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Aldo-Keto Reductases: Their Function, Structure and Role in Human Diseases

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 (27 March 2024) | Viewed by 1128

Special Issue Editor


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Guest Editor
Department of Biomedical Sciences, Noorda College of Osteopathic Medicine, Provo, UT 84606, USA
Interests: oxidative stress-induced signal transduction mechanisms; pathophysiology of secondary diabetic complications; carcinogenesis; inflammatory complications; therapeutic development of small molecular inhibitors and antioxidants
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Special Issue Information

Dear Colleagues,

This Special Issue is dedicated to articles focused on aldo-keto reductases (AKRs), investigating their functions, structures, and roles in various human diseases. AKRs, a subset of the NADPH-linked oxidoreductases superfamily, encompass enzymes like aldose reductase, aldehyde reductases, hydroxysteroid dehydrogenases, aflatoxin reductases, and other proteins that reduce a diverse variety of carbonyl compounds. The superfamily comprises 16 families including approximately 200 proteins.

Over the past few decades, research has unveiled the significant involvement of aldo-keto reductases in detoxification and xenobiotic metabolism, as well as lipid and carbohydrate metabolism. Moreover, their impact on human diseases, including diabetes, cancer, and various inflammatory and neurological complications, has been substantiated. The quest for therapeutic solutions has led to the development of aldo-keto reductase inhibitors from both natural and synthetic sources. These inhibitors have undergone evaluation in numerous preclinical and clinical studies, revealing their potential for treating various human diseases, notably inflammatory complications and cancer. Nevertheless, additional preclinical and clinical studies are required to gain a comprehensive understanding of the molecular mechanisms through which AKRs mediate these diseases.

We extend an invitation for contributions to this Special Issue encompassing novel structural and computational studies, functional analyses, preclinical and clinical research, and comprehensive reviews on aldo-keto reductases. The focus lies not only on unraveling the intricacies of AKRs but also on developing potent inhibitors of AKRs characterized by high specificity and minimal adverse effects, which are essential for efficient therapeutic implementation.

Dr. Kota V. Ramana
Guest Editor

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Keywords

  • aldose reductase
  • aldose reductase inhibitors
  • cancer
  • diabetes
  • inflammation
  • molecular modeling

Published Papers (1 paper)

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Research

20 pages, 6729 KiB  
Article
The Effect of Glucose on the Interaction of Bisphenol A and Bovine Hemoglobin Characterized by Spectroscopic and Molecular Docking Techniques
by Xianheng Li, Huan Li, Keqiang Lai and Junjian Miao
Int. J. Mol. Sci. 2023, 24(19), 14708; https://doi.org/10.3390/ijms241914708 - 28 Sep 2023
Viewed by 720
Abstract
The interaction mechanism of hemoglobin (Hb) with bisphenol A (BPA) in diabetic patients and the difference with healthy people have been studied using spectroscopic and molecular docking techniques at several glucose (Glc) concentration, with bovine hemoglobin (BHb) instead of Hb. It is found [...] Read more.
The interaction mechanism of hemoglobin (Hb) with bisphenol A (BPA) in diabetic patients and the difference with healthy people have been studied using spectroscopic and molecular docking techniques at several glucose (Glc) concentration, with bovine hemoglobin (BHb) instead of Hb. It is found that Glc can interact with BHb–BPA and affect its molecular structure, resulting in an altered microenvironment for tyrosine (Tyr) and tryptophan (Trp) in BHb–BPA. It is also found that Glc can bind to BHb alone, and its effect on the molecular structure of BHb is weaker than that on the structure of BHb in BHb–BPA complex. The results of circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) indicate that Glc causes an increase in the content of the α-helix and a decrease in that of the β-sheet of BHb–BPA by 1.5–1.9% and 3.1%, respectively. The results of molecular docking show that Glc binds to BHb–BPA through hydrogen and hydrophobic bonds, and the position of binding differs from that of Glc binding to BHb alone, which may be attributed to the fact that BPA affects the protein molecular structure of BHb and has an effect on the binding of BHb to Glc. This study provides some theoretical basis for the mechanism of BPA toxicity in vivo for people with different blood glucose levels. Full article
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