Involvement of Hydrogen Peroxide in Collagen Cross-linking by High Glucose in Vitro and in Vivo
Open accessAbstract
The Maillard reaction has been implicated in cross-linking and fluorescence formation of collagen exposed to high glucose in vitro. However, several pharmacologic agents, whose action seems unrelated to pathways of nonenzymatic glycation, have been demonstrated to prevent cross-linking in diabetes. To clarify this discrepancy, kinetic changes in glycation, glycoxidation (carboxymethyllysine, CML), and cross-linking (measured as tendon breaking time, TBT) were evaluated in rat tail tendons incubated in 5 and 30 mM glucose in vitro and in tendons implanted in vivo into diabetic rat peritoneal cavity. In vitro, rates were found to be both O2- and glucose-dependent. Tendon preglycation and presence of added 2 mM glycosylamine and Amadori compounds (Amadori product of glucose and propylamine) catalyzed these changes in a primarily O2-dependent manner. In the presence of Amadori compounds, kinetic changes were dramatically increased and were preventable by addition of catalase to the medium. Tendons implanted into diabetic rat peritoneum became more rapidly glycoxidized and cross-linked when implanted at day 30 from diabetes onset (high tissue glycation) compared to day 3 (low tissue glycation) in spite of similar glycation kinetics, suggesting a mechanistic dissociation between glycation, glycoxidation, and cross-linking in diabetes. Indeed, intraperitoneal injection of catalase and other antioxidants dramatically suppressed cross-linking, fluorescence formation, and, to some extent, glycoxidation, without affecting glycation. This study confirms the role of oxidative stress in protein cross-linking by the Maillard reaction in vitro and provides the first evidence for a role of H2O2 in cross-linking in diabetes. Whereas Amadori products are a potent source of H2O2 formation in vitro, their precise contribution to H2O2 generation and the actual role of Maillard reaction products in collagen cross-linking in diabetes requires further investigation.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The multiple higher mass electrophoretic components containing tissue metalloproteinase inhibitor 3 and vitronectin suggest the presence of covalent crosslinks.
“The multiple, higher mass electrophoretic components containing these proteins suggest the presence of covalent crosslinks, protein modifications that can be caused by reactive lipid and carbohydrate oxidation products (22, 23).”
From Drusen proteome analysis: an approach to the etiology of age-related macular degeneration (2002) · cites this paper as [23]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Role of Oxidative Stress in Development of Complications in Diabetes
Baynes, J. (1991) · Diabetes · doi:10.2337/diab.40.4.405 · Cited by 3,791 · see citing works
Stadtman, E. R. (1992) · Science · doi:10.1126/science.1355616 · Cited by 2,701 · see citing works
Dehydrated Foods, Chemistry of Browning Reactions in Model Systems
Hodge, J. E. (1953) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf60015a004 · Cited by 1,950 · see citing works
Wolff, S. P., & Dean, R. T. (1987) · Biochemical Journal · doi:10.1042/bj2450243 · Cited by 1,277 · see citing works
Aminoguanidine Prevents Diabetes-Induced Arterial Wall Protein Cross-Linking
Brownlee, M., Vlassara, H., Kooney, A., Ulrich, P. C., & Cerami, A. (1986) · Science · doi:10.1126/science.3487117 · Cited by 1,146 · see citing works
Protein glycation and oxidative stress in diabetes mellitus and ageing
Wolff, S. P., Jiang, Z. Y., & Hunt, J. V. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90040-a · Cited by 886 · see citing works
Ahmed, M. U., Thorpe, S. R., & Baynes, J. W. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)89188-3 · Cited by 864 · see citing works
Nonenzymatic Browning in Vivo: Possible Process for Aging of Long-Lived Proteins
Monnier, V. M., & Cerami, A. (1981) · Science · doi:10.1126/science.6779377 · Cited by 768 · see citing works
Self-citationJohnson, R. N., Metcalf, P., & Baker, J. R. (1983) · Clinica Chimica Acta · doi:10.1016/0009-8981(83)90078-5 · Cited by 763 · see citing works
New Aspects of the Maillard Reaction in Foods and in the Human Body
Ledl, F., & Schleicher, E. D. (1990) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199005653 · Cited by 738 · see citing works
Albumin—An important extracellular antioxidant?
Halliwell, B. B. (1988) · Biochemical Pharmacology · doi:10.1016/0006-2952(88)90126-8 · Cited by 648 · see citing works
Wells‐Knecht, K. J., Zyzak, D. V., Litchfield, J., Thorpe, S. R., & Baynes, J. (1995) · Biochemistry · doi:10.1021/bi00011a027 · Cited by 594 · see citing works
Glomb, M. A., & Monnier, V. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.17.10017 · Cited by 576 · see citing works
Self-citationMinotti, G., & Aust, S. D. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75755-x · Cited by 544 · see citing works
Hydrogen peroxide production during experimental protein glycation
Jiang, Z. Y., Woollard, A. C. S., & Wolff, S. P. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80974-n · Cited by 518 · see citing works
Fu, M.-X., Wells‐Knecht, K. J., Blackledge, J. A., Lyons, T. J., Thorpe, S. R., & Baynes, J. (1994) · Diabetes · doi:10.2337/diab.43.5.676 · Cited by 464 · see citing works
Enzymatic and nonenzymatic cross‐linking of collagen and elastin
Reiser, K. M., McCormick, R. J., & Rucker, R. B. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.7.1348714 · Cited by 452 · see citing works
Superoxide production from nonenzymatically glycated protein
Sakurai, T., & Tsuchiya, S. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80066-8 · Cited by 304 · see citing works
Intact human ceruloplasmin oxidatively modifies low density lipoprotein.
Ehrenwald, E., Chisolm, G. M., & Fox, P. L. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117127 · Cited by 262 · see citing works
Hunt, J. V., Bottoms, M., & Mitchinson, M. (1993) · Biochemical Journal · doi:10.1042/bj2910529 · Cited by 195 · see citing works
Ascorbic acid metabolism in diabetes mellitus
Som, S., Basu, S., Mukherjee, D., Deb, S., Choudhury, P. R., Mukherjee, S., Chatterjee, S. N., & Chatterjee, I. B. (1981) · Metabolism · doi:10.1016/0026-0495(81)90133-5 · Cited by 191 · see citing works
Collagen Defect Induced by Penicillamine
Nimni, M. E., & Bavetta, L. A. (1965) · Science · doi:10.1126/science.150.3698.905 · Cited by 188 · see citing works
Yu, P. H., & Zuo, D. (1993) · Diabetes · doi:10.2337/diab.42.4.594 · Cited by 174 · see citing works
A Defect in the Intramolecular and Intermolecular Cross-linking of Collagen Caused by Penicillamine
Nimni, M. E. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93565-9 · Cited by 156 · see citing works
Pathways of Formation of Glycoxidation Products during Glycation of Collagen
Wells-Knecht, M. C., Thorpe, S. R., & Baynes, J. (1995) · Biochemistry · doi:10.1021/bi00046a020 · Cited by 155 · see citing works
Brownlee, M., Pongor, S., & Cerami, A. (1983) · The Journal of Experimental Medicine · doi:10.1084/jem.158.5.1739 · Cited by 153 · see citing works
Chang, K. C., Uitto, J., Rowold, E., Grant, G. A., Kilo, C., & Williamson, J. R. (1980) · Diabetes · doi:10.2337/diacare.20.10.778 · Cited by 120 · see citing works
Mechanism of the degradation of non‐enzymatically glycated proteins under physiological conditions
Smith, P. R., & Thornalley, P. J. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17474.x · Cited by 119 · see citing works
Effect of phosphate on the kinetics and specificity of glycation of protein.
Watkins, N. G., Neglia, C. I., Dyer, D. G., Thorpe, S. R., & Baynes, J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48224-5 · Cited by 114 · see citing works
Odetti, P. R., Borgoglio, A., Pascale, A. D., Rolandi, R., & Adezati, L. (1990) · Diabetes · doi:10.2337/diab.39.7.796 · Cited by 112 · see citing works
Formation of Reactive Intermediates from Amadori Compounds under Physiological Conditions
Zyzak, D. V., Richardson, J. M., Thorpe, S. R., & Baynes, J. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1073 · Cited by 94 · see citing works
Chace, K. V., Carubelli, R., & Nordquist, R. E. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90223-6 · Cited by 87 · see citing works
Chemistry of the fructosamine assay: D-glucosone is the product of oxidation of Amadori compounds
Baker, J. R., Zyzak, D. V., Thorpe, S. R., & Baynes, J. (1994) · Clinical Chemistry · doi:10.1093/clinchem/40.10.1950 · Cited by 82 · see citing works
Sakurai, T., Sugioka, K., & Nakano, M. (1990) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(90)90106-8 · Cited by 82 · see citing works
Odetti, P. R., Pronzato, M. A., Noberasco, G., Cosso, L., Traverso, N., Cottalasso, D., & Marinari, U. M. (1994) · PubMed · Cited by 78 · see citing works
Diabetic complications : scientific and clinical aspects
Crabbe, M. J. C. (1987) · Medical Entomology and Zoology · Cited by 78 · see citing works
Interrelation of Platelet Vitamin E and Thromboxane Synthesis in Type I Diabetes Mellitus
Karpen, C. W., Cataland, S., O’Dorisio, T. M., & Panganamala, R. V. (1984) · Diabetes · doi:10.2337/diab.33.3.239 · Cited by 68 · see citing works
Brennan, M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)30028-6 · Cited by 66 · see citing works
Development of novel free radicals during the amino-carbonyl reaction of sugars with amino acids
Namiki, M., & Hayashi, T. (1975) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf60199a024 · Cited by 64 · see citing works
Suárez, G., Rajaram, R., Bhuyan, K. C., Oronsky, A. L., & Goidl, J. A. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113641 · Cited by 63 · see citing works
Blood glutathione and non-glucose reducing substances in diabetes
Illing, E. K. B., GRAY, C. H., & Lawrence, R. D. (1951) · Biochemical Journal · doi:10.1042/bj0480637 · Cited by 63 · see citing works
Serum, zinc, copper and insulin in diabetes mellitus.
Mc, M., Jb, B., & Ma, C. (1978) · PubMed · Cited by 59 · see citing works
Metal chelates of dl-penicillamine
Kuchinskas, E. J., & Rosen, Y. (1962) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(62)90090-5 · Cited by 58 · see citing works
Maillard reactions in chemistry, food and health
Kennedy, J. F., & Knill, C. J. (1995) · Carbohydrate Polymers · doi:10.1016/0144-8617(95)90076-4 · Cited by 56 · see citing works
Changes in lung lysyl oxidase activity in streptozotocin-diabetes and in starvation
Madia, A. M., Rozovski, S. J., & Kagan, H. M. (1979) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(79)90181-8 · Cited by 53 · see citing works
Serum amine oxidase activity contributes to crisis in mouse embryo cell lines.
Parchment, R. E., Lewellyn, A. L., Swartzendruber, D. E., & Pierce, G. B. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.11.4340 · Cited by 52 · see citing works
Yue, D. K., McLennan, S. V., Handelsman, D. J., Delbridge, L., Reeve, T., & Turtle, J. R. (1984) · Diabetes · doi:10.2337/diab.33.8.745 · Cited by 50 · see citing works
Yue, D. K., McLennan, S. V., Handelsman, D. J., Delbridge, L., Reeve, T., & Turtle, J. R. (1985) · Diabetes · doi:10.2337/diab.34.1.74 · Cited by 49 · see citing works
Richard, S., Tamas, C., Sell, D. R., & Monnier, V. M. (1991) · Diabetes · doi:10.2337/diab.40.8.1049 · Cited by 41 · see citing works
Self-citationAoki, Y., Yanagisawa, Y., Yazaki, K., Oguchi, H., KIYOSAWA, K., & Furuta, S. (1992) · Diabetologia · doi:10.1007/bf00401418 · Cited by 38 · see citing works
Darstellung aliphatischer Amadori‐Produkte
Micheel, F., & Hagemann, G. (1959) · Chemische Berichte · doi:10.1002/cber.19590921127 · Cited by 37 · see citing works
Changes in the Cross-linking of Collagen from Rat Tail Tendons Due to Diabetes
Brennan, M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)30029-8 · Cited by 31 · see citing works
Weninger, M., Xi, Z., Lubec, B., Szalay, S., Höger, H., & Lübec, G. (2008) · The Nephron journals/Nephron journals · doi:10.1159/000187000 · Cited by 23 · see citing works
Cohen, M. P., Klepser, H., & Wu, V.-Y. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90063-c · Cited by 8 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- Sell D. R., and Monnier V. M. (1995) in Handbook of Physiology (Masoro, E. J., ed) pp. 253-302, Oxford University Press, New York
- Parchment, R. E., Lewellyn, A., Swartzendruber, D., and Pierce, G. B. (1990) Proc. Natl. Acad. Sci. U. S. A. 87, 4340 -4344
Cited by
Sorted by citations
The Free Radical Theory of Aging Matures
BECKMAN, K. B., & AMES, B. N. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.2.547 · Cited by 3,879 · see citing works
Drusen proteome analysis: an approach to the etiology of age-related macular degeneration
Crabb, J. W., Miyagi, M., Gu, X., Shadrach, K., West, K. A., Sakaguchi, H., Kamei, M., Hasan, A., Yan, L., Rayborn, M. E., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222551899 · Cited by 1,208 · see citing works
Indian herbs and herbal drugs used for the treatment of diabetes
Modak, M., Dixit, P., Londhe, J., Ghaskadbi, S., & Devasagayam, T. P. A. (2007) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.40.163 · Cited by 989 · see citing works
Radicals and oxidative stress in diabetes
West, I. C. (2000) · Diabetic Medicine · doi:10.1046/j.1464-5491.2000.00259.x · Cited by 913 · see citing works
Kamalakkannan, N., & Prince, P. S. M. (2006) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/j.1742-7843.2006.pto_241.x · Cited by 532 · see citing works
The missing link: A single unifying mechanism for diabetic complications
Nishikawa, T., Edelstein, D., & Brownlee, M. (2000) · Kidney International · doi:10.1046/j.1523-1755.2000.07705.x · Cited by 512 · see citing works
Antioxidative and Anti-Glycation Activity of Garcinol fromGarcinia indicaFruit Rind
Yamaguchi, F., Ariga, T., Yoshimura, Y., & Nakazawa, H. (2000) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf990845y · Cited by 449 · see citing works
Hyperglycemia and Glycation in Diabetic Complications
Nègre‐Salvayre, A., Salvayre, R., Augè, N., Pamplona, R., & Portero‐Otín, M. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2484 · Cited by 424 · see citing works
ROS: Crucial Intermediators in the Pathogenesis of Intervertebral Disc Degeneration
Feng, C., Yang, M., Lan, M., Liu, C., Zhang, Y., Huang, B., Liu, H., & Zhou, Y. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/5601593 · Cited by 384 · see citing works
Ahmed, S., Sulaiman, S. A., Baig, A. A., Ibrahim, M., Liaqat, S., Fatima, S., Jabeen, S., Shamim, N., & Othman, N. H. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/8367846 · Cited by 354 · see citing works
Beckman, K. B., & Ames, B. N. (2000) · Elsevier eBooks · doi:10.1016/b978-044482650-3/50027-4 · Cited by 307 · see citing works
Therapeutic efficacy of ozone in patients with diabetic foot
Martı́nez-Sánchez, G., Al‐Dalain, S. M., Menéndez, S., Re, L., Giuliani, A., Candelario‐Jalil, E., Álvarez, H., Fernández‐Montequín, J. I., & León, O. S. (2005) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2005.08.020 · Cited by 303 · see citing works
Negative consequences of glycation
Brownlee, M. (2000) · Metabolism · doi:10.1016/s0026-0495(00)80078-5 · Cited by 284 · see citing works
Iron and liver fibrosis: Mechanistic and clinical aspects
Mehta, K. J., Farnaud, S., & Sharp, P. (2019) · World Journal of Gastroenterology · doi:10.3748/wjg.v25.i5.521 · Cited by 271 · see citing works
The Chemistry of Protein Oxidation in Food
Hellwig, M. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201814144 · Cited by 259 · see citing works
Monnier, V. M., Mustata, G. T., Biemel, K. M., Reihl, O., LEDERER, M. O., ZHENYU, D., & Sell, D. R. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1333.061 · Cited by 245 · see citing works
Self-citationEffect of curcumin on the advanced glycation and cross-linking of collagen in diabetic rats
Sajithlal, G. B., Chithra, P., & Chandrakasan, G. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00237-8 · Cited by 215 · see citing works
The dark side of dioxygen biochemistry
Valentine, J. S., Wertz, D. L., Lyons, T. J., Liou, L.-L., Goto, J. J., & Gralla, E. B. (1998) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(98)80067-7 · Cited by 208 · see citing works
Oxidative damage to extracellular matrix and its role in human pathologies
Rees, M. D., Kennett, E. C., Whitelock, J. M., & Davies, M. J. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.016 · Cited by 206 · see citing works
Diabetes, Oxidative Stress and Physical Exercise
Atalay, M., & Laaksonen, D. E. (2002) · Journal of Sports Science and Medicine · doi:10.52082/jssm.2002.1 · Cited by 203 · see citing works
The general case for redox control of wound repair
Sen, C. K. (2003) · Wound Repair and Regeneration · doi:10.1046/j.1524-475x.2003.11607.x · Cited by 197 · see citing works
Intervention against the Maillard reaction in vivo
Monnier, V. M. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.08.014 · Cited by 196 · see citing works
Self-citationProtective Activity of Green Tea against Free Radical- and Glucose-Mediated Protein Damage
Nakagawa, T., Yokozawa, T., TERASAWA, K., Shu, S., & Juneja, L. R. (2002) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf011339n · Cited by 194 · see citing works
Yim, M. B., Yim, H., Lee, C., Kang, S., & Chock, P. B. (2001) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2001.tb05634.x · Cited by 177 · see citing works
Diamanti‐Kandarakis, E., Katsikis, I., Piperi, C., Kandaraki, E., Piouka, A., Papavassiliou, A. G., & Panidis, D. (2008) · Clinical Endocrinology · doi:10.1111/j.1365-2265.2008.03247.x · Cited by 172 · see citing works
A pharmacological appraisal of medicinal plants with antidiabetic potential
Najmi, A. K., Khan, V., Akhtar, M., Aqil, M., Mujeeb, M., & Pillai, K. K. (2012) · Journal of Pharmacy And Bioallied Sciences · doi:10.4103/0975-7406.92727 · Cited by 166 · see citing works
Cellular Stresses and Stress Responses in the Pathogenesis of Insulin Resistance
Onyango, A. N. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/4321714 · Cited by 160 · see citing works
Mechanisms for the formation of glycoxidation products in end-stage renal disease
Weiss, M. F., Erhard, P., Kader-Attia, F. A., Wu, Y. C., DeOreo, P. B., Araki, A., Glomb, M. A., & Monnier, V. M. (2000) · Kidney International · doi:10.1046/j.1523-1755.2000.00117.x · Cited by 155 · see citing works
Self-citationLee, C., Yim, M. B., Chock, P. B., Yim, H., & Kang, S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.39.25272 · Cited by 152 · see citing works
Reactive oxygen species and biological aging: a mechanistic approach
Schöneich, C. (1999) · Experimental Gerontology · doi:10.1016/s0531-5565(98)00066-7 · Cited by 148 · see citing works
Indian Journal of Research in Pharmacy and Biotechnology
(2019) · Indian Journal of Research in Pharmacy and Biotechnology · doi:10.31426/ijrpb · Cited by 137 · see citing works
Wells-Knecht, M. C., Lyons, T. J., McCance, D. R., Thorpe, S. R., & Baynes, J. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119599 · Cited by 138 · see citing works
Arya, A., Al‐Obaidi, M. M. J., Shahid, N., Noordin, M. I., Looi, C. Y., Wong, W. F., Khaing, S. L., & Mustafa, M. R. (2014) · Food and Chemical Toxicology · doi:10.1016/j.fct.2014.06.010 · Cited by 141 · see citing works
Punithavathi, V. R., Anuthama, R., & Prince, P. S. M. (2008) · Journal of Applied Toxicology · doi:10.1002/jat.1343 · Cited by 131 · see citing works
Inhibitory effects of ethyl acetate extract of Teucrium polium on in vitro protein glycoxidation
Ardestani, A. D., & Yazdanparast, R. (2007) · Food and Chemical Toxicology · doi:10.1016/j.fct.2007.06.020 · Cited by 128 · see citing works
Ahmed, O. M., Abdel‐Moneim, A., Yazid, I. A., & Mahmoud, A. M. (2010) · Diabetologia Croatica · Cited by 123 · see citing works
Hormones and tendinopathies: the current evidence
Oliva, F., Piccirilli, E., Berardi, A. C., Frizziero, A., Tarantino, U., & Maffulli, N. (2016) · British Medical Bulletin · doi:10.1093/bmb/ldv054 · Cited by 121 · see citing works
Relevance of oxidative and carbonyl stress to long-term uremic complications
Miyata, T., Kurokawa, K., & de Strihou, C. V. Y. (2000) · Kidney International · doi:10.1046/j.1523-1755.2000.07615.x · Cited by 119 · see citing works
Jayanthy, G., & Pillai, S. S. (2015) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-015-2374-6 · Cited by 114 · see citing works
Ardestani, A. D., & Yazdanparast, R. (2007) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2007.07.014 · Cited by 114 · see citing works
Identification of α-dicarbonyl scavengers for cellular protection against carbonyl stress
Wondrak, G. T., Cervantes-Laurean, D., Roberts, M. J., Qasem, J. G., Kim, M., Jacobson, E. L., & Jacobson, M. K. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(01)00915-7 · Cited by 108 · see citing works
Parveen, K., Khan, M. R., Mujeeb, M., & Siddiqui, W. A. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.04.023 · Cited by 108 · see citing works
Lui, P. P. Y., Zhang, X., Yao, S., Sun, H., & Huang, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073571 · Cited by 107 · see citing works
Al-Dalain, S. M., Martı́nez, G., Candelario‐Jalil, E., Menéndez, S., Re, L., Giuliani, A., & León, O. S. (2001) · Pharmacological Research · doi:10.1006/phrs.2001.0867 · Cited by 107 · see citing works
The Proteomics of DrusenPreprint
Crabb, J. W. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a017194 · Cited by 103 · see citing works
Paget, C., Lecomte, M., Ruggiero-Lopez, D., Wiernsperger, N. F., & Lagarde, M. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00071-9 · Cited by 95 · see citing works
Onyango, A. N. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/2398573 · Cited by 96 · see citing works
Karthikesan, K., Pari, L., & Menon, V. P. (2010) · Journal of Functional Foods · doi:10.1016/j.jff.2010.04.001 · Cited by 93 · see citing works
Abdel-Moneim, A., El-Twab, S. M. A., Yousef, A. I., Abdel-Reheim, E. S., & Ashour, M. B. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.06.096 · Cited by 92 · see citing works
Peruško, M., Al-Hanish, A., Veličković, T. Ć., & Stanić-Vučinić, D. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.01.042 · Cited by 91 · see citing works
The Generation of Superoxide Anions in Glycation Reactions with Sugars, Osones, and 3-Deoxyosones
ORTWERTH, B. J., James, H. L., Simpson, G., & Linetsky, M. D. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8401 · Cited by 89 · see citing works
Histone carbonylation in vivo and in vitro
Wondrak, G. T., Cervantes-Laurean, D., Jacobson, E. L., & Jacobson, M. K. (2000) · Biochemical Journal · doi:10.1042/bj3510769 · Cited by 88 · see citing works
Synergistic effects of glucose and ultraviolet irradiation on the physical properties of collagen
Ohan, M. P., Weadock, K. S., & Dunn, M. G. (2002) · Journal of Biomedical Materials Research · doi:10.1002/jbm.10111 · Cited by 87 · see citing works
Advanced glycation end products induce crosslinking of collagen in vitro
Sajithlal, G. B., Chithra, P., & Chandrakasan, G. (1998) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(98)00043-x · Cited by 86 · see citing works
Takahashi, M., Pischetsrieder, M., & Monnier, V. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3437 · Cited by 86 · see citing works
Self-citationSilva, J. P., Dhall, S., Garcia, M., Chan, A., Costa, C., Gama, M., & Martins‐Green, M. M. (2015) · Acta Biomaterialia · doi:10.1016/j.actbio.2015.07.043 · Cited by 84 · see citing works
Saxena, A. K., Saxena, P., Wu, X., Obrenovich, M. E., Weiss, M. F., & Monnier, V. M. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0898 · Cited by 84 · see citing works
Self-citationProteomic Analysis of the Site Specificity of Glycation and Carboxymethylation of Ribonuclease
Brock, J. W. C., Hinton, D. J. S., Cotham, W. E., Metz, T., Thorpe, S. R., Baynes, J., & Ames, J. M. (2003) · Journal of Proteome Research · doi:10.1021/pr0340173 · Cited by 82 · see citing works
Urios, P., Grigorova-Borsos, A.-M., & Sternberg, M. (2007) · European Journal of Nutrition · doi:10.1007/s00394-007-0644-0 · Cited by 79 · see citing works
Wondrak, G. T., Roberts, M. J., Jacobson, M. K., & Jacobson, E. L. (2002) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2002.01788.x · Cited by 77 · see citing works
Rutter, Sell, Fraser, Obrenovich, Zito, Starke-Reed, & Monnier (2003) · International Journal for Vitamin and Nutrition Research · doi:10.1024/0300-9831.73.6.453 · Cited by 76 · see citing works
Anwer, T., Sharma, M., Pillai, K. K., & Iqbal, M. (2008) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/j.1742-7843.2008.00223.x · Cited by 75 · see citing works
Production of Nε-(Carboxymethyl)Lysine Is Impaired in Mice Deficient in NADPH Oxidase
Anderson, M. M., & Heinecke, J. W. (2003) · Diabetes · doi:10.2337/diabetes.52.8.2137 · Cited by 73 · see citing works
Ahangarpour, A., Heidari, H., Fatemeh, R. A. A., Pakmehr, M., Shahbazian, H. B., Ahmadi, I., Mombeini, Z., & Mehrangiz, B. H. (2014) · Journal of Diabetes & Metabolic Disorders · doi:10.1186/2251-6581-13-29 · Cited by 73 · see citing works
Oxidative deamination of lysine residue in plasma protein of diabetic rats
Akagawa, M., Sasaki, T., & Suyama, K. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03243.x · Cited by 67 · see citing works
Proteomic Approaches to Understanding Age-Related Macular Degeneration
Hollyfield, J. G., Salomon, R. G., & Crabb, J. W. (2003) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0067-4_11 · Cited by 63 · see citing works
Gotloib, L., Shostak, A., Wajsbrot, V., & Kushnier, R. (1999) · The Nephron journals/Nephron journals · doi:10.1159/000045393 · Cited by 63 · see citing works
Glycoxidation in aortic collagen from STZ-induced diabetic rats and its relevance to vascular damage
Meng, J., Sakata, N., Takebayashi, S., Asano, T., Futata, T., Nagai, R., Ikeda, K., Horiuchi, S., Myint, T., & Taniguchi, N. (1998) · Atherosclerosis · doi:10.1016/s0021-9150(97)00238-4 · Cited by 59 · see citing works
Babu, P. V. A., Sabitha, K. E., & Shyamaladevi, C. S. (2007) · Food and Chemical Toxicology · doi:10.1016/j.fct.2007.08.005 · Cited by 58 · see citing works
Oxidation and modification of extracellular matrix and its role in disease
Chuang, C. Y., Degendorfer, G., & Davies, M. J. (2014) · Free Radical Research · doi:10.3109/10715762.2014.920087 · Cited by 57 · see citing works
Early Glycation Products Produce Pentosidine Cross-links on Native Proteins
Chellan, P., & Nagaraj, R. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008626200 · Cited by 55 · see citing works
Nishigaki, I., Rajendran, P., Venugopal, R., Ekambaram, G., Sakthisekaran, D., & Nishigaki, Y. (2009) · Phytotherapy Research · doi:10.1002/ptr.2867 · Cited by 54 · see citing works
Acute oxidative stress induces peritoneal hyperpermeability, mesothelial loss, and fibrosis
Gotloib, L., Wajsbrot, V., Cuperman, Y., & Shostak, A. (2004) · Journal of Laboratory and Clinical Medicine · doi:10.1016/j.lab.2003.09.005 · Cited by 53 · see citing works
The Nrf2 transcription factor: A multifaceted regulator of the extracellular matrix
Hiebert, P. (2021) · Matrix Biology Plus · doi:10.1016/j.mbplus.2021.100057 · Cited by 52 · see citing works
Yatoh, S., Mizutani, M., Yokoo, T., Kozawa, T., Sone, H., Toyoshima, H., Suzuki, S., Shimano, H., Kawakami, Y., Okuda, Y., et al. (2005) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.562 · Cited by 52 · see citing works
Paradoxical Impact of Antioxidants on Post-Amadori Glycoxidation
Culbertson, S. M., Vassilenko, E. I., Morrison, L. D., & Ingold, K. U. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305099200 · Cited by 52 · see citing works
den Hollander, N. C., Mulder, D. J., Graaff, R., Thorpe, S. R., Baynes, J., Smit, G., & Smit, A. J. (2007) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-007-0507-0 · Cited by 52 · see citing works
Nandini, H. S., & Naik, P. R. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.11.034 · Cited by 51 · see citing works
Glucose stabilizes collagen sterilized with gamma irradiation
Ohan, M. P., & Dunn, M. G. (2003) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.20018 · Cited by 51 · see citing works
An in vitro study on the role of metal catalyzed oxidation in glyeation and crosslinking of collagen
Sajithlal, G. B., Chithra, P., & Chandrakasan, G. (1999) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006988719374 · Cited by 50 · see citing works
Extracellular matrix and oxidative stress regulate human retinal pigment epithelium growth
Eamegdool, S. S., Sitiwin, E. I., Cioanca, A. V., & Madigan, M. C. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.11.018 · Cited by 45 · see citing works
Protective activity of flavonoid and flavonoid glycosides against glucose-mediated protein damage
Kim, H. Y., Lee, J. M., Yokozawa, T., Sakata, K., & Lee, S. (2010) · Food Chemistry · doi:10.1016/j.foodchem.2010.11.068 · Cited by 42 · see citing works
Hrynets, Y., Ndagijimana, M., & Betti, M. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.02.026 · Cited by 42 · see citing works
Sell, D. R. (1997) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(97)01863-0 · Cited by 42 · see citing works
Plasma Glucose and the Action of Calorie Restriction on Aging
McCarter, R., Mejia, W., Ikeno, Y., Monnier, V. M., Kewitt, K., Gibbs, M. A., McMahan, C. A., & Strong, R. (2007) · The Journals of Gerontology Series A · doi:10.1093/gerona/62.10.1059 · Cited by 41 · see citing works
Self-citationUeda, Y., Miyata, T., Hashimoto, T., Yamada, H., Izuhara, Y., Sakai, H., & Kurokawa, K. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8523 · Cited by 40 · see citing works
Roy, V. K., Chenkual, L., & Gurusubramanian, G. (2015) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2015.11.006 · Cited by 40 · see citing works
Trigonelline and vildagliptin antidiabetic effect: improvement of insulin signalling pathway
Aldakinah, A.-A. A., Al‐Shorbagy, M. Y., Abdallah, D. M., & El-Abhar, H. S. (2017) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12713 · Cited by 39 · see citing works
Aminoguanidine prevented impairment of blood antioxidant system in insulin-dependent diabetic rats
Stoppa, G. R., Cesquini, M., Roman, E. A. F. R., Ogo, S. H., & Torsoni, M. A. (2005) · Life Sciences · doi:10.1016/j.lfs.2005.07.031 · Cited by 39 · see citing works
Jung, Y., Joe, B., Cho, S. J., & Konishi, Y. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2004.12.029 · Cited by 38 · see citing works
Inhibition of glycation reaction in tissue protein incubations by water soluble rutin derivative
Nagasawa, T., Tabata, N., Ito, Y., NISHIZAWA, N., Aiba, Y., & Kitts, D. D. (2003) · Springer eBooks · doi:10.1007/978-1-4419-9236-9_1 · Cited by 37 · see citing works
Mohamadin, A. M., Elberry, A. A., Gawad, H. S. A., Morsy, G. M., & Al-Abbasi, F. A. (2011) · Journal of Lipids · doi:10.1155/2011/167958 · Cited by 35 · see citing works
Lehti, M., Silvennoinen, M., Kivelä, R., Kainulainen, H., & Komulainen, J. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00444.2005 · Cited by 34 · see citing works
Inhibition of glycation reaction in tissue protein incubations by water soluble rutin derivative
Nagasawa, T., Tabata, N., Ito, Y., NISHIZAWA, N., Aiba, Y., & Kitts, D. D. (2003) · Molecular and Cellular Biochemistry · doi:10.1023/a:1024793429244 · Cited by 34 · see citing works
Separation and Analysis of Peptides and Proteins
Hühmer, A. F. R., Aced, G. I., Perkins, M. D., Gürsoy, R. N., JOIS, D. S. S., Larive, C. K., Siahaan, T. J., & Schöneich, C. (1997) · Analytical Chemistry · doi:10.1021/a1970003s · Cited by 34 · see citing works
Sulfhydryl oxidases: sources, properties, production and applications
Faccio, G., Nivala, O., Kruus, K., Büchert, J., & Saloheimo, M. (2011) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-011-3440-y · Cited by 33 · see citing works
Pari, L., & Murugan, P. (2007) · Fundamental and Clinical Pharmacology · doi:10.1111/j.1472-8206.2007.00542.x · Cited by 33 · see citing works
Kwak, S., Giraldo, J. P., Lew, T. T. S., Wong, M. H., Liu, P., Yang, Y. J., Koman, V. B., McGee, M. K., Olsen, B. D., & Strano, M. S. (2018) · Advanced Materials · doi:10.1002/adma.201804037 · Cited by 33 · see citing works
Icodextrin-induced lipid peroxidation disrupts the mesothelial cell cycle engine
Gotloib, L., Wajsbrot, V., & Shostak, A. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01296-0 · Cited by 33 · see citing works
Alternative Medicine in Diabetes - Role of Angiogenesis, Oxidative Stress, and Chronic Inflammation
El‐Refaei, M. F., Abduljawad, S. H., & Alghamdi, A. (2014) · The Review of Diabetic Studies · doi:10.1900/rds.2014.11.231 · Cited by 32 · see citing works
- Authors
- Elgawish, A., Glomb, M., Friedlander, M., & Monnier, V. M.
- Affiliations
- Case Western Reserve University (US)
- Corresponding author
- Monnier, Vincent M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1996-05
- Volume
- 271
- Issue
- 22
- Pages
- 12964-12971
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1981718074
- Cited by
- 201
- References
- 54
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 3 · 2022: 4 · 2021: 2 · 2020: 2 · 2019: 9 · 2018: 5 · 2017: 3 · 2016: 6 · 2015: 8 · 2014: 9 · 2013: 2 · 2012: 9
- FWCI
- 6.59
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Egyptian Cultural and Educational Bureau
- National Institutes of Health (5r01ag005601-13)
- National Institute on Aging (AG 05601)
- National Eye Institute (EY 07099, R01EY007099, 07099)
- Fogarty International Center
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Health Sciences › Medicine › Dermatology › Skin Diseases and Diabetes
- Keywords
- collagen cross-linking, hydrogen peroxide, high glucose, Maillard reaction, glycation, glycoxidation, carboxymethyllysine, Amadori compounds, glycosylamines, superoxide, catalase, oxidative stress, diabetes complications, antioxidants
- MeSH terms
- Animals, Antioxidants, Collagen, Cross-Linking Reagents, Diabetes Mellitus, Experimental, Female, Glucose, Hydrogen Peroxide, Kinetics, Streptozocin, Tendons, Maillard Reaction, Rats, Sprague-Dawley, Oxidative Stress, Rats, In Vitro Techniques
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
