An agent cleaving glucose-derived protein crosslinks in vitro and in vivo

@article{Vasan1996AnAC,
  title={An agent cleaving glucose-derived protein crosslinks in vitro and in vivo},
  author={S. Vasan and X. Zhang and Xini Zhang and A. Kapurniotu and J. Bernhagen and S. Teichberg and J. Basgen and D. Wagle and David Shih and Ihor Terlecky and R. Bucala and A. Cerami and J. Egan and P. Ulrich},
  journal={Nature},
  year={1996},
  volume={382},
  pages={275-278}
}
GLUCOSE and other reducing sugars react with proteins by a non-enzymatic, post-translational modification process called non-enzymatic glycosylation or glycation. The sugar-derived carbonyl group adds to a free amine, forming a reversible adduct which over time rearranges to produce a class of products termed advanced-glycation end-products (AGEs). These remain irreversibly bound to macromolecules and can covalently crosslink proximate amino groups1,2. The formation of AGEs on long-lived… Expand
Potential clinical utility of advanced glycation end product cross-link breakers in age- and diabetes-associated disorders.
TLDR
The potential clinical utility of AGE cross-link breakers in the prevention and management of age- and diabetes-associated disorders is summarized. Expand
Therapeutic potential of breakers of advanced glycation end product-protein crosslinks.
TLDR
This review presents the pre-clinical and clinical studies using ALT-711, a highly potent AGE-crosslink breaker that has the ability to reverse already-formed AGEs, and the therapeutic potential of crosslink breakers for cardiovascular complications and dermatological alterations associated with aging and diabetes. Expand
In Vitro Kinetic Studies of Formation of Antigenic Advanced Glycation End Products (AGEs)
TLDR
The mechanism-based approach to the study of AGE inhibition appears promising for the design and discovery of novel post-Amadori AGE inhibitors of therapeutic potential that may complement others, such as aminoguanidine, known to either prevent initial sugar attachment or to scavenge highly reactive dicarbonyl intermediates. Expand
Advanced glycation endproducts: what is their relevance to diabetic complications?
TLDR
Increasing expression of enzymes of the enzymatic defence against glycation provides a novel and potentially effective future therapeutic strategy to suppress protein glycation. Expand
Advanced Glycation End-Product Cross-Link Breakers
TLDR
Alagebrium is the first drug in a new class of thiazolium therapeutic agents that break established AGE cross-links between proteins and was effective in improving cardiac function and uncontrolled systolic blood pressure, particularly in more severely affected patients. Expand
Advanced Glycation Endproduct Crosslinking in the Cardiovascular System
TLDR
The accumulation of AGEs may help to explain the increased cardiac risk associated with aging as well as diabetes mellitus and hypertension, two conditions that accelerate and enhance AGE formation. Expand
The role of advanced glycation end products in various types of neurodegenerative disease: a therapeutic approach
TLDR
Several new therapeutic approaches that have been applied to treat these devastating disorders, including the use of various synthetic and naturally occurring inhibitors are discussed, including modulation of the AGE-RAGE axis is considered promising in the prevention of neurodegenerative diseases. Expand
Significance of Advanced Glycation End Products in Aging-Related Disease
Carbohydrates are indispensable nutrients for life. However, due to the presence of a carbonyl group, reducing sugars such as glucose react non-enzymatically with amino groups on proteins inExpand
Chlorogenic acid inhibits the formation of advanced glycation end products and associated protein cross-linking
TLDR
In vitro results suggest that CGA could be beneficial in the prevention of AGEs progression in patients with diabetes because CGA can attenuate A GEs deposition in glucose. Expand
Naturally occurring inhibitors against the formation of advanced glycation end-products.
TLDR
The Maillard reaction, the formation process of AGEs and harmful effects of A GEs to human health are introduced and typical effective AGE inhibitors with different inhibition mechanisms are reviewed in this paper. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 26 REFERENCES
Immunochemical detection of advanced glycosylation end products in vivo.
TLDR
It is suggested that tissue AGEs which form in vivo appear to contain a common immunological epitope which cross-reacts with A GEs prepared in vitro, supporting the concept that immunologically similar AGE structures form from the incubation of sugars with different proteins. Expand
Lipid advanced glycosylation: pathway for lipid oxidation in vivo.
TLDR
Data support the concept that AGE oxidation plays an important and perhaps primary role in initiating lipid oxidation in vivo, and increased levels of both apoprotein- and lipid-linked AGEs when compared to specimens obtained from normal, nondiabetic controls. Expand
Advanced glycation end products contribute to amyloidosis in Alzheimer disease.
TLDR
The results suggest that the in vivo half-life of beta-amyloid is prolonged in AD, resulting in greater accumulation of AGE modifications which in turn may act to promote accumulation of additional amyloid. Expand
Exogenous advanced glycosylation end products induce complex vascular dysfunction in normal animals: a model for diabetic and aging complications.
TLDR
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. Expand
Hemoglobin-AGE: a circulating marker of advanced glycosylation.
TLDR
Hb-AGE measurements may provide an index of long-term tissue modification by AGEs and prove useful in assessing the contribution of advanced glycosylation to a variety of diabetic and age-related complications. Expand
Advanced Glycation Endproducts Promote Adhesion Molecule (VCAM-1, ICAM-1) Expression and Atheroma Formation in Normal Rabbits
TLDR
In vivo evidence for a causal relationship between chronic AGE accumulation and atherosclerosis independent of diabetic hyperglycemia is provided, and the utility of this animal model for the study of diabetic vascular disease in relation to glycation is suggested. Expand
Advanced Maillard reaction end products are associated with Alzheimer disease pathology.
  • M. Smith, S. Taneda, +6 authors G. Perry
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1994
TLDR
Evidence is presented that antibodies against two Maillard end products, pyrraline and pentosidine, immunocytochemically label neurofibrillary tangles and senile plaques in brain tissue from patients with Alzheimer disease contain modifications typical of advanced Maillard reaction end products. Expand
Nonenzymatic glucosylation and glucose-dependent cross-linking of protein.
TLDR
A model system using RNase A has been established for studying the nonenzymatic glucosylation and glucose-dependent cross-linking of protein (Maillard reaction) under physiological conditions in vitro and the relevance of this reaction to the pathophysiology of diabetes is discussed. Expand
Accelerated age-related browning of human collagen in diabetes mellitus.
  • V. Monnier, R. Kohn, A. Cerami
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1984
TLDR
Collagen adducts from aged and diabetic individuals had absorption and fluorescence spectra identical to those of collagen samples that underwent nonenzymatic browning with glucose in vitro, suggesting their likely occurrence throughout the body could explain the correlation between arterial stiffening, decreased joint mobility, and the severity of microvascular complications in type I diabetics. Expand
Endothelial receptor-mediated binding of glucose-modified albumin is associated with increased monolayer permeability and modulation of cell surface coagulant properties
TLDR
The interaction of AGE- modified proteins with endothelium may play an important role in the early stages of increased vascular permeability, as well as vessel wall- related abnormalities of the coagulation system, characteristic of diabetes and aging. Expand
...
1
2
3
...