Prevention and/or Repair of Glycation in Mammalian and Invertebrate

Dear Colleagues,

The purpose of this Special Issue is to map the glycation prevent and/or repair system in mammalians and invertebrates. Glycation is a non-enzymatic reaction discovered by Louis Camille Maillard that occurs between reducing sugars or dicarbonyls (mainly glyoxal and methylglyoxal) and thiol or amino groups of proteins, nucleic acids, and aminolipids. Protein glycation begins with a condensation reaction between carbonyl groups and amino acids, after which a series of dehydrations, oxidations, and rearrangements leads to a myriad of products, including Schiff bases, Amadori products, advanced glycation end-products (AGEs), and protein crosslinks. Glycation results in protein inactivation and aggregation, mutations, and tumorigenesis and is involved in aging, atherosclerosis, hypertension, and neurovegetative, renal, autoimmune, and post-diabetic diseases. Thus, inhibiting any step of glycation can help in the prevention of these diseases. There are several systems for limiting glycation, among them enzymatic activities (glyoxalases, Park7/DJ-1) but also small molecules acting as scavengers of glycating agents. The Special Issue on “Prevention and/or Repair of Glycation in Mammalians and Invertebrates” will include historic reviews of the molecular science behind glycation and original data that focus on defining the following:

- Detoxification of glyoxals by enzymes;

- Scavengers of glycating agents;

- Metabolic syndrome and glycation;

- The enzymes involved in the protection against glycation, i.e., the new targets for anticancer drug development.

Dr. Julien Dairou
Guest Editor

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