Biomedical Chemistry: Research and Methods, 2018, 1(1), e00007

Comparative proteomic analysis of mouse liver and brain isatin-binding proteins

O.A. Buneeva *, A.T.Kopylov, V.G.Zgoda, A.E .Medvedev

Institute of Biomedical Chemistry, 10 Pogodinskaya str., Moscow, 119121 Russia; *e-mail: olbuneeva@gmail.com

Keywords: isatin, isatin-binding proteins, brain and liver, proteomic profiling, 5-aminocaproyl-isatin

DOI:10.18097/BMCRM00007

The whole version of this paper is available in Russian.

Isatin (indol-2,3-dione) is an endogenous indole, exhibiting various biological activities that are realized via its interacts with numerous target proteins (so-called isatin-binding proteins). To date, isatin-binding proteins have been characterized in the brain of mice and rats. In this study we have performed a comparative proteomic analysis of the isatin-binding proteins of the mouse liver and brain. Proteomic profiling of clarified lysates of membrane and soluble fractions of liver and brain homogenates was performed using 5-aminocaproyl-isatin as an affinity ligand. During affinity based separation of isatin-binding proteins of soluble and membrane fractions of mouse brain homogenates lysed with Triton X-100, 63 individual proteins were identified. A similar separation of mouse liver homogenate fractions during affinity chromatography resulted in identification of 80 proteins. All identified liver and brain proteins belonged to the following functional groups: (I) Carbohydrate metabolism and energy generation; (II) Lipid metabolism; (III) Metabolism of nucleotides and amino acids; (IV) Formation of the cytoskeleton, exocytosis; (V) Regulation of gene expression, cell division and differentiation; (VI) Antioxidant and protective proteins; (VII) Signal transmission and regulation of enzyme activity. The total number of isatin-binding proteins common for the brain and liver was only 12. The most common for the brain and liver of isatin-binding proteins was found in group VI (antioxidant and protective proteins), complete absence of coincidence in group II (lipid metabolism) and group IV (formation of the cytoskeleton, exocytosis). The observed differences in the profile of isatin-binding proteins appear to play an important role in the specific effects of isatin in certain organs.

Figure 1. Experimental design for proteomic profiling of mouse liver and brain isatin-binding proteins

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Table 1. Comparison of proteomic profiles of mouse brain and liver isatin-binding proteins

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Table 2. The list of identified isatin-binding proteins and their annotation in the GO terms

ACKNOWLEDGEMENTS

This work was performed within the framework of the Program for Basic Research of State Academies of Sciences for 2013-2020 (proteomic analysis of isatin binding proteins).

The mass spectrometry analysis was performed using the “Human Proteome” Core Facility (Institute of Biomedical Chemistry, Moscow) supported by the Ministry of Education and Science of the Russian Federation (agreement no. 14.621.21.0017; a unique project identifier RFMEFI62117X0017).

SUPPLEMENTARY

Supplementary materials are available at http://dx.doi.org/10.18097/BMCRM00007

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