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2. List of Contributors

Author

Bell, M.J., primary, Berman, R.F., additional, Bernstock, J.D., additional, Bogoslovsky, T., additional, Brawman-Mintzer, O., additional, Cebak, J.E., additional, Chaudry, I.H., additional, Corser-Jensen, C.E., additional, Diaz-Arrastia, R., additional, Eisenberg, H.M., additional, Fox, L.A., additional, Gopinath, S.P., additional, Gurkoff, G.G., additional, Hall, E.D., additional, Hameed, M.Q., additional, Heidenreich, K.A., additional, Hernandez-Tejada, M.A., additional, Hersh, D.S., additional, Hill, R.L., additional, Howard, R.B., additional, Hubbard, W.J., additional, Jorge, R.E., additional, Keiski, M.A., additional, Kenney, K., additional, Kim, N., additional, Kinssies, R., additional, Kulbe, J.R., additional, Leath, T.C., additional, Lin, H.L., additional, Lyeth, B.G., additional, Miskin, B., additional, Moore, C., additional, Mtaweh, H., additional, Patel, M.B., additional, Robertson, C.S., additional, Rodriguez-Romanacce, H., additional, Romeika, J., additional, Rotenberg, A., additional, Sayeed, I., additional, Schinzel, R., additional, Schober, M.E., additional, Sen, A.N., additional, Shahlaie, K., additional, Simard, J.M., additional, Simon, D., additional, Singh, I.N., additional, Stein, D.G., additional, Sun, D., additional, Tegtmeier, F., additional, Tobinick, E., additional, Wang, J.A., additional, Wilson, L.D., additional, and Wurzelmann, M., additional

Published
2017
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12. Abstracts Second Congress of the European Society for Clinical Neuropharmacology: Würzburg, November 9–11, 1995

Author

Agid, Y., Arendt, T., Gärtner, U., Holzer, M., Fruth, P., Brückner, M. K., Arzberger, T., Weindl, A., Baas, H., Demisch, L., Harder, S., Bürklin, F., Fischer, P. A., Bagli, M., Rao, M. L., Sobanski, T., Laux, G., Barbier, P., Fumagalli, F., Donati, E., Maggio, R., Racagni, G., Corsini, G. U., Riva, M., Berger, J., Löschl, B., Bernheimer, H., Lugowska, A., Tylki-Szymanska, A., Gieselmann, V., Molzer, B., Faé, I., Bernocchi, G., Scherini, E., Necchi, D., Bigl, M., Bleyl, D., Bigl, V., Eschrich, K., Block, F., Schwarz, M., Blum-Degen, D., Müller, Th., Kuhn, W., Gerlach, M., Przuntek, H., Riederer, R., Bonuccelli, U., Ceravolo, R., Nuti, A., D'Avino, C., Placidi, G., Perugi, G., Cassano, G. B., Del Dotto, P., Piccini, P., Colzi, A., Muratorio, A., Braak, H., Braak, E., Yilmazer, D. M., de Vos, R. A. I., Jansen, E. N. H., Bringmann, G., Clement, H. W., Grote, C., Rausch, F., Reichmann, H., Riederer, P., Sontag, K. -H., Wesemann, W., God, R., Feineis, D., Brückner, R., Protzen, J. -A., Fähr, S., Rausch, W. -D., Brunt, E. R. P., Pruim, J., Willemsen, A. J., van Weerden, T. W., Bryan-Lluka, L. J., Bönisch, H., Büttner, Th., Kühn, W., McMonagle, U., Calza, L., Pozza, M., Coraddu, F., Farci, G., Carlsson, A., Napolitano, A., Salvetti, S., Dell'Agnello, G., Renna, M., Conquet, F., Bashir, Z., Daniel, H., Ferraguti, F., Collingridge, G., Crépel, F., Coos Verhoef, J., Merkus, F. W. H. M., Junginger, H. E., Cruz-Sánchez, F. F., Kutschka, T., Beeg, M., Deuschle, M., Weber, B., Körner, A., Standhardt, H., Lammers, C. -H., Motzek-Noé, T., Heuser, I., Earl, C. D., Reum, T., Sautter, J., Xie, J. -X, Kupsch, A., Oertel, W. H., Morgenstern, R., Emilien, G. M., Maloteaux, J. M., Seghers, A., Charles, G., Erdmann, R., Högemann, D., Fichter, N., Lücking, C. H., Landwehrmeyer, G. B., Winter, T., Feuerstein, T. J., Fitzgeral, D., Anderson, M. C., Lawlor, B., Tipton, K. F., Frackowiak, R. S. J., Freo, U., Dam, M., Pizzolato, G., Merico, A., Ori, C., Sale, E., Battistin, L., Fritze, J., Froelich, L., Goetz, M., Gsell, W., Jellinger, K., Beckmann, H., Fünfgeld, E. W., Glinka, Y., Youdim, M. B. H., Götz, M. E., Breithaupt, W., Burger, R., Streifler, M., Simanyi, M., Müller, F., Danielczyk, W., Hirning, T., Sohlbach, M., Nafc, R., Sternadl, H., Winter, M., Nöth, U., Heim, C., Hartmann, J., Künig, G., Niedermeyer, B., Berger, W., Deckert, J., Abel, F., Heinsen, H., Senitz, D., Mayr, J., Ransmayr, G., Hartung, H. -P., Heils, A., Teufel, A., Petri, S., Seemann, M., Bengel, D., Degen, H. J., Lesch, K. P., Sontag, T., Heinen, F., Korinthenberg, R., Heiss, W. -D., Rüb, U., Gangus, B., Jungkunz, G., Bauer, M., Ulmar, G., Böcker, F., Schüler, M., Bethke, B., Lockemann, U., Hermans, E., Vanhoorde, P., Hesse, S., Hüll, M., Fiebich, B., Lieb, K., Strauss, S., Berger, M., Volk, B., Bauer, J., Iversen, L. L., Janetzky, B., Hauck, S., Jeanjean, A. P., Laterre, E. C., Bancher, C., Jost, W. H., Kalus, P., Kanner, B., Khrapova, E. V., Brusov, O. S., Knauber, J., Müller, W. E., Korczyn, A. D., Kornhuber, J., Parsons, C. G., Hartmann, S., Retz, W., Kamolz, S., Thome, J., Koutsilieri, E., Chen, T. -S., Kreutzberg, G. W., Krieglstein, J., Winkel, R., Danielcyk, S., Gerstner, A., Mattern, C., Häcker, R., Labunsky, D., Zhirnova, I., Komelkova, L., Popova, L., Avdiunina, I., Lakke, J. P. W. F., Lange, K. W., Steup, A., Tucha, O., Naumann, M., Lassmann, H., Leszek, J., Gasiorowski, K., Inglot, D., Lohse, M. J., Löschmann, P. -A., Eblen, F., Wüllner, U., Klockgether, T., Dichgans, J., Macrae, I. M., Mimmack, M. L., Emson, P., Norta, M., Borchert, H. -H., Medori, R., Chan, W. W., Heinemann, T., Melzacka, M., Kolasiewicz, W., Sieklucka, M., Jaros, T., Mesec, A., Šega, S., Kiauta, T., Moser, A., Vieregge, P., Siebecker, F., Münch, G., Schinzel, R., Michaelis, J., Cunningham, A., Da Prada, M., Borroni, E., Zürcher, G., Reiners, K., Neveu, P. J., Nitsch, R. M., Pavese, N., Lucetti, C., Rossi, G., Offen, D., Ziv, I., Stein, R., Barzilai, A., Hochman, A., Melamed, E., Ozawa, H., Hashimoto, E., Saito, T., Ymamoto, M., Takahata, N., Frölich, L., Paulus, W., Hermsteiner, E., Haug, B., Bandelow, B., Peckys, D., Gleichauf, O., Jackisch, R., Landwehrmeyer, B., Bloß, H. G., Plaschke, K., Müller, D., Hoyer, S., Avdyuna, L. A., Putzke, J., Spanagel, R., Tolle, T. R., Zieglgänsberger, W., Rabey, J. -M., Orlov, E., von Raison, F., Lehmann, K., Havemann-Reinecke, U., Butà, M., Federspiel, S., Maier, H., Abdel-mohsen, M., Abdel-moneim, M., Reynolds, G. P., Sardar, A. M., Eggett, C. J., Rosario, P., de la Morena, E., José Barro, M., Rossini, P. M., Roth, J., Růžička, E., Svobodová, I., Mečíř, P., Jech, R., Remeš, F., Kleinschroth, A., Schliebs, R., Roßner, S., Heider, M., Schubert, H., König, P., Schuttes, H., HaveIec, L., Schwartz, J. -C., Sendtner, M., Smith, A., Li, M., Griesbeck, O., Parsadanian, A., Holtmann, B., Carroll, P., Toyka, K. V., Thoenen, H., Sharkawy, A. A., Ibrahim, T. A., Pulkowski, U., Siesjö, B. K., Klessaschek, M., Sopper, S., Demuth, M., Dörries, R., Hemm, S., Stahl-Hennig, C., Brinkmann, R., ter Meulen, V., Sperk, G., Schwarzer, C., Stern, G., Storm, G., Strein, I., Struck, M., Stürenburg, H. J., Kunze, K., Svadovsky, A. I., Morgunov, K. V., Peresedov, V. V., Moshkin, A. V., Teherani, D. K., Baumer, A., Rösier, M., Rösler, M., Wiesbeck, G. A., Wodarz, N., Boning, J., Timerbaeva, S. L., Alekseeva, N. S., Toso, A., Barletta, D., Tuulik, V., Lossmann, E., Raja, A., Meister, A., Uitti, R. J., Rajput, A. H., Ahlskog, J. E., Offord, K. P., Schroeder, D. R., O'Brien, P. C., Vaglini, F., Fascetti, F., Pardini, C., Mancino, L., Velbinger, K., Hartmann, H., Eckert, A., Grüter, S., Behrens, S., Niemann, J., Guschelbauer, B., Lauk, M., Wissel, J., Poewe, W., Wurthman, C., Janzen, E. N. H., Goping, G., Adegemo, O. M., Gemma, A., Kuijpers, J., Pollard, H. B., Zielke, B., Ziemann, U., and Bruns, D.

Published
1995
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22. [Increased levels of circulating advanced glycation end products in a model of acute renal insufficiency in rats]

Author

Peter Boor, Bozek P, Blazícek P, Syrová D, Schinzel R, Heidland A, Pecovová A, and Sebeková K

Subjects
Glycation End Products, Advanced, Male, Oxidative Stress, Creatinine, Lysine, Malondialdehyde, Animals, Acute Kidney Injury, Rats, Wistar, Antioxidants, Lipofuscin, Rats
Abstract

Advanced glycation end products (AGEs) are formed from proteins and peptides by non-enzymatic glycation or glycooxidation. AGEs are formed slowly during aging, and they accumulate in circulation and tissues in diabetes and chronic renal failure. Kidney plays a key role in the disposal of AGEs. Aim of this study was to verify the hypothesis that, acute loss of renal function with enhanced oxidative and carbonyl stress should result in a rise of circulating AGEs levels.Acute renal failure (ARI) was induced in rats by bilateral nephrectomy (24-72 hours). The data on AGEs levels, oxidative status and antioxidative defense was compared to those of sham operated animals. 48 hours after the induction of ARI concentrations of AGEs, determined fluorimetrically or as carboxymethyllysine, rose 2-fold, and they correlated with concentrations of creatinine (r = 0.938, p0.001 and r = 0.815, p0.001, respectively). Malondialdehyde (MDA) and lipofuscine (LF) concentrations rose in a time dependent manner, suggesting an enhanced oxidative and carbonyl stress. Enhanced lipid peroxidation did not result from the suppressed antioxidant defense: activity of superoxide dismutase rose by 50%, while that of glutathione peroxidase was not compromised. Total antioxidant status increased, probably due to the accumulation of uremic toxins with scavenging capacity, such as hyppurate.According to our knowledge our data was first to show a rapid increase in circulating AGEs concentrations in the model of acute renal failure in rats. If AGEs accumulate in acute renal failure in humans, their contribution to acute toxicity, and/or to the development of later complications, might be of a great importance.

Published
2001

24. AGE-induced genomic damage in kidney tubule cells

Author

Schupp, N, Heidland, A, Scheurich, M, Schinzel, R, Klassen, A, Sebekova, K, Stopper, H, Schupp, N, Heidland, A, Scheurich, M, Schinzel, R, Klassen, A, Sebekova, K, and Stopper, H

Published
2004

39. Paradox of circulating advanced glycation end product concentrations in patients with congestive heart failure and after heart transplantation.

Author

Heicfland, A., Šeboková, K., Frangiosa, A., de Santo, L. S., Cirillo, M., Rossi, F., Cotrufo, M., Perna, A., Klassen, A., Schinzel, R., and de Santo, N. G.

Subjects
CONGESTIVE heart failure, HEART diseases, HEART failure, TRANSPLANTATION of organs, tissues, etc., GLOMERULAR filtration rate, KIDNEY function tests
Abstract

Objectives: To analyse circulating concentrations of advanced glycation end products (AG Es) in patients with severe congestive heart failure (CHF) and after heart transplantation; to identify the potential contribution of kidney function to plasma AGE concentrations; and to determine whether AGE concentrations and parameters of oxidative stress are interrelated. Methods and results: Circulating NE-(carboxymethyl)lysine (CML) and AGE associated fluorescence (AGE- Fl), lipid peroxidation, and glomerular filtration rate (GFR) were measured in a cross sectional study of 22 patients with advanced CHF, 30 heart transplant recipients, and 20 healthy controls. Compared with the controls, the Cl-IF patients had decreased CML (mean (SEM) 467.8 (20.0) ng/ml v 369.3 (22.3) ng/ml, p < 0.01), AGE-Fl (mean (SEM) 302.2 (13.3) arbitrary units v 204.9(15.7) arbitrary units, p < 0.01), and GFR (p < 0.01). CML was positively related to decreased total protein and serum albumin and negatively to body mass index (p < 0.01). In contrast, in the heart transplant group, impaired GFR was associated with a notable rise of both CMI (mean (SEM) 876.1 (53.1) ng/ml, p < 0.01) and AGE-Fl (mean (SEM) 385.6 (26.1) arbitrary units, p < 0.01). A positive relation between CML and serum albumin (r = 0.394, p <0.05) and lipofuscin (r =0.651, p < 0.01) was found. Conclusions: The contrasting concentration of CML and AGE-Fl between patients with CHF and after heart transplantation in the presence of decreased GFR and oxidative stress are explained by lowered plasma proteins in CHF and higher concentrations in heart transplant recipients. In heart transplant recipients, in addition to myocardial inflammatory processes, immunosuppression may be important for enhanced formation of AGEs. [ABSTRACT FROM AUTHOR]

Published
2004
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40. Impact of metabolic control and serum lipids on the concentration of advanced glycation end products in the serum of children and adolescents with type 1 diabetes, as determined by fluorescence spectroscopy and nepsilon-(carboxymethyl)lysine ELISA.

Author

Galler A, Müller G, Schinzel R, Kratzsch J, Kiess W, Münch G, Galler, Angela, Müller, Grit, Schinzel, Reinhard, Kratzsch, Juergen, Kiess, Wieland, and Münch, Gerald

Abstract

Objective: Advanced glycation end products (AGEs) are a complex and heterogenous group of proteins that are formed by nonenzymatic glycation in a series of reactions. It is hypothesized that they may play a role in the pathogenesis of diabetes-related complications; at present, however, their exact biological role is scarcely understood. Clinical studies so far have shown that serum levels of AGEs are correlated with clinical stages of diabetes complications such as retinopathy and nephropathy. This study was performed in children and adolescents with type 1 diabetes to examine the putative role of serum AGEs in respect to metabolic control and diabetes complications in relation to a number of clinical and laboratory parameters.Research Design and Methods: We studied 99 children and adolescents up to the age of 20 years with type 1 diabetes and 60 control subjects. Serum levels of AGEs were measured with two different methods [fluorescence spectroscopy and Nepsilon-(carboxymethyl)lysine (CML) enzyme-linked immunosorbent assay] and correlated with clinical data, such as age, diabetes duration, BMI, and long-term metabolic control determined by HbA(1c), and laboratory parameters, such as serum lipids.Results: Serum levels of fluorescent AGEs, but not of CML-AGEs, in children and adolescents with type 1 diabetes were significantly higher compared with control subjects. There was an age-dependent increase of fluorescent AGEs in children and adolescents with diabetes that was not seen in healthy children and adolescents. Levels of fluorescent AGEs in patients with diabetes between 13 and 16 years of age correlated positively with HbA(1c) levels. No significant association between levels of AGEs and diabetes duration was found. Children and adolescents with diabetes and high serum triglycerides had significantly higher serum levels of fluorescent AGEs. Children and adolescents with diabetes between the age of 13 and 16 years with high levels of LDL had significantly higher levels of fluorescent AGEs.Conclusions: In this study we demonstrated a clear age-dependent increase of fluorescent AGEs but not of CML-AGEs in children and adolescents with diabetes type 1. Moreover we showed a strong association between serum AGEs and serum triglycerides and cholesterol. The observed effect may be caused by a loss of optimal regulation of lipid metabolism. It could suggest a link between triglycerides and formation of AGEs. This new and interesting finding and its impact on metabolic control and the development of diabetes complications should be examined in the future. [ABSTRACT FROM AUTHOR]

Published
2003
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42. Advanced glycation end products (AGEs)-induced expression of TGF-beta 1 is suppressed by a protease in the tubule cell line LLC-PK1.

Author

Xiang, G, Schinzel, R, Simm, A, Münch, G, Sebekova, K, Kasper, M, Niwa, T, Schmitz, C, and Heidland, A

Abstract

Advanced glycation end products (AGEs) are assumed to play a key role in diabetic nephropathy (DN). Since little is known about their action in tubule cells, we investigated in LLC-PK1 cells: (i) whether AGE-bovine serum albumin (AGE-BSA) affects cell proliferation and expression of transforming growth factor-beta (TGF-beta 1); and (ii) whether the AGE-induced effects can be modulated by trypsin due to interference with its binding proteins at the cell surface.

Published
2001
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46. The phosphate recognition site of Escherichia colimaltodextrin phosphorylase

Author

Schinzel, R. and Drueckes, P.

Abstract

The role of two positively charged amino acid residues located at the active site of Escherichia colimaltodextrin phosphorylase was investigated by site-directed mutagenesis, Substitution of Lys539by an arginine caused a 600-fold reduction, substitution of Arg534by a glutamine caused an even larger 7000-fold reduction of the catalytic rate while substrate binding remained essentially unaffected. Since the Arg534→Gln exchange reduces the catalytic rate near to inactivity and even the conservative Lys534→Arg exchange caused a marked decrease of activity, the central functional role of both positively charged residues in phosphorylase catalysis anticipated by the crystallographic analysis of the corresponding amino acid residues Arg569and Lys574in the catalytic site of phosphorylase bwas confirmed.

Published
1991
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