Document Type : Original Articles
Authors
1
Cellular and Molecular Research Center, Research Institute for Prevention of Non-Communicable Diseases, Qazvin University of Medical Sciences, Iran.
2
Cellular and Molecular Research Center, Qazvin University of Medical Sciences, Qazvin, Iran.
3
Clinical Pharmacist, Baylor Scott & White Medical Center – Lakeway 100 Medical Pkwy, Lakeway, TX 78738.
4
Cellular and Molecular Research Center, Research Institute for prevention of Non-Communicable Disease, Qazvin University of Medical Sciences, Qazvin, Iran.
5
Department of Clinical Biochemistry, School of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
6
Student Research Committee, School of Paramedical, Qazvin University of Medical Sciences, Qazvin, Iran.
7
Division of Food Safety and Hygiene, Department of Environmental Health Engineering, School of Public Health, Tehran University of Medical Sciences, Tehran, Iran.
10.22092/ari.2025.367353.3379
Abstract
Fibroblast growth factor receptor type II (FGFR2b) is crucial in mediating cellular signal transduction and controlling vital biological processes such as cell growth and differentiation. The disruption or impairment of signaling pathways mediated by this particular receptor has been closely associated with the pathophysiology of various human malignancies, including breast cancer, ovarian cancer, and endometrial cancer. It has been observed that toxic heavy metals, such as Lead, Cadmium, and Aluminum, exert their detrimental effects primarily through the alteration of established signaling pathways within the cellular environment. The primary objective of this research endeavor is to conduct a comprehensive investigation into the effects of the heavy metals Lead (Pb2+), Cadmium (Cd2+), and Aluminum (Al3+) on both the structural integrity and stability of recombinant FGFR2b. The analysis of intrinsic fluorescence emission and circular dichroism (CD) spectra of FGFR2b, when exposed to varying concentrations of these heavy toxic metals, indicated a gradual series of structural fluctuations that corresponded with the increased concentrations of the metals present. Furthermore, the findings from fluorescence and Fourier-transform infrared (FTIR) analysis of the protein structure demonstrated that the influence exerted by Pb2+ at concentrations of 100 and 500 µM was significantly more pronounced and impactful than the effects produced by the other two metals under investigation The structure and stability of FGFR2b as a key receptor in cellular signal transduction were reduced by Pb2+. These results shed light on the effect of toxic heavy metals on the biological functions of the cells via a change in their signaling pathways.
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