Advanced glycation end products (AGEs) are non-enzymatic post-translational modifications of proteins that can accumulate to high concentrations and contribute to the decline of body tissues. A lead biocatalyst has been discovered to reverse the AGE modifications in vitro which could be further developed to enable a better understanding of AGEs ...

2022年1月25日 · Scientists have found that a number of nutritional components in the diet play a very important role in controlling glycation and even reversing it! These compounds include: Carnosine a combination of two amino acids beta-alanine and histidine.

2019年5月2日 · Advanced glycation end products (AGEs) are harmful compounds that are created when proteins or fats combine with sugars in the bloodstream in a process known as glycation. AGEs can also be encountered in foods, and foods that have been exposed to high temperatures, such as in grilling or frying, tend to be high in these compounds.

2019年9月16日 · Herein, we show that MnmC, an enzyme involved in a bacterial tRNA-modification pathway, is capable of reversing the AGEs carboxyethyl-lysine (CEL) and carboxymethyl-lysine (CML) back to their native lysine structure.

2021年6月3日 · In peptide 1, glycation drops by 19.3% over 48 hpd, which we attribute to the reversal of glycation.

1999年1月1日 · It is now well established in vivo that early glycation products progress over time to irreversibly bound cross-links termed advanced glycation endproducts (AGEs), which in turn have been implicated in the development of many of the pathological sequelae of diabetes and aging, such as atherosclerosis and renal insufficiency. 5 Evidence for a ...

1999年1月1日 · Enhanced formation and accumulation of advanced glycation end products (AGEs) have been proposed to play a major role in the pathogenesis of diabetic complications, and atherosclerosis, leading to the development of a range of diabetic complications including nephropathy, retinopathy and neuropathy.

Pharmacological reversal of advanced glycation end-product-mediated protein crosslinking. It is well known that glucose reacts non-enzymati- cally with protein amino groups with eventual forma- tion of covalent protein-protein crosslinks, which are called advanced glycation end-products (AGEs) [1].

2019年4月23日 · Here, we show that MnmC, an enzyme involved in a bacterial tRNA‐modification pathway, is capable of reversing the AGEs carboxyethyl‐lysine (CEL) and carboxymethyl‐lysine (CML) back to their...

Advanced glycation end products: detection and reversal. Advanced glycation end products: detection and reversal Methods Enzymol. 1999:309:152-72. doi: 10.1016/s0076-6879(99)09013-8. Authors Y al-Abed 1 , A Kapurniotu, R Bucala. Affiliation 1 Picower Institute for Medical ...