{"title":"Maillard compounds as crosslinks in heated beta-casein-glucose systems.","authors":"L. Pellegrino, M. Boekel, H. Gruppen, P. Resmini","doi":"10.1533/9781845698447.2.100","DOIUrl":"https://doi.org/10.1533/9781845698447.2.100","url":null,"abstract":"Summary Heat-induced covalent aggregation of β-casein reported to be sugar-dependent has been studied with respect to both the early and advanced stages of the Maillard reaction. The aggregation of β-casein via reaction with glucose evaluated by gel-permeation chromatography in model solutions heated under a wide range of concentrations appeared to occur free of interference only in very dilute solutions (1 mg protein/mL), and was not related to the amount of fructoselysine and lysyl pyrraline. It was clearly related to the formation of pentosidine which, however, never exceeded 2 mmol/mol β-casein. The heat-induced incorporation of [U-14C]-labelled Lys or Arg into β-casein in the presence of glucose simulated intermolecular crosslinking and suggested that only few reactive residues can act as acceptors. The radioactive patterns obtained by Ion-exchange chromatography and RP-HPLC. after either acid or enzymatic hydrolysis of the labelled β-casein, showed that highly basic and hydrophobic molecules involving mutual interactions of Arg and Lys are responsible for β-casein aggregation.","PeriodicalId":359473,"journal":{"name":"The Maillard Reaction in Foods and Medicine","volume":"56 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"133609418","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Influence of D-Glucose Configuration on the Kinetics of the Nonenzymatic; Browning Reaction","authors":"J. Häseler, Beate Beyerlein, L. Kroh","doi":"10.1533/9781845698447.4.172","DOIUrl":"https://doi.org/10.1533/9781845698447.4.172","url":null,"abstract":"Summary The kinetics of the nonenzymatic browning reaction, especially caramelization, was influenced by the configuration of D-glucose. Spectrophotometric analysis suggests a higher reactivity of β-D-glucose in comparison with α-D-glucose during caramelization. More 5-hydroxymethyl-2-furaldehyde (HMF) and 2-furaldehyde (FF) were obtained from β-D-glucose than from α-D-glucose. In addition to the 3-deoxyglucosone pathway, an alternative mechanism via two C3-fragments was proposed. The formation of 1,6-anhydro-β-D-glucose and glucobioses was independent of the configuration of glucose because it passes through a glycosyl cation. Due to steric preference, the 1→6-linked glucobioses isomaltose and gentiobiose are favoured. Under Maillard reaction conditions, the formation of HMF was also influenced by the configuration. At the start of the reaction the Amadori compound was formed slightly easier from α-D-glucose.","PeriodicalId":359473,"journal":{"name":"The Maillard Reaction in Foods and Medicine","volume":"1 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"129465239","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"α-Acetyl-N-Heterocycles from Glutamic Acid and Carbohydrates","authors":"J. V. D. Ven, H. Weenen","doi":"10.1533/9781845698447.8.452","DOIUrl":"https://doi.org/10.1533/9781845698447.8.452","url":null,"abstract":"","PeriodicalId":359473,"journal":{"name":"The Maillard Reaction in Foods and Medicine","volume":"126 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"133420651","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Photo-Enhanced Modification of Human Skin Elastin in Actinic Elastosis by Nɛ-(Carboxymethyl)lysine, one of the Glycoxidation Products of the Maillard Reaction","authors":"Kumiko Mizutari, T. Ono, K. Kayashima","doi":"10.1533/9781845698447.8.427a","DOIUrl":"https://doi.org/10.1533/9781845698447.8.427a","url":null,"abstract":"","PeriodicalId":359473,"journal":{"name":"The Maillard Reaction in Foods and Medicine","volume":"24 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"132474333","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
P. Beisswenger, S. Howell, R. Stevens, A. Siegel, S. Lal, W. Randall, B. Szwergold, F. Kappler, T. Brown
{"title":"The Role of 3-Deoxyglucosone and the Activity of its Degradative Pathways in the Etiology of Diabetic Microvascular Disease","authors":"P. Beisswenger, S. Howell, R. Stevens, A. Siegel, S. Lal, W. Randall, B. Szwergold, F. Kappler, T. Brown","doi":"10.1533/9781845698447.7.298","DOIUrl":"https://doi.org/10.1533/9781845698447.7.298","url":null,"abstract":"Summary To address the role of 3-deoxyglucosone (3DG) and the activity of its major degradative pathways in diabetic nephropathy and retinopathy we have measured 3DG and its degradation products [3-deoxyfructose (3DF) and 3-deoxy-2-keto-gluconic acid (DGA)] in plasma and RBCs. In addition to these compounds, we have quantified HbA lc , renal dysfunction [glomerular filtration rate (GFR) and urinary albumin excretion(UAE)] and diabetic retinal sequelae over 2-3 years in 25 IDDM subjects with minimal complications during the earliest stages of diabetic microangiopathy. They were also measured in 58 subjects with NIDDM and 30 non-diabetic subjects. Plasma 3DG, 3DF and erythrocyte DGA were significantly elevated in diabetic subjects relative to controls. We also found a highly significant association between plasma 3DG and HbA lc concentrations, indicating that glycemic control is an important determinant of 3DG levels. An increased flux of 3DG to DGA and 3DF was associated with greater degrees of hyperglycemia, since both degradation products correlated with HbA lc values. Increasing rates of GFR also correlated with plasma 3DG levels and 3DG levels increased with increasing urinary albumin excretion (UAE). By contrast, there was an inverse correlation between plasma 3DF and UAE. Subjects showing progression of retinopathy also showed reduced plasma levels of the 3DG product 3DF relative to nonprogressors. As retinal perfusion decreased, we also observed increased 3DG levels.","PeriodicalId":359473,"journal":{"name":"The Maillard Reaction in Foods and Medicine","volume":"42 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"131779216","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
K. Ikeda, R. Nagai, T. Sakamoto, T. Higashi, Y. Jinnouchi, H. Sano, Kenshi Matsumoto, Masaki Yoshida, S. Ueda, S. Horiuchi, T. Araki
{"title":"Immunochemical Approaches to AGE-Structures—Characterization of Anti-AGE Antibodies","authors":"K. Ikeda, R. Nagai, T. Sakamoto, T. Higashi, Y. Jinnouchi, H. Sano, Kenshi Matsumoto, Masaki Yoshida, S. Ueda, S. Horiuchi, T. Araki","doi":"10.1533/9781845698447.7.310","DOIUrl":"https://doi.org/10.1533/9781845698447.7.310","url":null,"abstract":"Summary Recent immunological approaches have greatly helped broaden our understanding of the biomedical significance of AGEs (advanced glycation end-products) in aging and age-enhanced disease processes. We previously prepared a monoclonal anti-AGE antibody (6D12) that recognized a common AGE-structure(s) as a major immunochemical epitope. Subsequently, Nɛ-(carboxymethyl)lysine (CML), one of the glycoxidation products of AGEs, was demonstrated to be a major immunological epitope among AGEs, and 6D12 turned out to recognize CML as an epitope. In the present study, 13 different polyclonal anti-AGE antibodies were characterized in order to obtain the other epitope structure(s), other than CML (non-CML). We used CML-bovine serum albumin as an authentic CML-protein and AGE-lysozyme as an authentic non-CML-protein. The results indicated that these antibodies were classified into 3 groups (Group I, II & III). Group I was specific for CML, but both Group II and Group III were unreactive to CML. Group II, but not Group III, recognized AGE-lysozyme, suggesting Group II and III were specific for non-CML but different epitopes. The epitope of Group II was formed much earlier than that of Group III during incubation of BSA with glucose in vitro. Furthermore, we made two monoclonal anti-AGE antibodies (M-1 and M-2) whose epitope structures appeared to be identical or closely similar to Group III and Group II, respectively. These results indicate that AGE-proteins express two major non-CML epitopes in addition to CML.","PeriodicalId":359473,"journal":{"name":"The Maillard Reaction in Foods and Medicine","volume":"29 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"133947637","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Nonenzymic Glycation of Phosphatidylethanolamine in Vivo","authors":"K. Suyama, Kazutoshi Watanabe","doi":"10.1533/9781845698447.8.446","DOIUrl":"https://doi.org/10.1533/9781845698447.8.446","url":null,"abstract":"","PeriodicalId":359473,"journal":{"name":"The Maillard Reaction in Foods and Medicine","volume":"13 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"132936422","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
H. Sano, T. Higashi, Y. Jinnouchi, R. Nagai, Kenshi Matsumoto, Zhuo Qin, K. Ikeda, Y. Ebina, H. Makino, S. Horiuchi
{"title":"Insulin Accelerates the Endocytic Uptake and Degradation of Advanced Glycation End-Products Mediated by The Macrophage Scavenger Receptor","authors":"H. Sano, T. Higashi, Y. Jinnouchi, R. Nagai, Kenshi Matsumoto, Zhuo Qin, K. Ikeda, Y. Ebina, H. Makino, S. Horiuchi","doi":"10.1533/9781845698447.7.386","DOIUrl":"https://doi.org/10.1533/9781845698447.7.386","url":null,"abstract":"Summary The macrophage scavenger receptor (MSR), one of the receptors for advanced glycation end-products (AGEs), mediates endocytic uptake and degradation of AGE-proteins in several cell types. In the present study, we examined whether MSR function was regulated by insulin signaling. Co-expression of human insulin receptor (IR) with MSR in Chinese hamster ovary (CHO) cells showed that insulin accelerated the degradation of AGE proteins to 160% of the control. The insulin-enhanced endocytic uptake of AGE-proteins was significantly inhibited by phosphatidylinositol-3-OH kinase (PI(3)K) inhibitors, wortmannin and LY294002. Thus, insulin signaling through the PI(3)K pathway may regulate MSR-mediated endocytic uptake of AGE-proteins.","PeriodicalId":359473,"journal":{"name":"The Maillard Reaction in Foods and Medicine","volume":"22 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"130606512","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
N. Traverso, S. Menini, L. Cosso, D. Cottalasso, M. Pronzato, U. Marinari
{"title":"Antibody Titres against Oxidativety Modified Proteins Reveal an Increased Oxidative Stress in Diabetic Rats","authors":"N. Traverso, S. Menini, L. Cosso, D. Cottalasso, M. Pronzato, U. Marinari","doi":"10.1533/9781845698447.8.448A","DOIUrl":"https://doi.org/10.1533/9781845698447.8.448A","url":null,"abstract":"","PeriodicalId":359473,"journal":{"name":"The Maillard Reaction in Foods and Medicine","volume":"15 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"122000672","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Modification of Protein Structure following Reaction with Epoxyalkenals","authors":"R. Zamora, F. Hidalgo","doi":"10.1533/9781845698447.8.453","DOIUrl":"https://doi.org/10.1533/9781845698447.8.453","url":null,"abstract":"","PeriodicalId":359473,"journal":{"name":"The Maillard Reaction in Foods and Medicine","volume":"45 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"125456295","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}