
• Tomokiyo, Ri., Jinnouchi, K., Honda, M., Wada, Y., Hanada, N., Hiraoka, T., Suzuki, H., Kodama, T., Takahashi, K. and Takeya, M. (2002). Production, characterization, and interspecies reactivities of monoclonal antibodies against human class A macrophage scavenger receptors. Atherosclerosis. 161(1):123–132.
   PubMed Web of Science ®Google Scholar
• Tuberoso, C. I., Kowalczyk, A., Coroneo, V., Russo, M. T., Dessì, S. and Cabras, P. (2005). Chemical composition and antioxidant, antimicrobial, and antifungal activities of the essential oil of Achillea ligustica all. J. Agric. Food Chem. 53(26):10148–10153.
   PubMed Web of Science ®Google Scholar
• Utzmann, C. M. and Lederer, M. O. (2000). Identification and quantification of aminophospholipid-linked maillard compounds in model systems and egg yolk products. J. Agric. Food Chem. 48:1000.
   PubMed Web of Science ®Google Scholar
• Valencia, J. V., Weldon, S. C., Quinn, D., Kiers, G. H., DeGroot, J., TeKoppele, J. M. and Hughes, T. E. (2004). Advanced glycation end product ligands for the receptor for advanced glycation end products: biochemical characterization and formation kinetics. Anal Biochem. 324(1):68–78.
   PubMed Web of Science ®Google Scholar
• Vanderhoof, J. A. (2008). Probiotics in allergy management. J. Pediatr. Gastroenterol Nutr. 47(Suppl 2):S38–S40.
   PubMedGoogle Scholar
• Verma, A. K., Kumar, S., Das, M and Dwivedi, P. D. (2012). A comprehensive review of legume allergy. Clin.Rev. Allerg Immunol. doi 10.1007/s12016-012-8310-6.
   Web of Science ®Google Scholar
• Verma, A. K., Kumar, S., Das, M. and Dwivedi, P. D. (2013). Impact of thermal processing on legume allergens. Plant Foods Hum. Nutr. 67:430–441.
   Web of Science ®Google Scholar
• Villaverde, A. and Estévez, M. (2013). Carbonylation of myofibrillar proteins through the Maillard pathway: effect of reducing sugars and reaction temperature. J. Agric. Food Chem. 61(12):3140–3147.
   PubMed Web of Science ®Google Scholar
• Vissers, Y. M., Blanc, F., Skov, P. S., Johnson, P. E., Rigby, N. M., Przybylski-Nicaise, L., Bernard, H., Wal, J. M., Ballmer-Weber, B., Zuidmeer-Jongejan, L. and Szepfalusi, Z. (2011). Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut. PLoS One. 6(8):e23998. doi: 10.1371/journal.pone.0023998.
   PubMed Web of Science ®Google Scholar
• Vlassara, H., Li, Y. M., Imani, F., Wojciechowicz, D., Yang, Z., Liu, F. T. and Cerami, A. (1995). Identification of galectin-3 as a high-affinity binding protein for advanced glycation end products (AGE): A new member of the AGE-receptor complex. Mol. Med. 1(6):634–646.
   PubMed Web of Science ®Google Scholar
• Wells, K. K. J., Zyzak, D. V., Litchfield, J. E., Thorpe, S. R. and Baynes, J. W. (1995). Mechanism of autoxidative glycosylation: identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose. Biochemistry. 34:3702–3709.
   PubMed Web of Science ®Google Scholar
• Whitmore, L. and Wallace, B. A. (2008). Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers. 89(5):392–400.
   PubMed Web of Science ®Google Scholar
• Yamagishi, S., Ueda, S. and Okuda, S. (2007). Food-derived advanced glycation end products (AGEs): a novel therapeutic target for various disorders. Curr. Pharm. Des. 13(27):2832–2836.
   PubMed Web of Science ®Google Scholar
• Yang, Z. H., Li, C., Li, Y. Y. and Wang, Z. H. (2013). Effects of Maillard reaction on allergenicity of buckwheat allergen Fag t 3 during thermal processing. J. Sci. Food Agric. 93:1510–1515.
   PubMed Web of Science ®Google Scholar
• Yanga, S. Y., Kima, S. W., Kimb, Y., Leeb, S. H., Jeonb, C. H. and Lee, K. W. (2015). Optimization of Maillard reaction with ribose for enhancing anti-allergy effect of fish protein hydrolysates using response surface methodology. Food Chem. 176:420–425.
   PubMed Web of Science ®Google Scholar
• Yin, J., Hedegaard, R. V., Skibsted, L. H. and Andersen, M. L. (2014). Epicatechin and epigallocatechin gallate inhibit formation of intermediary radicals during heating of lysine and glucose. Food Chem. 146:48–55.
   PubMed Web of Science ®Google Scholar
• Yin, S. W., Tang, C. H., Wen, Q. B., Yang, X. Q. and Li, L. (2008). Functional properties and in vitro trypsin digestibility of red kidney bean (Phaseolus vulgaris L.) protein isolate: Effect of high-pressure treatment. Food Chem. 110(4):938–45.
   PubMed Web of Science ®Google Scholar
• Yonekura, H., Yamamoto, Y., Sakurai, S., Petrova, R. G., Abedin, M. J., Yasui, K., Takeuchi, M., Makita, Z., Takasawa, S. and Okamoto, H. (2003). Novel splice variants of the receptor for advanced glycation end-products expressed in human vascular endothelial cells and pericytes, and their putative roles in diabetes-induced vascular injury. Biochem J. 370(Pt 3):1097–10109.
   PubMed Web of Science ®Google Scholar
• Zeng, J. and Davies, M. J. (2005). Evidence for the formation of adducts and S-(carboxymethyl) cysteine on reaction of alpha-dicarbonyl compounds with thiol groups on amino acids, peptides, and proteins. Chem. Res. Toxicol. 18(8):1232–1241.
   PubMed Web of Science ®Google Scholar
• Zhang, G., Huang, G., Xiao, L. and Mitchell, A. E. (2011). Determination of advanced glycation endproducts by LC-MS/MS in raw and roasted almonds (Prunus dulcis). J. Agric. Food Chem. 59(22):12037–12046.
   PubMed Web of Science ®Google Scholar
• Zhang, M., Xu, W. and Deng, Y. (2013). A new strategy for early diagnosis of type 2 diabetes by standard-free, label-free LC-MS/MS quantification of glycated peptides. Diabetes. 62(11):3936–3942.
   PubMed Web of Science ®Google Scholar
• Zhang, Y., Cocklin, R. R., Bidasee, K. R. and Wang, M. (2003). Rapid determination of advanced glycation end products of proteins using MALDI-TOF-MS and PERL script peptide searching algorithm. J. Biomol. Tech. 14(3):224–230.
   PubMedGoogle Scholar
• Zheng, L., Jiangb, M., Youa, J., Luoa, Y. and Fenga, L. (2014). Impact of Maillard reaction conditions on the antigenicity of parvalbumin, the major allergen in grass carp. grass carp. Food Agric. Immunology. 25:486–497.
   Web of Science ®Google Scholar
• Zill, H., Bek, S., Hofmann, T., Huber, J., Frank, O., Lindenmeier, M., Weigle, B., Erbersdobler, H. F., Scheidler, S., Busch, A. E. and Faist, V. (2003). RAGE-mediated MAPK activation by food-derived AGE and non-AGE products. Biochem. Biophys. Res. Commun. 300(2):311–315.
   PubMed Web of Science ®Google Scholar
• Zill, H., Günther, R., Erbersdobler, H. F., Fölsch, U. R. and Faist, V. (2001). RAGE expression and AGE-induced MAP kinase activation in Caco-2 cells. Biochem. Biophys. Res. Commun. 288(5):1108–1111.
   PubMed Web of Science ®Google Scholar
• Zong, H., Madden, A., Ward, M., Mooney, M. H., Elliott, C. T. and Stitt, A. W. (2010). Homodimerization is essential for the receptor for advanced glycation end products (RAGE)-mediated signal transduction. J. Biol. Chem. 285(30):23137–23146.
   PubMed Web of Science ®Google Scholar