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Special Issue "Aldose Reductase: Its 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: 27 March 2024 | Viewed by 306

Special Issue 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 anti-oxidants

Special Issue Information

Dear Colleagues,

This special issue is dedicated to articles related to aldose reductase and its function, structure, and role in various human diseases. Aldose reductase is the first and rate-limiting enzyme that catalyzes the conversion of glucose to sorbitol in the polyol pathway of glucose metabolism. In the past few decades, several studies have shown that aldose reductase causes several secondary diabetic complications, such as diabetic retinopathy, neuropathy, nephropathy, cardiomyopathy, and cataractogenesis via promoting cellular osmotic stress and oxidative stress. Various aldose reductase inhibitors have been developed from natural and synthetic sources and evaluated in several preclinical and clinical studies on diabetic complications. Most of these inhibitors failed in clinical studies for treating secondary diabetic complications. However, only one aldose reductase inhibitor is currently on the market to control diabetic neuropathy in some Asian countries. Further, recent studies have also shown that aldose reductase inhibitors, besides preventing secondary diabetic complications, could also prevent various inflammatory complications such as asthma, sepsis, uveitis, and colon and breast cancers. These studies have indicated the potential therapeutic development of aldose reductase inhibitors for the treatment of inflammatory complications and cancer. However, additional preclinical and clinical studies are required to understand the molecular mechanisms through which the aldose reductase mediates these human diseases. The development of potent inhibitors with high specificity and low adverse effects is necessary for efficient therapeutic implementation. This special issue invites novel structural and computational studies, functional studies, preclinical and clinical research studies, and comprehensive reviews on aldose reductase.

Dr. Kota V. Ramana
Guest Editor

Manuscript Submission Information

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

Published Papers (1 paper)

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The Effect of Glucose on the Interaction of Bisphenol A and Bovine Hemoglobin Characterized by Spectroscopic and Molecular Docking Techniques
Int. J. Mol. Sci. 2023, 24(19), 14708; https://doi.org/10.3390/ijms241914708 - 28 Sep 2023
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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
(This article belongs to the Special Issue Aldose Reductase: Its Function, Structure and Role in Human Diseases)
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