Structural alterations in rat liver proteins due to streptozotocin-induced diabetes and the recovery effect of selenium: Fourier transform infrared microspectroscopy and neural network study

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Bozkurt O., Bayari S. H., Severcan M., Krafft C., Popp J., Severcan F.

JOURNAL OF BIOMEDICAL OPTICS, vol.17, no.7, 2012 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 17 Issue: 7
  • Publication Date: 2012
  • Doi Number: 10.1117/1.jbo.17.7.076023
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Keywords: diabetes, liver, selenium, protein structure, Fourier transform infrared imaging, Fourier transform infrared microspectroscopy, neural networks, FTIR SPECTROSCOPIC CHARACTERIZATION, SECONDARY STRUCTURE, IR SPECTROSCOPY, MESSENGER-RNA, TISSUE, RAMAN, HEART, HIPPOCAMPUS, HOMEOSTASIS, EXPRESSION
  • Middle East Technical University Affiliated: Yes


The relation between protein structural alterations and tissue dysfunction is a major concern as protein fibrillation and/or aggregation due to structural alterations has been reported in many disease states. In the current study, Fourier transform infrared microspectroscopic imaging has been used to investigate diabetes-induced changes on protein secondary structure and macromolecular content in streptozotocin-induced diabetic rat liver. Protein secondary structural alterations were predicted using neural network approach utilizing the amide I region. Moreover, the role of selenium in the recovery of diabetes-induced alterations on macromolecular content and protein secondary structure was also studied. The results revealed that diabetes induced a decrease in lipid to protein and glycogen to protein ratios in diabetic livers. Significant alterations in protein secondary structure were observed with a decrease in alpha-helical and an increase in beta-sheet content. Both doses of selenium restored diabetes-induced changes in lipid to protein and glycogen to protein ratios. However, low-dose selenium supplementation was not sufficient to recover the effects of diabetes on protein secondary structure, while a higher dose of selenium fully restored diabetes-induced alterations in protein structure. (C) 2012 Society of Photo-Optical Instrumentation Engineers (SPIE). [DOI: 10.1117/1.JBO.17.7.076023]