Identification of significant potential signaling pathways and differentially expressed proteins in patients with wheat intolerance based on quantitative proteomics

2021 ◽  
pp. 104317
Author(s):  
Wei Zhang ◽  
Lin Sun ◽  
Yupeng Wang ◽  
Min Zhao ◽  
Qi Zhang ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
Quantitative Proteomics ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Significant Potential

scholarly journals Serum Proteomic Analysis of Cannabis Use Disorder in Male Patients

Molecules ◽  
2021 ◽  
Vol 26 (17) ◽  
pp. 5311
Author(s):  
Fawaz Alasmari ◽  
Sary Alsanea ◽  
Assim A. Alfadda ◽  
Ibrahim O. Alanazi ◽  
Mohthash Musambil ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
Proteomic Analysis ◽  
Cannabis Use ◽  
Farnesoid X Receptor ◽  
Differentially Expressed ◽  
Interleukin 12 ◽  
Control Group ◽  
Cannabis Use Disorder ◽  
Differentially Expressed Proteins ◽  
Healthy Control

Cannabis use has been growing recently and it is legally consumed in many countries. Cannabis has a variety of phytochemicals including cannabinoids, which might impair the peripheral systems responses affecting inflammatory and immunological pathways. However, the exact signaling pathways that induce these effects need further understanding. The objective of this study is to investigate the serum proteomic profiling in patients diagnosed with cannabis use disorder (CUD) as compared with healthy control subjects. The novelty of our study is to highlight the differentially changes proteins in the serum of CUD patients. Certain proteins can be targeted in the future to attenuate the toxicological effects of cannabis. Blood samples were collected from 20 male individuals: 10 healthy controls and 10 CUD patients. An untargeted proteomic technique employing two-dimensional difference in gel electrophoresis coupled with mass spectrometry was employed in this study to assess the differentially expressed proteins. The proteomic analysis identified a total of 121 proteins that showed significant changes in protein expression between CUD patients (experimental group) and healthy individuals (control group). For instance, the serum expression of inactive tyrosine protein kinase PEAK1 and tumor necrosis factor alpha-induced protein 3 were increased in CUD group. In contrast, the serum expression of transthyretin and serotransferrin were reduced in CUD group. Among these proteins, 55 proteins were significantly upregulated and 66 proteins significantly downregulated in CUD patients as compared with healthy control group. Ingenuity pathway analysis (IPA) found that these differentially expressed proteins are linked to p38MAPK, interleukin 12 complex, nuclear factor-κB, and other signaling pathways. Our work indicates that the differentially expressed serum proteins between CUD and control groups are correlated to liver X receptor/retinoid X receptor (RXR), farnesoid X receptor/RXR activation, and acute phase response signaling.

scholarly journals Tandem Mass Tag-Based Quantitative Proteomic Analysis Reveals Pathways Involved in Brain Injury Induced by Chest Exposure to Shock Waves

2021 ◽  
Vol 14 ◽  
Author(s):  
Changci Tong ◽  
Peifang Cong ◽  
Ying Liu ◽  
Xiuyun Shi ◽  
Lin Shi ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Brain Injury ◽  
Signaling Pathways ◽  
Brain Damage ◽  
Western Blotting ◽  
Differentially Expressed ◽  
Tandem Mass ◽  
Differentially Expressed Proteins ◽  
Blast Exposure ◽  
Tandem Mass Tag

Recurrent chest blast exposure can lead to brain inflammation, oxidative stress, and mental disorders in soldiers. However, the mechanism that underlies brain injury caused indirectly by chest blasts remains unclear. It is urgent to find additional reliable biomarkers to reveal the intimate details of the pathogenesis of this phenomenon. We used the term tandem mass tag (TMT) labeling combined with liquid chromatography–tandem mass spectrometry (LC-MS/MS) to screen for differentially expressed proteins in rat brain at different time points after a chest blast. Data are available via ProteomeXchange with the identifier PXD025204. Gene Ontology (GO), the Kyoto Encyclopedia of Genes and Genomes (KEGG), the Database for Annotation, Visualization and Integrated Discovery (DAVID), and Cytoscape analyses were used to analyze the proteomic profiles of blast-exposed rats. In addition, we performed Western blotting to verify protein levels. We identified 6,931 proteins, of which 255 were differentially expressed and 43, 84, 52, 97, and 49 were identified in brain tissues at 12, 24, 48, and 72 h and 1 week after chest blast exposure, respectively. In this study, the GO, KEGG, Clusters of Orthologous Groups of proteins, and Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) analyses indicated that brain damage caused by chest blast exposure involved many important biological processes and signaling pathways, such as inflammation, cell adhesion, phagocytosis, neuronal and synaptic damage, oxidative stress, and apoptosis. Furthermore, Western blotting confirmed that these differentially expressed proteins and affected signaling pathways were associated with brain damage caused by chest blast exposure. This study identifies potential protein biomarkers of brain damage caused indirectly by chest blast and new targets for the treatment of this condition.

scholarly journals Comparative proteome analysis of the spinal dural arteriovenous fistula arterial draining vein with label-free quantitative proteomics

2020 ◽  
Author(s):  
Peixi Liu ◽  
Yuan Shi ◽  
Sichen Li ◽  
Yingjun Liu ◽  
Yingjie Zhou ◽  
...  
Keyword(s):  
Quantitative Proteomics ◽  
Dural Arteriovenous Fistula ◽  
Kegg Pathway ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Label Free ◽  
Spinal Dural Arteriovenous Fistula ◽  
Differentially Expressed Protein ◽  
Kegg Pathway Analysis ◽  
Go Terms

Abstract Background: Spinal dural arteriovenous fistula (SDAVF) is the most common spinal vascular shunt lesion. Although pathological changes in the SDAVF draining vein (SDAVF-DV) have been elucidated, protein changes remain enigmatic. We investigated protein changes in the SDAVF-DV.Methods: Three SDAVF-DV samples were collected, and superficial temporal artery (STA) and superficial temporal vein (STV) samples were used as controls. After quantification and enzymolysis of the proteins, label-free quantitative proteomics was performed, and the peptide mixture was fractionated and analysed by liquid chromatography tandem mass spectrometry (LC-MS/MS) to identify the differentially expressed proteins. Bioinformatics analysis of the differentially expressed proteins was also performed using Gene Ontology (GO), Kyoto Encyclopedia of Genes and Genomes (KEGG) and protein-protein interaction (PPI) network analyses.Results: Compared with the STA, the SDAVF-DV had 195 upregulated proteins and 303 downregulated proteins. GO analysis showed that the most differential GO terms in each category were the adenylate cyclase-modulating G protein-coupled receptor signalling pathway, U6 snRNP and SH3 domain binding. KEGG pathway analysis showed that the most differentially expressed protein pathway was focal adhesion. Compared with the STV, the SDAVF-DV had 158 upregulated proteins and 362 downregulated proteins. GO analysis showed that the most differential GO terms in each category were lamellipodium assembly, U6 snRNP, and SH3 domain binding. KEGG pathway analysis showed that the most differentially expressed protein pathway was dilated cardiomyopathy. The PPI analysis revealed PPIs among the top 300 proteins.Conclusions: We demonstrated that the SDAVF-DV showed specific protein expression changes under long-period venous hypertension. The results of the present study will provide insights into the pathogenesis of SDAVF formation at the protein level. The proteomic results provide a scientific foundation for further study to explore the pathophysiological mechanism of SDAVF.

scholarly journals Identification and validation of differentially expressed proteins in epithelial ovarian cancers using quantitative proteomics

Oncotarget ◽  
2016 ◽  
Vol 7 (50) ◽  
pp. 83187-83199 ◽  
Author(s):  
Hong Qu ◽  
Yuling Chen ◽  
Guangming Cao ◽  
Chongdong Liu ◽  
Jiatong Xu ◽  
...  
Keyword(s):  
Quantitative Proteomics ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Ovarian Cancers

Quantitative proteomics reveals stage-specific protein regulation of triple negative breast cancer

2020 ◽  
Author(s):  
Yuxiang Lin ◽  
Ling Lin ◽  
Fangmeng Fu ◽  
Chuan Wang ◽  
Anqi Hu ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Signaling Pathways ◽  
Quantitative Proteomics ◽  
Protein Identification ◽  
High Resolution Mass Spectrometry ◽  
Therapeutic Targets ◽  
Differentially Expressed ◽  
Amino Acid Synthesis ◽  
Tumor Tissues ◽  
Grade Iii

Abstract BackgroundTriple negative breast cancer (TNBC) is a heterogeneous disease with more aggressive clinical courses than other subtypes of breast cancer. In this study, we performed high-resolution mass spectrometry-based quantitative proteomics with TNBC clinical tissue specimens to explore the early and sensitive diagnostic signatures and potential therapeutic targets for TNBC patients. Methods We performed an iTRAQ-labeling coupled LC-MS/MS approach to explore the global proteome in tumor tissues and corresponding para-tumor tissues from 24 patients with grade I-II and grade III primary TNBC. Relative peptide quantification and protein identification were performed by Proteome Discoverer TM software with Mascot search engine. Differentially expressed proteins were analyzed by bioinformatic analyses, including GO function classification annotation and KEGG enrichment analysis. Pathway analyses for protein-protein interactions and upstream regulations of differentially expressed candidates were performed by Ingenuity Pathway Analysis (IPA) software. Results Totally, 5,401 unique proteins were identified and quantified in different stage of TNBCs. 865 proteins were changed in patients with grade I or II TNBC, among which 309 were up-regulated and 556 were down-regulated. Meanwhile, for patients with grade III TNBC, 359 proteins were increased and 672 proteins were decreased. Comparing to para-cancerous tissues, various signaling pathways and metabolic processes, including PPAR pathways, PI3K-Akt pathway, one-carbon metabolism, amino acid synthesis, and lipid metabolism were activated in TNBC cancer tissues. Death receptor signaling was significantly activated in grade I-II TNBCs, however, remarkably inhibited in grade III TNBCs. Conclusions Overall, our proteomic data presented precise quantification of potential signatures, signaling pathways, regulatory networks, and characteristic differences in each clinicopathological subgroup. The proteome provides complementary information for TNBC accurate subtype classification and therapeutic targets research.

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