advanced glycation end products

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advanced glycation end products



Proteins that have been nonenzymatically modified by the addition of sugar residues to lysine. These altered proteins increase with aging and in patients with hyperglycemia and diabetes mellitus.
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28-31) They also reveal how the deadly effects of advanced glycation end products are related to their ability to promote oxidative stress and inflammation by cross-linking with body proteins, which alters protein structure and function.
Autoantibody against N(epsilon)-(carboxymethyl)lysine: an advanced glycation end product of the Maillard reaction.
This culminates in the formation of advanced glycation end products (AGEs) that cause damage to collagen molecules, leading to wrinkles, creping, and loose skin.
Over the course of several weeks, the early glycation products undergo a series of chemical reactions to become irreversibly cross-linked protein derivatives, referred to as advanced glycation end products.
Cross linking and glycation of connective issue proteins, such as collagen, results in the formation of advanced glycation end products or AGEs, which accumulate with age and induce stiffening of cartilage and the extracellular matrix, resulting in cataracts in the eyes and arthritis in the joints.
Immunohistochemical localization of different epitopes of advanced glycation end products in human atherosclerotic lesions.
RESULTS: Proteins in mouse lung-lining fluid whose expression was consistently altered by As included glutathione-S-transferase (GST)-omega-1, contraspin, apolipoprotein A-I and A-IV, enolase-1, peroxiredoxin-6, and receptor for advanced glycation end products (RAGE).
High levels of advanced glycation end products (AGEs) have been shown to predict cardiovascular complications better than blood sugar levels in patients with diabetes.
Amphoterin can interact with macrophage cell surface receptors for advanced glycation end products to enhance expression of tissue-type plasminogen activator (6).
The research suggests that high consumption of compounds called advanced glycation end products, or AGEs (which form naturally in the body at low levels) can suppress an anti-ageing enzyme known as Sirt1.
This forms advanced glycation end products (commonly shortened, appropriately, to AGEs), which cause protein fibers to become stiff and malformed.

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