Identification of breast cancer metastasis-associated proteins in an isogenic tumor metastasis model using two-dimensional gel electrophoresis and liquid chromatography-ion trap-mass spectrometry

PROTEOMICS ◽  
2006 ◽  
Vol 6 (11) ◽  
pp. 3352-3368 ◽  
Author(s):  
Da-Qiang Li ◽  
Lei Wang ◽  
Fei Fei ◽  
Yi-Feng Hou ◽  
Jian-Min Luo ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Tumor Metastasis ◽  
Cancer Metastasis ◽  
Ion Trap ◽  
Breast Cancer Metastasis ◽  
Ion Trap Mass Spectrometry ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Associated Proteins ◽  
Metastasis Model

Identification of secreted and surface proteins from Enterococcus faecalis

2009 ◽  
Vol 55 (8) ◽  
pp. 967-974 ◽  
Author(s):  
Abdellah Benachour ◽  
Thierry Morin ◽  
Laurent Hébert ◽  
Aurélie Budin-Verneuil ◽  
André Le Jeune ◽  
...  
Keyword(s):  
Cell Surface ◽  
Enterococcus Faecalis ◽  
Virulence Factors ◽  
Gel Electrophoresis ◽  
Ion Trap ◽  
Surface Proteins ◽  
Two Dimensional Gel Electrophoresis ◽  
Proteomic Approach ◽  
Associated Proteins

Secreted and surface proteins of bacteria are key molecules that interface the cell with the environment. Some of them, corresponding to virulence factors, have already been described for Enterococcus faecalis , the predominant species involved in enterococcal nosocomial infections. In a global proteomic approach, the identification of the most abundant secreted and surface-associated proteins of E. faecalis JH2-2 strain was carried out. These proteins were separated by gel electrophoresis or directly subjected to in vivo trypsinolysis and then analyzed by liquid chromatography – electrospray ion trap tandem mass spectrometry. Putative functions were assigned by homology to the translated genomic database of E. faecalis. A total of 44 proteins were identified, eight secreted proteins from the supernatant culture and 38 cell surface proteins from two-dimensional gel electrophoresis and in vivo trypsinolysis among which two are common to the two groups. Their sequences analysis revealed that 35 of the 44 proteins harbour characteristic features (signal peptide or transmembrane domains) consistent with an extracellular localization. This study may be considered as an important step to encourage proteomic-based investigations of E. faecalis cell surface associated proteins that could lead to the discovery of virulence factors and to the development of new therapeutic tools.

scholarly journals RNA-seq and two-dimensional gel electrophoresis revealed genomic and proteomic signatures during bacteriophage-host interactions in Pseudomonas aeruginosa

2019 ◽  
Author(s):  
Yinling Tan ◽  
Qiu Zhong ◽  
Xia Zhao ◽  
Canhuang Chen ◽  
Yang Li ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Gel Electrophoresis ◽  
Phage Infection ◽  
Two Dimensional ◽  
Rna Seq ◽  
Two Dimensional Gel Electrophoresis ◽  
Host Interactions ◽  
Associated Proteins ◽  
Infection Processes ◽  
Lysogenic Phage

Abstract Background Understanding the biological nature of bacteriophage is important in exploring the therapeutic and biotechnological potentials of bacteriophages. However, available information is limited to the infection processes on either model phages infecting Escherichia coli or lytic phages against pathogens. The interplay between lysogenic phage and its host was rarely studied. Results We investigated the interactions between Pseudomonas aeruginosa and a lysogenic bacteriophage PaP3 through RNA-seq and two-dimensional gel electrophoresis (2D-GE). Compared to the uninfected host, a total of 2,891 (51.3%) differentially expressed genes (DGEs) were identified, most of which were repressed by phages, including the changes in metabolic-related and virulence-associated genes. The RT-qPCR results showed consistent directional changes compared with the RNA-seq results. According to 2D-GE, phage structure proteins were detected after phage infection. The host proteins, such as flagella hook-associated proteins, disappeared gradually after phage infection and may be shut off by phage. Conclusions All these indicate that although lysogenic phages do not immediately lyse the host, they play a significant regulatory role in the expression of host genes. Our findings provide an expanded view of the lysogenic phage infection processes and may offer potential targets for therapeutic intervention against P. aeruginosa infections.

Age- and ploidy-related changes in rat liver nuclear proteins as assessed by one- and two-dimensional gel electrophoresis

1982 ◽  
Vol 60 (3) ◽  
pp. 204-214 ◽  
Author(s):  
Klaus Brasch
Keyword(s):  
Gel Electrophoresis ◽  
Minor Component ◽  
Subsequent Stage ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Nonhistone Proteins ◽  
Stage Of Development ◽  
Age Related ◽  
Associated Proteins ◽  
A Minor

Hepatocyte nuclei from young (3–5 week), mature (8–12 week), and aged (over 32 weeks) rats were isolated and characterized by flow cytometry. Nuclei were bulk separated into diploid (2C), tetraploid (4C), and octoploid (8C) enriched fractions on sucrose gradients. Total, 0.35 M NaCl soluble, and residual proteins were prepared from all nuclear stages and examined by one- and two-dimensional gel electrophoresis. Within limits of sensitivity of these techniques, the following general features emerged. (a) A majority of proteins visualized were common to and present in similar relative quantities in nuclei from all age and ploidy groups. (b) A relatively higher proportion of nonhistone proteins (NHP) were saline-soluble in 2C nuclei from young rats than at any subsequent stage of development. (c) Several age-related and to a lesser extent ploidy-related fluctuations in pattern among the NHP were evident. These reflected primarily differences in solubility rather than major quantitative changes among individual proteins. (d) Exceptions to the foregoing included a group of high molecular weight components (> 100 000), a major and a minor component between 45 000 and 50 000, and a heterogeneous group of proteins in 2C nuclei from very young animals. There were no obvious differences among the histones, although these proteins were not examined in detail. The complex pattern of changes observed are discussed in terms of known aspects of hepatocyte differentiation and are related to possible changes in nucleoplasmic, nuclear matrix and Hn-RNP associated proteins.

Diversity of Glycoprotein Deficiencies in Glanzmann’s Thrombasthenia

1985 ◽  
Vol 54 (03) ◽  
pp. 626-629 ◽  
Author(s):  
M Meyer ◽  
F H Herrmann
Keyword(s):  
High Resolution ◽  
Gel Electrophoresis ◽  
Type Ii ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Structural Variant ◽  
Glanzmann’S Thrombasthenia ◽  
Crossed Immunoelectrophoresis ◽  
Glanzmann's Thrombasthenia ◽  
Platelet Proteins

SummaryThe platelet proteins of 9 thrombasthenic patients from 7 families were analysed by high resolution two-dimensional gel electrophoresis (HR-2DE) and crossed immunoelectrophoresis (CIE). In 7 patients both glycoproteins (GPs) IIb and Ilia were absent or reduced to roughly the same extent. In two related patients only a trace of GP Ilb-IIIa complex was detected in CIE, but HR-2DE revealed a glycopeptide in the position of GP Ilia in an amount comparable to type II thrombasthenia. This GP Ilia-like component was neither recognized normally by anti-GP Ilb-IIIa antibodies nor labeled by surface iodination. In unreduced-reduced two-dimensional gel electrophoresis two components were observed in the region of GP Ilia. The assumption of a structural variant of GP Ilia in the two related patients is discussed.

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