Abstract
In recent years, there has been a progress in the study of glycation reaction which is one the possible reason for multiple metabolic disorders. Glycation is a nonenzymatic reaction between nucleic acids, lipids, and proteins resulting into the formation of early glycation products that may further lead to the accumulation of advanced glycation end products (AGEs). The precipitation of AGEs in various cells, tissues, and organs is one of the factors for the initiation and progression of various metabolic derangements including the cancer. The AGE interaction with its receptor “RAGE” activates the inflammatory pathway; yet, the downregulation of RAGE and its role in these pathways are not clear. We explore the effect of anticancer novel nanoassemblies on AGEs to determine its role in the regulation of the expression of RAGE, NFƙB, TNF-α, and IFN-γ. This paper is based on the in vivo and in vitro study in glycation and lung cancer model systems. Upon the treatment of nanoassemblies in both the model systems, we observed a protective effect of nanoassemblies over the inhibition of glycative and oxidative stress via mRNA expression analysis. The mRNA expression results corroborated with the reactive oxygen species (ROS), carboxy-methyl-lysine (CML), and fluorescence studies. In this study, we found that the presence of common factors for glycation and lung cancer is oxidative and glycative stress. This oxidation and glycation might be responsible for the initiation of inflammation which may further lead to uncontrolled growth of cells leading to cancer. This can be a strong association between lung cancer and glycation reaction. The intervention of the anticancer and antiglycation effects of multimodal nanoassemblies throughout the study promises a new pathway for cancer research.
Highlights
Glycation is the nonenzymatic reaction between free amino groups of proteins and nucleic acids and free carbonyl groups of reducing sugars which damage or alter the protein structure and functions [1,2,3,4,5,6]
Hi-SYBr Master Mix, Agarose, Tris buffer, ethidium bromide, bromophenol blue, Protein Estimation Kit (G Biosciences), DNPH, methylglyoxal, bovine serum albumin, phosphate buffer saline (PBS), antibiotic antimycotic solution, and trypsin, glucometer (One Touch Select simple), 0.2 μm syringe filter (Sartorius), DCFDA dye, nitrosodiethylamine, alloxan monohydrate, UV-spectrophotometer (Eppendorf), spectrofluorometer (Agilent technologies, Carry Eclipse), phenobarbitone (Abbot), RPMI (Cell Clone), fetal bovine serum (Gibco), and RNA later (Invitrogen)
The level of Fasting blood glucose (FBG) was measured as a strong factor in the glycation animal model
Summary
Glycation is the nonenzymatic reaction between free amino groups of proteins and nucleic acids and free carbonyl groups of reducing sugars which damage or alter the protein structure and functions [1,2,3,4,5,6]. The damage caused to biological macromolecules through glycation and its final product, advanced glycation end products (AGEs), is the focal point of this study which leads to multiple metabolic disorders. AGEs are responsible for many diseases like, diabetes, ageing, and neurological disorders. Previous studies have shown that AGEs are responsible for lung, breast, prostate, liver and head and neck cancer [7,8,9,10]. The nanoparticle-based drug delivery systems have unique properties as compared with traditional drug formulations. Nowadays, these are being extensively used in the treatment of diseases, such as diabetes, cardiovascular diseases, and cancer [15, 16]. We used multifunctional nanoassemblies using perfluoroaryl-labelled albumin (PFT-Hcy-HSA) with a fluorescent dye (Cy7) and BioMed Research International
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