A proteomic approach to identify metalloproteins and metal-binding proteins in liver from diabetic rats

作者：Braga Camila Pereira^*; Souza Vieira Jose Cavalcante; Grove Ryan A; Boone Cory H T; Leiter Aline de Lima; Rabelo Buzalaf Marilia Afonso; Henrique Fernandes Ana Angelica; Adamec Jiri; Padilha Pedro de Magalhaes

来源：International Journal of Biological Macromolecules, 2017, 96: 817-832.

DOI：10.1016/j.ijbiomac.2016.12.073

• Electrospray ionization-tandem mass spectrometry
• Flame atomic absorption spectrometry
• Graphite furnace atomic absorption spectrometry
• Metalloproteomic
• Type 1 diabetes
• Two-dimensional electrophoresis

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.

• 出版日期2017-3