General Information:

Id: 2,088 (click here to show other Interactions for entry)
Diseases: Diabetes mellitus, type II - [OMIM]
Insulin resistance
Mammalia
review
Reference: Schmidt AM et al.(1999) Activation of receptor for advanced glycation end products: a mechanism for chronic vascular dysfunction in diabetic vasculopathy and atherosclerosis. Circ. Res. 84: 489-497 [PMID: 10082470]

Interaction Information:

Comment In the setting of hyperglycemia, nonenzymatic glycoxidation results from the interaction of aldoses, such as glucose, with free amino groups on polypeptides or lipids. Formation of early glycation end products, such as Schiff bases and Amadori products, the best-known of which is hemoglobin A1c, is reversible. Further molecular rearrangements, often involving oxidation, eventuate in the formation of advanced glycation end products (AGEs).
Formal Description
Interaction-ID: 16827

phenotype

hyperglycemia

increases_quantity of

drug/chemical compound

Advanced glycation end-product

Comment Although AGEs may have been previously considered to be restricted to diabetes, it is now recognized that oxidation alone can lead to AGE formation and AGEs have been identified in atherosclerotic tissues without diabetes.
Formal Description
Interaction-ID: 16837

increases_quantity of

drug/chemical compound

Advanced glycation end-product

Comment In the endothelium, AGEs diminish vascular barrier function, enhance expression of vascular cell adhesion molecule-1 (VCAM-1), quench nitric oxide, and alter the balance of cellular coagulant properties, in part through induction of procoagulant tissue factor.
Formal Description
Interaction-ID: 16838

drug/chemical compound

Advanced glycation end-product

affects_activity of

Comment In the endothelium, AGEs diminish vascular barrier function, enhance expression of vascular cell adhesion molecule-1 (VCAM-1), quench nitric oxide, and alter the balance of cellular coagulant properties, in part through induction of procoagulant tissue factor.
Formal Description
Interaction-ID: 16839

drug/chemical compound

Advanced glycation end-product

increases_expression of

gene/protein

VCAM1

Drugbank entries Show/Hide entries for VCAM1
Comment In the endothelium, AGEs diminish vascular barrier function, enhance expression of vascular cell adhesion molecule-1 (VCAM-1), quench nitric oxide, and alter the balance of cellular coagulant properties, in part through induction of procoagulant tissue factor.
Formal Description
Interaction-ID: 16840

drug/chemical compound

Advanced glycation end-product

affects_quantity of

drug/chemical compound

NO

Comment In the endothelium, AGEs diminish vascular barrier function, enhance expression of vascular cell adhesion molecule-1 (VCAM-1), quench nitric oxide, and alter the balance of cellular coagulant properties, in part through induction of procoagulant tissue factor.
Formal Description
Interaction-ID: 16841

drug/chemical compound

Advanced glycation end-product

affects_activity of

process

coagulation

Comment In the endothelium, AGEs diminish vascular barrier function, enhance expression of vascular cell adhesion molecule-1 (VCAM-1), quench nitric oxide, and alter the balance of cellular coagulant properties, in part through induction of procoagulant tissue factor.
Formal Description
Interaction-ID: 16842

drug/chemical compound

Advanced glycation end-product

increases_expression of

gene/protein

F3

Drugbank entries Show/Hide entries for F3
Comment Receptor for advanced glycation end products (RAGE) is a member of the immunoglobulin superfamily of cell surface molecules and engages diverse ligands relevant to distinct pathological processes. One class of RAGE ligands includes glycoxidation products, termed advanced glycation end products, which occur in diabetes, at sites of oxidant stress in tissues, and in renal failure and amyloidoses.
Formal Description
Interaction-ID: 16844

drug/chemical compound

Advanced glycation end-product

interacts (colocalizes) with

gene/protein

AGER

Comment Receptor for advanced glycation end products (RAGE) is a member of the immunoglobulin superfamily of cell surface molecules and engages diverse ligands relevant to distinct pathological processes. One class of RAGE ligands includes glycoxidation products, termed advanced glycation end products, which occur in diabetes, at sites of oxidant stress in tissues, and in renal failure and amyloidoses.
Formal Description
Interaction-ID: 16852

increases_quantity of

drug/chemical compound

Advanced glycation end-product