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Upregulated Proteins (upregulated + protein)
Selected AbstractsProteomic identification of an upregulated isoform of annexin A3 in the rat brain following reversible cerebral ischemiaGLIA, Issue 16 2007Heike Junker Abstract We used proteomics to identify regulated proteins following cerebral ischemia in a rat model. Young rats were subjected to reversible middle cerebral artery (MCA) occlusion and proteins were extracted from the peri-infarcted and the corresponding contralateral area at days 3 and 14 postischemia. Proteins were analyzed by two-dimensional polyacrylamide gel electrophoresis followed by mass spectrometry. We report for the first time that an isoform of annexin A3 (ANXA3) was among the upregulated proteins in the postischemic rat brain. The results were confirmed by real-time PCR and by western blotting. Double- and triple-immunostaining with neuronal and microglia/macrophagic markers demonstrated that ANXA3 is produced by resting microglia in control tissue and by activated microglial/macrophage cells in the infarcted area. 3D-images of the infarcted area suggest that ANXA3 is associated with a phagocytic phenotype. Our study identifies ANXA3 as a novel marker of brain microglia, which should be of substantial value in future studies of microglial cells and its role in the postischemic brain. © 2007 Wiley-Liss, Inc. [source] Comparative proteomic analysis of passaged Helicobacter pyloriJOURNAL OF BASIC MICROBIOLOGY, Issue 5 2009Mao-Jun Zhang Abstract In order to identify the proteins associated with Helicobacter pylori colonization in mice, we used 2-dimensional gel electrophoresis (2-DE) to analyze the membrane- and soluble-cellular proteins extracted from H. pylori strain 26695 and the mouse-passaged homolog 88-3887. We defined 2- and 3-fold changes in protein expression as the threshold values for differential expression in the membrane-protein and whole-cell-protein fractions, respectively. The differentially expressed proteins were identified by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/TOF). A total of 29 proteins, including 16 membrane- or membrane-associated proteins (13 upregulated, 3 downregulated) and 13 cellular proteins (10 upregulated, 3 downregulated) were differentially expressed between the strains 26695 and 88-3887. Among the upregulated proteins, 10 proteins had been previously shown to be associated with the mouse colonization, and 13 upregulated proteins were shown to be associated with the adaptation of H. pylori in murine hosts for the first time in this study. The identified proteins were classified as proteins related to metabolism, stress response, virulence, or adhesion. The data presented in this report indicated that there were subsets of upregulated proteins in mouse-adapted H. pylori. In particular, the adhesins, virulence factors, and stress-response proteins are likely to contribute to colonization in mice. (© 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim) [source] Comparative proteomic analysis of primary mouse liver c-Kit,(CD45/TER119), stem/progenitor cellsJOURNAL OF CELLULAR BIOCHEMISTRY, Issue 4 2007Yu-Fei He Abstract Liver stem/progenitor cells play a key role in liver development and maybe also in liver cancer development. In our previous study a population of c-Kit,(CD45/TER119), liver stem/progenitor cells in mouse fetal liver, was successfully sorted with large amount (106,107) by using immuno-magnetic microbeads. In this study, the sorted liver stem/progenitor cells were used for proteomic study. Proteins of the sorted liver stem/progenitor cells and unsorted fetal liver cells were investigated using two-dimensional electrophoresis. A two-dimensional proteome map of liver stem/progenitor cells was obtained for the first time. Proteins that exhibited significantly upregulation in liver stem/progenitor cells were identified by peptide mass fingerprinting and peptide sequencing. Nineteen protein spots corresponding to 12 different proteins were identified as showing significant upregulation in liver stem/progenitor cells and seem to play important roles in such cells in cell metabolism, cell cycle regulation, and stress. An interesting finding is that most of the upregulated proteins were overexpressed in various cancers (11 of 12, including 6 in human hepatocellular carcinoma (HCC)) and involved in cancer development as reported in previous studies. Some of the identified proteins were validated by real-time PCR, Western blotting, and immunostaining. Taken together, the data presented provide a significant new protein-level insight into the biology of liver stem/progenitor cells, a key population of cells that might be also involved in liver cancer development. J. Cell. Biochem. 102: 936,946, 2007. © 2007 Wiley-Liss, Inc. [source] Proteomic identification of peroxiredoxin 6 for host defence against Opisthorchis viverrini infectionPARASITE IMMUNOLOGY, Issue 5 2010J. KHOONTAWAD Summary Opisthorchis viverrini infection causes opisthorchiasis and is a risk factor for cholangiocarcinoma via chronic inflammation. To investigate the mechanism of O. viverrini -induced liver disease, we applied a proteomic approach to examine alterations in hepatic protein levels in O. viverrini -infected hamsters. Two-dimensional gel electrophoresis (2DE) revealed that O. viverrini infection induced upregulation (1·5- to 4·3-fold) of 25 proteins and downregulation (1·5 to 2·5-fold) of 24 proteins compared with uninfected animals. Expression of proteins related to stress response, DNA replication and repair, and cell structure was significantly increased, whereas that of proteins associated with normal liver function, such as metabolism, blood volume maintenance and fatty acid cycle was decreased. Among the upregulated proteins, a 2·7-fold increase in peroxiredoxin 6 (Prdx6), an antioxidant protein, was confirmed by 2DE and immunoblot analysis, Western blot and quantitative PCR. Immunohistochemical analysis showed that Prdx6 expression was observed mainly in the cytoplasm of inflammatory cells. These results suggest that Prdx6 is important for host defence against O. viverrini infection. This study provides basic information for Prdx6 as a potential biomarker and therapeutic target for opisthorchiasis. [source] Identification of secreted proteins regulated by cAMP in glioblastoma cells using glycopeptide capture and label-free quantificationPROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 3 2009Jennifer J. Hill Dr. Abstract Exposure of glioblastoma U87MG cells to a cAMP analog leads to a decrease in proliferation, invasion, and angiogenic potential. Here, we apply a label-free MS-based approach to identify formerly N -linked glycopeptides that change in abundance upon cAMP treatment. Over 150 unique glycopeptides in three biological repetitions were quantified, leading to the identification of 14 upregulated proteins and 21 downregulated proteins due to cAMP treatment. Of these, eight have been validated, either through comparison with microarray data or by Western blot. We estimate our ability to identify differentially expressed peptides at greater than 85% in a single biological repetition, while the analysis of multiple biological repetitions lowers the false positive rate to ,2%. Many of the proteins identified in this study are involved in cell signaling and some, such as Tenascin C, Cathepsin L, Neuroblastoma suppressor of tumorigenicity, and AXL/UFO tyrosine,protein kinase receptor, have been previously shown to be involved in glioblastoma progression. We also identify several semitryptic peptides that increase in abundance upon cAMP treatment, suggesting that cAMP regulates protease activity in these cells. Overall, these results demonstrate the benefits of using a highly specific enrichment method for quantitative proteomic experiments. [source] Quantitative proteome analysis of HCC cell lines with different metastatic potentials by SILACPROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 23-24 2008Ning Chen Abstract Hepatocellular carcinoma (HCC) is one of the most common cancers worldwide and metastasis is the main cause for treatment failure and high fatality of HCC. In order to make further exploration into the mechanism of HCC metastasis and to search for the candidates of diagnostic marker and therapeutic target, stable-isotope labeling by amino acids in cell culture (SILAC) technique was employed to conduct differential proteome analysis on HCC cell lines , MHCC97L and HCCLM6 with low and high metastatic potentials. In total, 2335 reliable proteins were identified using LTQ-FT mass spectrum, among which 91 proteins were upregulated and 61 proteins were downregulated in HCCLM6. Most of the upregulated proteins were involved in adherence, morphogenesis, and lipid synthesis, while lots of the downregulated proteins were involved in electron transport, which might be crucial for HCC metastasis. Six dysregulated proteins were validated by Western blotting in the cell lines. Interestingly, the upregulation of solute carrier family 12 member 2 (SLC 12A2) and protein disulfide-isomerase A4 (PDIA4) were further confirmed in the culture supernatants by Western blotting and in the sera of HCC patients with different metastatic potentials by ELISA. Our study provided not only the valuable insights into the HCC metastasis mechanisms but also the potential candidate biomarkers for prediction of HCC metastasis. [source] | ||||||||||