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

• Autor(a) principal: Braga, Camila Pereira [UNESP]
• Data de Publicação: 2017
• Outros Autores: Souza Vieira, Jose Cavalcante [UNESP], Grove, Ryan A., Boone, Cory H. T., Leiter, Aline de Lima, Rabelo Buzalaf, Marilia Afonso, Henrique Fernandes, Ana Angelica [UNESP], Adamec, Jiri, Padilha, Pedro de Magalhaes [UNESP]
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UNESP
• Texto Completo: http://dx.doi.org/10.1016/j.ijbiomac.2016.12.073; http://hdl.handle.net/11449/162416
• topic: 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. (C) 2017 Elsevier B.V. All rights reserved.