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Prevention and/or Repair of Glycation in Mammalian and Invertebrate

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (31 March 2021) | Viewed by 4894

Special Issue Editor


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Guest Editor
Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologique, Université de Paris, UMR 8601, CNRS, F-75013 Paris, France
Interests: glycation; Park7; enzymology; toxicology; analytical chemistry; oxidative stress; xenobiotic; metabolism
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Special Issue Information

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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Keywords

  • Glycation
  • Methylglyoxal/Glyoxal
  • Glyoxalases
  • Park7/DJ-1
  • Advanced glycation end products (AGEs)
  • Maillard reaction
  • Protein glycation
  • DNA and protein repair
  • Scavengers
  • Enzymology

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Published Papers (1 paper)

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Research

20 pages, 7912 KiB  
Article
A Potential Role for Fructosamine-3-Kinase in Cataract Treatment
by Sander De Bruyne, Loes van Schie, Jonas Himpe, Filip De Somer, Inge Everaert, Wim Derave, Caroline Van den Broecke, Manon Huizing, Nezahat Bostan, Marijn Speeckaert, Nico Callewaert, Elisabeth Van Aken and Joris R. Delanghe
Int. J. Mol. Sci. 2021, 22(8), 3841; https://doi.org/10.3390/ijms22083841 - 7 Apr 2021
Cited by 13 | Viewed by 4125
Abstract
Cataracts are the major cause of blindness worldwide, largely resulting from aging and diabetes mellitus. Advanced glycation end products (AGEs) have been identified as major contributors in cataract formation because they alter lens protein structure and stability and induce covalent cross-linking, aggregation, and [...] Read more.
Cataracts are the major cause of blindness worldwide, largely resulting from aging and diabetes mellitus. Advanced glycation end products (AGEs) have been identified as major contributors in cataract formation because they alter lens protein structure and stability and induce covalent cross-linking, aggregation, and insolubilization of lens crystallins. We investigated the potential of the deglycating enzyme fructosamine-3-kinase (FN3K) in the disruption of AGEs in cataractous lenses. Macroscopic changes of equine lenses were evaluated after ex vivo intravitreal FN3K injection. The mechanical properties of an equine lens pair were evaluated after treatment with saline and FN3K. AGE-type autofluorescence (AF) was measured to assess the time-dependent effects of FN3K on glycolaldehyde-induced AGE-modified porcine lens fragments and to evaluate its actions on intact lenses after in vivo intravitreal FN3K injection of murine eyes. A potential immune response after injection was evaluated by analysis of IL-2, TNFα, and IFNγ using an ELISA kit. Dose- and time-dependent AF kinetics were analyzed on pooled human lens fragments. Furthermore, AF measurements and a time-lapse of macroscopic changes were performed on intact cataractous human eye lenses after incubation with an FN3K solution. At last, AF measurements were performed on cataractous human eyes after crossover topical treatment with either saline- or FN3K-containing drops. While the lenses of the equine FN3K-treated eyes appeared to be clear, the saline-treated lenses had a yellowish-brown color. Following FN3K treatment, color restoration could be observed within 30 min. The extension rate of the equine FN3K-treated lens was more than twice the extension rate of the saline-treated lens. FN3K treatment induced significant time-dependent decreases in AGE-related AF values in the AGE-modified porcine lens fragments. Furthermore, in vivo intravitreal FN3K injection of murine eyes significantly reduced AF values of the lenses. Treatment did not provoke a systemic immune response in mice. AF kinetics of FN3K-treated cataractous human lens suspensions revealed dose- and time-dependent decreases. Incubation of cataractous human eye lenses with FN3K resulted in a macroscopic lighter color of the cortex and a decrease in AF values. At last, crossover topical treatment of intact human eyes revealed a decrease in AF values during FN3K treatment, while showing no notable changes with saline. Our study suggests, for the first time, a potential additional role of FN3K as an alternative treatment for AGE-related cataracts. Full article
(This article belongs to the Special Issue Prevention and/or Repair of Glycation in Mammalian and Invertebrate)
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