Quantitative proteomic analysis of okadaic acid treated mouse small intestines reveals differentially expressed proteins involved in diarrhetic shellfish poisoning

2012 ◽  
Vol 75 (7) ◽  
pp. 2038-2052 ◽  
Author(s):  
Juan Wang ◽  
Yu-Yu Wang ◽  
Lin Lin ◽  
Yue Gao ◽  
Hua-Sheng Hong ◽  
...  
Keyword(s):  
Okadaic Acid ◽  
Proteomic Analysis ◽  
Treated Mouse ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Shellfish Poisoning ◽  
Diarrhetic Shellfish Poisoning ◽  
Quantitative Proteomic Analysis ◽  
Small Intestines

scholarly journals Label-free quantitative proteomic analysis of the inhibition effect of Lactobacillus rhamnosus GG on Escherichia coli biofilm formation in co-culture

2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Huiyi Song ◽  
Ni Lou ◽  
Jianjun Liu ◽  
Hong Xiang ◽  
Dong Shang
Keyword(s):  
Escherichia Coli ◽  
Proteomic Analysis ◽  
Biofilm Formation ◽  
Lactobacillus Rhamnosus ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Label Free ◽  
Quantitative Proteomic Analysis ◽  
E Coli ◽  
Protein Ubiquitination

Abstract Background Escherichia coli (E. coli) is the principal pathogen that causes biofilm formation. Biofilms are associated with infectious diseases and antibiotic resistance. This study employed proteomic analysis to identify differentially expressed proteins after coculture of E. coli with Lactobacillus rhamnosus GG (LGG) microcapsules. Methods To explore the relevant protein abundance changes after E. coli and LGG coculture, label-free quantitative proteomic analysis and qRT-PCR were applied to E. coli and LGG microcapsule groups before and after coculture, respectively. Results The proteomic analysis characterised a total of 1655 proteins in E. coli K12MG1655 and 1431 proteins in the LGG. After coculture treatment, there were 262 differentially expressed proteins in E. coli and 291 in LGG. Gene ontology analysis showed that the differentially expressed proteins were mainly related to cellular metabolism, the stress response, transcription and the cell membrane. A protein interaction network and Kyoto Encyclopaedia of Genes and Genomes (KEGG) pathway analysis indicated that the differentiated proteins were mainly involved in the protein ubiquitination pathway and mitochondrial dysfunction. Conclusions These findings indicated that LGG microcapsules may inhibit E. coli biofilm formation by disrupting metabolic processes, particularly in relation to energy metabolism and stimulus responses, both of which are critical for the growth of LGG. Together, these findings increase our understanding of the interactions between bacteria under coculture conditions.

scholarly journals Quantitative proteomic analysis of differentially expressed proteins in tubers of potato plants differing in resistance to Dickeya solani

2019 ◽  
Vol 441 (1-2) ◽  
pp. 317-329 ◽  
Author(s):  
Renata Lebecka ◽  
Michał Kistowski ◽  
Janusz Dębski ◽  
Katarzyna Szajko ◽  
Zofia Murawska ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Quantitative Proteomic Analysis ◽  
Potato Plants ◽  
Dickeya Solani

Quantitative proteomic analysis reveals differentially expressed proteins in Leishmania major metacyclogenesis

2020 ◽  
Vol 149 ◽  
pp. 104557
Author(s):  
Nasrin Amiri-Dashatan ◽  
Mostafa Rezaei-Tavirani ◽  
Hakimeh Zali ◽  
Mehdi Koushki ◽  
Nayebali Ahmadi
Keyword(s):  
Proteomic Analysis ◽  
Leishmania Major ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Quantitative Proteomic Analysis

scholarly journals Isolation of Proteins from Potato Tubers

2017 ◽  
Vol 75 (1) ◽  
pp. 23-27 ◽  
Author(s):  
Zofia Murawska ◽  
Janusz Dębski ◽  
Katarzyna Szajko ◽  
Renata Lebecka
Keyword(s):  
Proteomic Analysis ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Potato Tubers ◽  
Experimental Conditions ◽  
Quantitative Proteomic Analysis ◽  
Reproducible Method

Abstract Here we optimized an efficient and reproducible method for proteins isolation from potato tubers for quantitative proteomic analysis, aimed at detection of differentially expressed proteins upon various experimental conditions.

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