TY - JOUR
T1 - A proteomic approach to identify metalloproteins and metal-binding proteins in liver from diabetic rats
AU - Braga, Camila Pereira
AU - Vieira, José Cavalcante Souza
AU - Grove, Ryan A.
AU - Boone, Cory H.T.
AU - Leite, Aline de Lima
AU - Buzalaf, Marília Afonso Rabelo
AU - Fernandes, Ana Angélica Henrique
AU - Adamec, Jiri
AU - Padilha, Pedro de Magalhaes
N1 - Publisher Copyright:
© 2017 Elsevier B.V.
PY - 2017/3/1
Y1 - 2017/3/1
N2 - 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.
AB - 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.
KW - Electrospray ionization-tandem mass spectrometry
KW - Flame atomic absorption spectrometry
KW - Graphite furnace atomic absorption spectrometry
KW - Metalloproteomic
KW - Two-dimensional electrophoresis
KW - Type 1 diabetes
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U2 - 10.1016/j.ijbiomac.2016.12.073
DO - 10.1016/j.ijbiomac.2016.12.073
M3 - Article
C2 - 28057574
AN - SCOPUS:85008613382
SN - 0141-8130
VL - 96
SP - 817
EP - 832
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -