The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Exogenous advanced glycosylation end products induce complex vascular dysfunction in normal animals: a model for diabetic and aging complications.
Open accessAbstract
Advanced glycosylation end products (AGEs) have been implicated in many of the complications of diabetes and normal aging. Markedly elevated vascular tissue and circulating AGEs were linked recently to the accelerated vasculopathy of end-stage diabetic renal disease. To determine the pathogenic role of AGEs in vivo, AGE-modified albumin was administered to healthy nondiabetic rats and rabbits alone or in combination with the AGE-crosslink inhibitor aminoguanidine. Within 2-4 weeks of AGE treatment, the AGE content of aortic tissue samples rose to six times the amount found in controls (P < 0.001). Cotreatment with aminoguanidine limited tissue AGE accumulation to levels two times that of control. AGE administration was associated with a significant increase in vascular permeability, as assessed by 125I label tracer methods. This alteration was absent in animals that received aminoguanidine in addition to AGE. Significant mononuclear cell migratory activity was observed in subendothelial and periarteriolar spaces in various tissues from AGE-treated rats compared to normal cellularity noted in tissues from animals treated with aminoguanidine. Blood pressure studies of AGE-treated rats and rabbits revealed markedly defective vasodilatory responses to acetylcholine and nitroglycerin compared to controls (P < 0.001), consistent with marked NO. inactivation; aminoguanidine treatment significantly prevented this defect. These in vivo data demonstrate directly that AGEs, independent of metabolic or genetic factors, can induce complex vascular alterations resembling those seen in diabetes or aging. AGE administration represents an animal model system for the study of diabetic and aging complications as well as for assessing the efficacy of newly emerging therapies aimed at inhibiting advanced glycosylation.
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Cites
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Advanced Glycosylation End Products in Tissue and the Biochemical Basis of Diabetic Complications
Flier, J. S., Underhill, L. H., Brownlee, M., Cerami, A., & Vlassara, H. (1988) · New England Journal of Medicine · doi:10.1056/nejm198805193182007 · Cited by 2,511
Self-citationBucala, R., Tracey, K. J., & Cerami, A. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115014 · Cited by 1,165
Self-citationAminoguanidine Prevents Diabetes-Induced Arterial Wall Protein Cross-Linking
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Self-citationAdvanced Glycosylation End Products in Patients with Diabetic Nephropathy
Makita, Z., Radoff, S., Rayfield, E. J., Yang, Z., Skolnik, E., Delaney, V., Friedman, E. A., Cerami, A., & Vlassara, H. (1991) · New England Journal of Medicine · doi:10.1056/nejm199109193251202 · Cited by 918
Self-citationBarger, A. C., Beeuwkes, R., Lainey, L. L., & Silverman, K. J. (1984) · New England Journal of Medicine · doi:10.1056/nejm198401193100307 · Cited by 849
Accelerated age-related browning of human collagen in diabetes mellitus.
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Self-citationCachectin/TNF and IL-1 Induced by Glucose-Modified Proteins: Role in Normal Tissue Remodeling
Vlassara, H., Brownlee, M., Manogue, K. R., Dinarello, C. A., & Pasagian, A. (1988) · Science · doi:10.1126/science.3259727 · Cited by 597
Self-citationAminoguanidine treatment inhibits the development of experimental diabetic retinopathy.
Hammes, H. P., Martin, S., Federlin, K., Geisen, K., & Brownlee, M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.24.11555 · Cited by 524
Immunochemical detection of advanced glycosylation end products in vivo.
Makita, Z., Vlassara, H., Cerami, A., & Bucala, R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42741-x · Cited by 491
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Cited by
Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
Thornalley, P. J., LANGBORG, A., & Minhas, H. S. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3440109 · Cited by 1,243
Impaired nitric oxide-mediated vasodilation in patients with non-insulin-dependent diabetes mellitus
Williams, S. B., Cusco, J. A., Roddy, M.-A., Johnstone, M. T., & Creager, M. A. (1996) · Journal of the American College of Cardiology · doi:10.1016/0735-1097(95)00522-6 · Cited by 1,014
Wang (2012) · doi:10.1161/circresaha.111.261388 · Cited by 957
Ting, H. H., Timimi, F. K., Boles, K. S., Creager, S. J., Ganz, P., & Creager, M. A. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118394 · Cited by 871
Koschinsky, T., He, C.-J., Mitsuhashi, T., Bucala, R., Liu, C., Buenting, C., Heitmann, K., & Vlassara, H. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.12.6474 · Cited by 792
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Metadata
- Authors
- Vlassara, H., Fuh, H., Makita, Z., Krungkrai, S., Cerami, A., & Bucala, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1992-12-15
- Volume
- 89
- Issue
- 24
- Pages
- 12043-12047
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2060895623
- Cited by
- 377
- References
- 23
- FWCI
- 7.29
- Type
- journal article
- Language
- en
- Open access
- green
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- Vlassara, H., Fuh, H., Makita, Z., Krungkrai, S., Cerami, A., & Bucala, R. (1992). Exogenous advanced glycosylation end products induce complex vascular dysfunction in normal animals: a model for diabetic and aging complications. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.89.24.12043
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