Braga Camila Pereira, Vieira José Cavalcante Souza, Grove Ryan A, Boone Cory H T, Leite Aline de Lima, Buzalaf Marília Afonso Rabelo, Fernandes Ana Angélica Henrique, Adamec Jiri, Padilha Pedro de Magalhaes
Department of Chemistry and Biochemistry, Institute of Bioscience of Botucatu, São Paulo State University, Botucatu, SP, Brazil.
Department of Chemistry and Biochemistry, Institute of Bioscience of Botucatu, São Paulo State University, Botucatu, SP, Brazil.
Int J Biol Macromol. 2017 Mar;96:817-832. doi: 10.1016/j.ijbiomac.2016.12.073. Epub 2017 Jan 3.
Proteins play crucial roles in biological systems, thus studies comparing the protein pattern present in a healthy sample with an affected sample have been widely used for disease biomarker discovery. Although proteins containing metal ions constitute only a small proportion of the proteome, they are essential in a multitude of structural and functional processes. The correct association between metal ions and proteins is essential because this binding can significantly interfere with normal protein function. Employment of a metalloproteomic study of liver samples from diabetic rats permitted determination of the differential abundance of copper-, selenium-, zinc- and magnesium-associated proteins between diabetic, diabetic treatment with insulin and non-diabetic rats. Proteins were detected by ESI-MS/MS. Seventy-five different proteins were found with alterations in the metal ions of interest. The most prominent pathways affected under the diabetic model included: amino-acid metabolism and its derivates, glycogen storage, metabolism of carbohydrates, redox systems and glucose metabolism. Overall, the current methods employed yielded a greater understanding of metal binding and how type 1 diabetes and insulin treatment can modify some metal bonds in proteins, and therefore affect their mechanism of action and function.
