Seasonal changes in atrophy-associated proteins of the sonic muscle in the big-snout croaker, Johnius macrorhynus (Pisces, Sciaenidae), identified by using a proteomic approach

2011 ◽  
Vol 37 (4) ◽  
pp. 977-991 ◽  
Author(s):  
Yuan-Chih Lin ◽  
Kuo-Hsun Chiu ◽  
Jentaie Shiea ◽  
Hurng-Wern Huang ◽  
Hin-Kiu Mok
2004 ◽  
Vol 70 (5) ◽  
pp. 2748-2755 ◽  
Author(s):  
M. Graça Silveira ◽  
Maja Baumgärtner ◽  
Frank M. Rombouts ◽  
Tjakko Abee

ABSTRACT The practical application of commercial malolactic starter cultures of Oenococcus oeni surviving direct inoculation in wine requires insight into mechanisms of ethanol toxicity and of acquired ethanol tolerance in this organism. Therefore, the site-specific location of proteins involved in ethanol adaptation, including cytoplasmic, membrane-associated, and integral membrane proteins, was investigated. Ethanol triggers alterations in protein patterns of O. oeni cells stressed with 12% ethanol for 1 h and those of cells grown in the presence of 8% ethanol. Levels of inosine-5′-monophosphate dehydrogenase and phosphogluconate dehydrogenase, which generate reduced nicotinamide nucleotides, were decreased during growth in the presence of ethanol, while glutathione reductase, which consumes NADPH, was induced, suggesting that maintenance of the redox balance plays an important role in ethanol adaptation. Phosphoenolpyruvate:mannose phosphotransferase system (PTS) components of mannose PTS, including the phosphocarrier protein HPr and EIIMan, were lacking in ethanol-adapted cells, providing strong evidence that mannose PTS is absent in ethanol-adapted cells, and this represents a metabolic advantage to O. oeni cells during malolactic fermentation. In cells grown in the presence of ethanol, a large increase in the number of membrane-associated proteins was observed. Interestingly, two of these proteins, dTDT-glucose-4,6-dehydratase and d-alanine:d-alanine ligase, are known to be involved in cell wall biosynthesis. Using a proteomic approach, we provide evidence for an active ethanol adaptation response of O. oeni at the cytoplasmic and membrane protein levels.


2009 ◽  
Vol 55 (8) ◽  
pp. 967-974 ◽  
Author(s):  
Abdellah Benachour ◽  
Thierry Morin ◽  
Laurent Hébert ◽  
Aurélie Budin-Verneuil ◽  
André Le Jeune ◽  
...  

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.


2007 ◽  
Vol 357 (2) ◽  
pp. 531-536 ◽  
Author(s):  
Jing Liu ◽  
Ping Zhu ◽  
Jiarou Peng ◽  
Keqiu Li ◽  
Jinwei Du ◽  
...  

PROTEOMICS ◽  
2006 ◽  
Vol 6 (7) ◽  
pp. 2225-2235 ◽  
Author(s):  
Merry L. Lindsey ◽  
Danielle K. Goshorn ◽  
Susana Comte-Walters ◽  
Jennifer W. Hendrick ◽  
Elizabeth Hapke ◽  
...  

2007 ◽  
Vol 189 (9) ◽  
pp. 3434-3444 ◽  
Author(s):  
M. Jiang ◽  
S. M. Sullivan ◽  
A. K. Walker ◽  
J. R. Strahler ◽  
P. C. Andrews ◽  
...  

ABSTRACT Biogenesis of the large ribosomal subunit requires the coordinate assembly of two rRNAs and 33 ribosomal proteins. In vivo, additional ribosome assembly factors, such as helicases, GTPases, pseudouridine synthetases, and methyltransferases, are also critical for ribosome assembly. To identify novel ribosome-associated proteins, we used a proteomic approach (isotope tagging for relative and absolute quantitation) that allows for semiquantitation of proteins from complex protein mixtures. Ribosomal subunits were separated by sucrose density centrifugation, and the relevant fractions were pooled and analyzed. The utility and reproducibility of the technique were validated via a double duplex labeling method. Next, we examined proteins from 30S, 50S, and translating ribosomes isolated at both 16°C and 37°C. We show that the use of isobaric tags to quantify proteins from these particles is an excellent predictor of the particles with which the proteins associate. Moreover, in addition to bona fide ribosomal proteins, additional proteins that comigrated with different ribosomal particles were detected, including both known ribosomal assembly factors and unknown proteins. The ribosome association of several of these proteins, as well as others predicted to be associated with ribosomes, was verified by immunoblotting. Curiously, deletion mutants for the majority of these ribosome-associated proteins had little effect on cell growth or on the polyribosome profiles.


2016 ◽  
Vol 12 (6) ◽  
pp. 5295-5302 ◽  
Author(s):  
Narges Khaghanzadeh ◽  
Kazuyuki Nakamura ◽  
Yasuhiro Kuramitsu ◽  
Abbas Ghaderi ◽  
Zahra Mojtahedi

2007 ◽  
Vol 119 (2-4) ◽  
pp. 240-247 ◽  
Author(s):  
Francesca Taverna ◽  
Armando Negri ◽  
Renata Piccinini ◽  
Alfonso Zecconi ◽  
Simona Nonnis ◽  
...  

Cancers ◽  
2021 ◽  
Vol 13 (21) ◽  
pp. 5573
Author(s):  
Lucia Borszéková Borszéková Pulzová ◽  
Jan Roška ◽  
Michal Kalman ◽  
Ján Kliment ◽  
Pavol Slávik ◽  
...  

Rete testis invasion (RTI) is an unfavourable prognostic factor for the risk of relapse in clinical stage I (CS I) seminoma patients. Notably, no evidence of difference in the proteome of RTI-positive vs. -negative CS I seminomas has been reported yet. Here, a quantitative proteomic approach was used to investigate RTI-associated proteins. 64 proteins were differentially expressed in RTI-positive compared to -negative CS I seminomas. Of them, 14-3-3γ, ezrin, filamin A, Parkinsonism-associated deglycase 7 (PARK7), vimentin and vinculin, were validated in CS I seminoma patient cohort. As shown by multivariate analysis controlling for clinical confounders, PARK7 and filamin A expression lowered the risk of RTI, while 14-3-3γ expression increased it. Therefore, we suggest that in real clinical biopsy specimens, the expression level of these proteins may reflect prognosis in CS I seminoma patients.


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