scholarly journals Label-free Quantitative Analysis of Changes in Broiler Liver Proteins under Heat Stress using SWATH-MS Technology

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Xiangfang Tang ◽  
Qingshi Meng ◽  
Jie Gao ◽  
Sheng Zhang ◽  
Hongfu Zhang ◽  
...  
2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Sarah Tonello ◽  
Francesca Stradolini ◽  
Giulia Abate ◽  
Daniela Uberti ◽  
Mauro Serpelloni ◽  
...  

AbstractProtein electrochemistry represents a powerful technique for investigating the function and structure of proteins. Currently available biochemical assays provide limited information related to the conformational state of proteins and high costs. This work provides novel insights into the electrochemical investigation of the metalloprotein p53 and its redox products using label-free direct electrochemistry and label-based antibody-specific approaches. First, the redox activities of different p53 redox products were qualitatively investigated on carbon-based electrodes. Then, focusing on the open p53 isoform (denatured p53), a quantitative analysis was performed, comparing the performances of different bulk and nanostructured materials (carbon and platinum). Overall, four different p53 products could be successfully discriminated, from wild type to denatured. Label-free analysis suggested a single electron exchange with electron transfer rate constants on the order of 1 s−1. Label-based analysis showed decreasing affinity of pAb240 towards denatured, oxidized and nitrated p53. Furthermore, platinum nanostructured electrodes showed the highest enhancement of the limit of detection in the quantitative analysis (100 ng/ml). Overall, the obtained results represent a first step towards the implementation of highly requested complex integrated devices for clinical practices, with the aim to go beyond simple protein quantification.


2012 ◽  
Vol 11 (9) ◽  
pp. 4755-4763 ◽  
Author(s):  
Nisha A. Patel ◽  
Andrew Crombie ◽  
Susan E. Slade ◽  
Konstantinos Thalassinos ◽  
Chris Hughes ◽  
...  

RSC Advances ◽  
2014 ◽  
Vol 4 (62) ◽  
pp. 32960 ◽  
Author(s):  
Lingling Ye ◽  
Guiqing Wen ◽  
Jinchao Dong ◽  
Yanghe Luo ◽  
Qingye Liu ◽  
...  

2019 ◽  
Vol 8 (12) ◽  
pp. 2128 ◽  
Author(s):  
Giuseppe Grande ◽  
Federica Vincenzoni ◽  
Francesca Mancini ◽  
Ferran Barrachina ◽  
Antonella Giampietro ◽  
...  

In the grey zone of testosterone levels between 8 and 12 nmol/L, the usefulness of therapy is controversial; as such, markers of tissue action of androgens may be helpful in adjusting clinical decisions. To better understand the effect of the hypothalamic-pituitary-testicular axis on male accessory secretion, we performed a proteomic quantitative analysis of seminal plasma in patients with secondary hypogonadism, before and after testosterone replacement therapy (TRT). Ten male patients with postsurgical hypogonadotrophic hypogonadism were enrolled in this study, and five of these patients were evaluated after testosterone treatment. Ten men with proven fertility were selected as a control group. An aliquot of seminal plasma from each individual was subjected to an in-solution digestion protocol and analyzed using an Ultimate 3000 RSLC-nano HPLC apparatus coupled to a LTQ Orbitrap Elite mass spectrometer. The label-free quantitative analysis was performed via Precursor Ions Area Detector Node. Eleven proteins were identified as decreased in hypogonadic patients versus controls, which are primarily included in hydrolase activity and protein binding activity. The comparison of the proteome before and after TRT comes about within the discovery of six increased proteins. This is the primary application of quantitative proteomics pointed to uncover a cluster of proteins reflecting an impairment not only of spermatogenesis but of the epididymal and prostate epithelial cell secretory function in male hypogonadism. The identified proteins might represent putative clinical markers valuable within the follow-up of patients with distinctive grades of male hypogonadism.


2012 ◽  
Vol 11 (6) ◽  
pp. M111.015974 ◽  
Author(s):  
Berend Hoekman ◽  
Rainer Breitling ◽  
Frank Suits ◽  
Rainer Bischoff ◽  
Peter Horvatovich

2019 ◽  
Author(s):  
Liu Ping ◽  
Guo Lulu ◽  
Mao Huaming ◽  
Gu Zhaobing

Abstract Background: Chronic heat stress (CHS), aggravated by global warming, reduces the production efficiency of the buffalo dairy industry. CHS changes protein abundance, and low-abundant proteins take important roles in biological processes. Results: The objective of the study was to assess differences in low-abundant serum proteins in dairy buffaloes at thermoneutral (TN) or under chronic heat stress (CHS) conditions with proteomic approaches. Six dairy buffaloes as reference animal raised in TN season, and another six dairy buffaloes raised in CHS to discover the molecular mechanism of thermal fitness in hot season with serum proteomics. After the removal of multiple high-abundant proteins in serum, 344 low-abundant proteins were identified in serum with label-free quantification. Of these, 17 low-abundant differentially expressed serum proteins with known functions were detected, and five of these differentially expressed proteins were validated with parallel reaction monitoring. These five proteins were associated with various aspects of heat stress, including decreased heat production, increased blood oxygen delivery, and enhanced natural disease resistance. Conclusions: Lipase (LPL), glutathione peroxidase 3 (GPX3), cathelicidin-2 (CATHL2), ceruloplasmin (CP), and hemoglobin subunit alpha 1 (HBA1) were shown to play cooperative roles in CHS fitness in dairy buffalo. Dairy buffaloes adapt to CHS and hypoxia with high levels of RBCs, HBA1 and CP increased blood oxygen delivery capacity and thermal fitness.


2012 ◽  
Vol 405 (2-3) ◽  
pp. 635-645 ◽  
Author(s):  
Anna Laura Capriotti ◽  
Giulio Caracciolo ◽  
Giuseppe Caruso ◽  
Chiara Cavaliere ◽  
Daniela Pozzi ◽  
...  

2020 ◽  
Author(s):  
Muhammad Arshad ◽  
Alpa Puri ◽  
Aaron J Simkovich ◽  
Justin Renaud ◽  
Margaret Y Gruber ◽  
...  

Abstract Background Abiotic stress, including heat, is one of the major factors that affect alfalfa growth and forage yield. The small RNA, microRNA156 (miR156), regulates multiple traits in alfalfa during abiotic stress. The aim of this study was to explore the role of miR156 in regulating heat response in alfalfa at the protein level. Results In this study, we compared an empty vector control and miR156 overexpressing (miR156OE) alfalfa plants after exposing them to heat stress (40 ° C) for 24 hours. We measured physiological parameters of control and miR156OE plants under heat stress, and collected leaf samples for protein analysis. A higher proline and antioxidant contents were detected in miR156OE plants than in controls under heat stress. Protein samples were analyzed by label-free quantification proteomics. Across all samples, a total of 1878 protein groups were detected. Under heat stress, 45 protein groups in the empty vector plants were significantly altered (P < 0.05; |log 2 FC| > 2). Conversely, 105 protein groups were significantly altered when miR156OE alfalfa was subjected to heat stress, of which 91 were unique to miR156OE plants. The identified protein groups unique to miR156OE plants were related to diverse functions including metabolism, photosynthesis, stress-response and plant defenses. Furthermore, we identified transcription factors in miR156OE plants, which belonged to squamosa promoter binding-like protein, MYB, ethylene responsive factors, AP2 domain, ABA response element binding factor and bZIP families of transcription factors. Conclusions These results suggest a positive role for miR156 in heat stress response in alfalfa. They reveal a miR156-regulated network of mechanisms at the protein level to modulate heat responses in alfalfa.


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