Comparative proteomic analysis of primary mouse liver c-Kit−(CD45/TER119)− stem/progenitor cells

2007 ◽  
Vol 102 (4) ◽  
pp. 936-946 ◽  
Author(s):  
Yu-Fei He ◽  
Yin-Kun Liu ◽  
Hao-Jie Lu ◽  
Jun Chen ◽  
Peng-Yuan Yang
2018 ◽  
Vol 1 (1) ◽  
pp. e00007 ◽  
Author(s):  
O.A. Buneeva ◽  
A.T. Kopylov ◽  
V.G. Zgoda ◽  
A.E. Medvedev

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.


Biomaterials ◽  
2013 ◽  
Vol 34 (6) ◽  
pp. 1669-1685 ◽  
Author(s):  
Jumi Kim ◽  
Young-Joo Jeon ◽  
Hye Eun Kim ◽  
Jeong Min Shin ◽  
Hyung Min Chung ◽  
...  

Stem Cells ◽  
2004 ◽  
Vol 22 (6) ◽  
pp. 1003-1014 ◽  
Author(s):  
Wen Tao ◽  
Mu Wang ◽  
Emily D. Voss ◽  
Ross R. Cocklin ◽  
Jaime A. Smith ◽  
...  

2021 ◽  
Vol 22 (12) ◽  
pp. 6323
Author(s):  
Alexander L. Rusanov ◽  
Peter M. Kozhin ◽  
Olga V. Tikhonova ◽  
Victor G. Zgoda ◽  
Dmitry S. Loginov ◽  
...  

In vitro models are often used for studying macrophage functions, including the process of phagocytosis. The application of primary macrophages has limitations associated with the individual characteristics of animals, which can lead to insufficient standardization and higher variability of the obtained results. Immortalized cell lines do not have these disadvantages, but their responses to various signals can differ from those of the living organism. In the present study, a comparative proteomic analysis of immortalized PMJ2-R cell line and primary peritoneal macrophages isolated from C57BL/6 mice was performed. A total of 4005 proteins were identified, of which 797 were quantified. Obtained results indicate significant differences in the abundances of many proteins, including essential proteins associated with the process of phagocytosis, such as Elmo1, Gsn, Hspa8, Itgb1, Ncf2, Rac2, Rack1, Sirpa, Sod1, C3, and Msr1. These findings indicate that outcomes of studies utilizing PMJ2-R cells as a model of peritoneal macrophages should be carefully validated. All MS data are deposited in ProteomeXchange with the identifier PXD022133.


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