High performance mass spectrometry based proteomics reveals enzyme and signaling pathway regulation in neutrophils during the early stage of surgical trauma

Arshid, Samina; Tahir, Muhammad; Fontes, Belchor; Montero, Edna Frasson de Souza; Castro, Mariana S.; Roepstorff, Peter; Fontes, Wagner

doi:10.1002/prca.201600001

Cited by 13 publications

(16 citation statements)

References 75 publications

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“…During our analysis, the laparotomy group did not have a statistically significant effect on phosphoproteome of the kinases and phosphatases, compared to the iIR and iIPC. There are very few proteins with significantly higher phosphorylation regulation in the laparotomy group compared to the control group, like the up-regulation of 60S acidic ribosomal protein P2 (P02401) and the down-regulation of 26S proteasome non-ATPase regulatory subunit 1 (O88761), in agreement with previous findings of higher rates of mRNA processing and protein synthesis for the neutrophil after surgical trauma [32].…”

Section: Various Studies Have Documented Different Ratios Of S/t/y Phsupporting

confidence: 89%

“…Some of these regulated proteins have their abundance profile kept at control levels if the IPC is applied, and most of the enzymes presenting this profile are hydrolases or transferases [31]. Less frequent, but still significant abundance changes were found for proteins related to the protein biosynthesis and proteasome degradation processes in mild surgical trauma [32]. Since protein phosphatases are a subclass of hydrolases and protein kinases are a subclass of transferases, the analysis of protein phosphorylation was developed as a follow-up study from our previous work.…”

Section: Introductionmentioning

confidence: 99%

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Phosphoproteomic Analysis of Rat Neutrophils Shows the Effect of Intestinal Ischemia/Reperfusion and Preconditioning on Kinases and Phosphatases

Tahir

Arshid

Fontes

et al. 2020

IJMS

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Intestinal ischemia reperfusion injury (iIRI) is a severe clinical condition presenting high morbidity and mortality worldwide. Some of the systemic consequences of IRI can be prevented by applying ischemic preconditioning (IPC), a series of short ischemia/reperfusion events preceding the major ischemia. Although neutrophils are key players in the pathophysiology of ischemic injuries, neither the dysregulation presented by these cells in iIRI nor the protective effect of iIPC have their regulation mechanisms fully understood. Protein phosphorylation, as well as the regulation of the respective phosphatases and kinases are responsible for regulating a large number of cellular functions in the inflammatory response. Moreover, in previous work we found hydrolases and transferases to be modulated in iIR and iIPC, suggesting the possible involvement of phosphatases and kinases in the process. Therefore, in the present study, we analyzed the phosphoproteome of neutrophils from rats submitted to mesenteric ischemia and reperfusion, either submitted or not to IPC, compared to quiescent controls and sham laparotomy. Proteomic analysis was performed by multi-step enrichment of phosphopeptides, isobaric labeling, and LC-MS/MS analysis. Bioinformatics was used to determine phosphosite and phosphopeptide abundance and clustering, as well as kinases and phosphatases sites and domains. We found that most of the phosphorylation-regulated proteins are involved in apoptosis and migration, and most of the regulatory kinases belong to CAMK and CMGC families. An interesting finding revealed groups of proteins that are modulated by iIR, but such modulation can be prevented by iIPC. Among the regulated proteins related to the iIPC protective effect, Vamp8 and Inpp5d/Ship are discussed as possible candidates for control of the iIR damage.

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Section: Various Studies Have Documented Different Ratios Of S/t/y Phsupporting

confidence: 89%

Section: Introductionmentioning

confidence: 99%

Phosphoproteomic Analysis of Rat Neutrophils Shows the Effect of Intestinal Ischemia/Reperfusion and Preconditioning on Kinases and Phosphatases

Tahir

Arshid

Fontes

et al. 2020

IJMS

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“…Prior to protein digestion, a volume of digestion buffer was added to reach a final concentration of 0.005 M DTT, 0.001 M CaCl 2 and 0.02 M TEAB in a final volume of 75 µl. All samples were digested with trypsin (Promega, Fitchburg, WI, USA) with a 1/50 (w/w) enzyme/substrate ratio and incubated at 37 °C for 18 h. A solution of TFA (trifluoroacetic acid) was added to a final concentration of 1% to stop tryptic activity 75 .…”

Section: Methodsmentioning

confidence: 99%

Proteomic landscape of seminal plasma associated with dairy bull fertility

Viana

Martins

Pontes

et al. 2018

Sci Rep

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Male fertility is the ability of sperm to fertilize the egg and sustain embryo development. Several factors determine the fertilizing capacity of mammalian sperm, including those intrinsic to sperm and components of the seminal plasma. The present study analyzed the seminal fluid proteome of Bos taurus and potential associations between proteins and fertility scores. Mass spectrometry coupled with nano HPLC allowed the identification of 1,159 proteins in the dairy bull seminal plasma. There were 50 and 29 seminal proteins more abundant in high (HF) low fertility (LF) bulls, respectively. Based on multivariate analysis, C-type natriuretic peptide, TIMP-2, BSP5 and sulfhydryl oxidase indicated relationship with HF bulls. Clusterin, tissue factor pathway inhibitor 2, galectin-3-binding protein and 5′-nucleotidase were associated with LF bulls. Abundance of NAD(P)(+)-arginine ADP-ribosyltransferase, prosaposin and transmembrane protein 2 proteins had the highest positive correlations with fertility ranking. Quantities of vitamin D-binding protein, nucleotide exchange factor SIL1 and galectin-3-binding protein showed the highest negative correlations with fertility ranking. A fertility ranking score was calculated and the relationship with these proteins was significant (Spearman’s rho = 0.94). The present findings represent a major and novel contribution to the study of bovine seminal proteins. Indicators of fertility can be used to improve reproductive biotechnologies.

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“…Proteomics is the science of studying protein composition and alterations in cells, tissues, and organisms. Proteomics is widely used in basic and clinical medical research [ 7 ] for the identification of biomarkers [ 8 , 9 ], posttranslational protein modifications [ 10 ], and the regulation of signaling pathways [ 11 ]. Proteomics research of lung cancer has focused on the classification of lung cancer [ 12 ], the correlation between protein and gene expressions [ 13 , 14 ], identification of new molecular targets [ 15 , 16 ], and the development of new drugs [ 17 , 18 ].…”

Section: Introductionmentioning

confidence: 99%

LC-MS/MS-Based Quantitative Proteomics Analysis of Different Stages of Non-Small-Cell Lung Cancer

Zhou

Kong

Wang

et al. 2021

BioMed Research International

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Lung cancer has a higher incidence rate and mortality rate than all other cancers. Early diagnosis and treatment of lung cancer remain a major challenge, and the 5-year survival rate of its patients is only 15%. Basic and clinical research, especially the discovery of biomarkers, is crucial for improving the diagnosis and treatment of lung cancer patients. To identify novel biomarkers for lung cancer, we used the iTRAQ8-plex labeling technology combined with liquid chromatography-tandem mass spectrometry (LC-MS/MS) to analyze the serum and urine of patients with different stages of lung adenocarcinoma and healthy individuals. A total of 441 proteins were identified in the serum, and 1,161 proteins were identified in the urine. The levels of elongation factor 1-alpha 2, proteasome subunit alpha type, and spermatogenesis-associated protein increased significantly in the serum of patients with lung cancer compared with those in healthy controls. The levels of transmembrane protein 143, cadherin 5, fibronectin 1, and collectin-11 decreased significantly in the serum of patients with metastases compared with those of nonmetastatic lung cancer patients. In the urine of stage III and IV lung cancer patients, the prostate-specific antigen and prostatic acid phosphatase decreased significantly, whereas neutrophil defensin 1 increased significantly. The results of LC-MS/MS were confirmed by enzyme-linked immunosorbent assay (ELISA) for transmembrane protein 143, cadherin 5, fibronectin 1, and collectin-11 in the serum. These proteins may be a potential early diagnosis and metastasis biomarkers for lung adenocarcinoma. Furthermore, the relative content of these markers in the serum and urine could be used to determine the progression of lung adenocarcinoma and achieve accurate staging and diagnosis.

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High performance mass spectrometry based proteomics reveals enzyme and signaling pathway regulation in neutrophils during the early stage of surgical trauma

Abstract: Collectively, our results reveal that neutrophils drastically regulate their biochemical pathways after the early stages of surgical trauma, showing lower activity. This implies higher susceptibility of the trauma patients to infection and bystander tissues damage.

Cited by 13 publications

References 75 publications

Phosphoproteomic Analysis of Rat Neutrophils Shows the Effect of Intestinal Ischemia/Reperfusion and Preconditioning on Kinases and Phosphatases

Phosphoproteomic Analysis of Rat Neutrophils Shows the Effect of Intestinal Ischemia/Reperfusion and Preconditioning on Kinases and Phosphatases

Proteomic landscape of seminal plasma associated with dairy bull fertility

LC-MS/MS-Based Quantitative Proteomics Analysis of Different Stages of Non-Small-Cell Lung Cancer

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