scholarly journals SEEKING CANDIDATE MOLECULES AS PROGNOSTIC HEALING MARKERS IN CHRONIC VENOUS ULCERS

2020 ◽  
Author(s):  
Nayara Rodrigues Vieira Cavassan ◽  
Noemia Aparecida Partelli Mariani ◽  
Caio Cavassan Camargo ◽  
Ivan Rodrigo Wolf ◽  
Benedito Barraviera ◽  
...  
Keyword(s):  
Standard Treatment ◽  
Healing Process ◽  
Mass Spectrometry Analysis ◽  
Complement C3 ◽  
Potential Candidate ◽  
Label Free ◽  
Wound Area ◽  
Spectrometry Analysis ◽  
Quantitative Expression ◽  
Venous Ulcers

ABSTRACTSeeking and identifying biomarker molecules in inflammatory exudate of chronic venous ulcers (CVUs) can aid health professionals in the healing prognosis. The therapeutic failure or cure is related to the quantitative expression of determinate proteins. This work aimed to identify the proteins expressed in inflammatory exudates from CVUs and correlate them with reduction or increase in the wound size. For 90 days, 28 participants that received standard treatment for 37 CVUs were monitored. The inflammatory exudates were collected before treatment initiation (T=0) and analyzed via the Label-free Shotgun. After 90 days the wound area was reduced in 25 (67.6%) of them. Mass spectrometry analysis of all the inflammatory exudates showed four proteins differentially expressed and related to favorable or unfavorable evolution of the healing process. Complement C3 and ceruloplasmin were identified in all the lesions analyzed and were expressed differentially in lesions that presented diminished area in the studied period. Apoliprotein A1 and neutrophil defensin-1 presented differential expression in ulcers that either did not diminish or augmented their wound area through 90 days. These results suggest that Complement C3, Ceruloplasmin, Apoliprotein A1 and Neutrophil-defensin-1 proteins are potential candidate molecules for prognostic healing markers in chronic venous ulcers.

Quantitative proteomics identifies FOLR1 to drive sorafenib resistance via activating autophagy in hepatocellular carcinoma cells

2021 ◽  
Author(s):  
Hongwei Chu ◽  
Changqing Wu ◽  
Qun Zhao ◽  
Rui Sun ◽  
Kuo Yang ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Folate Receptor ◽  
Mass Spectrometry Analysis ◽  
Label Free ◽  
Spectrometry Analysis ◽  
Underlying Mechanisms ◽  
Related Proteins ◽  
Hcc Cells

Abstract Sorafenib is commonly used to treat advanced human hepatocellular carcinoma (HCC). However, clinical efficacy has been limited by drug resistance. In this study, we used label-free quantitative proteomic analysis to systematically investigate the underlying mechanisms of sorafenib resistance in HCC cells. A total of 1709 proteins were confidently quantified. Among them, 89 were differentially expressed, and highly enriched in the processes of cell-cell adhesion, negative regulation of apoptosis, response to drug and metabolic processes involving in sorafenib resistance. Notably, folate receptor α (FOLR1) was found to be significantly upregulated in resistant HCC cells. In addition, in-vitro studies showed that overexpression of FOLR1 decreased the sensitivity of HCC cells to sorafenib, whereas siRNA-directed knockdown of FOLR1 increased the sensitivity of HCC cells to sorafenib. Immunoprecipitation-mass spectrometry analysis suggested a strong link between FOLR1 and autophagy related proteins. Further biological experiments found that FOLR1-related sorafenib resistance was accompanied by the activation of autophagy, whereas inhibition of autophagy significantly reduced FOLR1-induced cell resistance. These results suggest the driving role of FOLR1 in HCC resistance to sorafenib, which may be exerted through FOLR1-induced autophagy. Therefore, this study may provide new insights into understanding the mechanism of sorafenib resistance.

scholarly journals The Oligopeptide Transport System Is Essential for the Development of Natural Competence in Streptococcus thermophilus Strain LMD-9

2009 ◽  
Vol 191 (14) ◽  
pp. 4647-4655 ◽  
Author(s):  
Rozenn Gardan ◽  
Colette Besset ◽  
Alain Guillot ◽  
Christophe Gitton ◽  
Véronique Monnet
Keyword(s):  
Quorum Sensing ◽  
Streptococcus Thermophilus ◽  
Defined Medium ◽  
Mass Spectrometry Analysis ◽  
Transport Systems ◽  
Label Free ◽  
Spectrometry Analysis ◽  
Proteomic Approach ◽  
Liquid Chromatography Tandem Mass ◽  
Oligopeptide Transport

ABSTRACT In gram-positive bacteria, oligopeptide transport systems, called Opp or Ami, play a role in nutrition but are also involved in the internalization of signaling peptides that take part in the functioning of quorum-sensing pathways. Our objective was to reveal functions that are controlled by Ami via quorum-sensing mechanisms in Streptococcus thermophilus, a nonpathogenic bacterium widely used in dairy technology in association with other bacteria. Using a label-free proteomic approach combining one-dimensional electrophoresis with liquid chromatography-tandem mass spectrometry analysis, we compared the proteome of the S. thermophilus LMD-9 to that of a mutant deleted for the subunits C, D, and E of the ami operon. Both strains were grown in a chemically defined medium (CDM) without peptides. We focused our attention on proteins that were no more detected in the ami deletion mutant. In addition to the three subunits of the Ami transporter, 17 proteins fulfilled this criterion and, among them, 7 were similar to proteins that have been identified as essential for transformation in S. pneumoniae. These results led us to find a condition of growth, the early exponential state in CDM, that allows natural transformation in S. thermophilus LMD-9 to turn on spontaneously. Cells were not competent in M17 rich medium. Furthermore, we demonstrated that the Ami transporter controls the triggering of the competence state through the control of the transcription of comX, itself controlling the transcription of late competence genes. We also showed that one of the two oligopeptide-binding proteins of strain LMD-9 plays the predominant role in the control of competence.

scholarly journals Microbial Desulfurization of Gasoline in a Mycobacterium goodii X7B Immobilized-Cell System

2005 ◽  
Vol 71 (1) ◽  
pp. 276-281 ◽  
Author(s):  
Fuli Li ◽  
Ping Xu ◽  
Jinhui Feng ◽  
Ling Meng ◽  
Yuan Zheng ◽  
...  
Keyword(s):  
Sulfur Content ◽  
Immobilized Cells ◽  
Industrial Applications ◽  
Cell System ◽  
Mass Spectrometry Analysis ◽  
Organic Sulfur ◽  
Potential Candidate ◽  
Immobilized Cell ◽  
Spectrometry Analysis ◽  
Mycobacterium Goodii

ABSTRACT Mycobacterium goodii X7B, which had been primarily isolated as a bacterial strain capable of desulfurizing dibenzothiophene to produce 2-hydroxybiphenyl via the 4S pathway, was also found to desulfurize benzothiophene. The desulfurization product was identified as o-hydroxystyrene by gas chromatography (GC)-mass spectrometry analysis. This strain appeared to have the ability to remove organic sulfur from a broad range of sulfur species in gasoline. When Dushanzi straight-run gasoline (DSRG227) containing various organic sulfur compounds was treated with immobilized cells of strain X7B for 24 h, the total sulfur content significantly decreased, from 227 to 71 ppm at 40�C. GC flame ionization detection and GC atomic emission detection analysis were used to qualitatively evaluate the effects of M. goodii X7B treatment on the contents of gasoline. In addition, when immobilized cells were incubated at 40�C with DSRG275, the sulfur content decreased from 275 to 54 ppm in two consecutive reactions. With this excellent efficiency, strain X7B is considered a good potential candidate for industrial applications for the biodesulfurization of gasoline.

Label-free quantitative proteomic analysis of the YAP/TAZ interactome

2014 ◽  
Vol 306 (9) ◽  
pp. C805-C818 ◽  
Author(s):  
Priyanka Kohli ◽  
Malte P. Bartram ◽  
Sandra Habbig ◽  
Caroline Pahmeyer ◽  
Tobias Lamkemeyer ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Interactions ◽  
Affinity Purification ◽  
Single Copy ◽  
Single Step ◽  
Mass Spectrometry Analysis ◽  
Single Shot ◽  
Label Free ◽  
Protein Protein Interactions ◽  
Spectrometry Analysis

The function of an individual protein is typically defined by protein-protein interactions orchestrating the formation of large complexes critical for a wide variety of biological processes. Over the last decade the analysis of purified protein complexes by mass spectrometry became a key technique to identify protein-protein interactions. We present a fast and straightforward approach for analyses of interacting proteins combining a Flp-in single-copy cellular integration system and single-step affinity purification with single-shot mass spectrometry analysis. We applied this protocol to the analysis of the YAP and TAZ interactome. YAP and TAZ are the downstream effectors of the mammalian Hippo tumor suppressor pathway. Our study provides comprehensive interactomes for both YAP and TAZ and does not only confirm the majority of previously described interactors but, strikingly, revealed uncharacterized interaction partners that affect YAP/TAZ TEAD-dependent transcription. Among these newly identified candidates are Rassf8, thymopoetin, and the transcription factors CCAAT/enhancer-binding protein (C/EBP)β/δ and core-binding factor subunit β (Cbfb). In addition, our data allowed insights into complex stoichiometry and uncovered discrepancies between the YAP and TAZ interactomes. Taken together, the stringent approach presented here could help to significantly sharpen the understanding of protein-protein networks.

Comparative Whey Proteome Profiling of Donkey Milk With Human and Cow Milk

2020 ◽  
Author(s):  
Xinhao Zhang ◽  
Guimiao Jiang ◽  
Chuanliang Ji ◽  
Haijing Li ◽  
Yantao Wang ◽  
...  
Keyword(s):  
Cholesterol Metabolism ◽  
Whey Proteins ◽  
Bioinformatic Analysis ◽  
Mass Spectrometry Analysis ◽  
Cow Milk ◽  
Label Free ◽  
Donkey Milk ◽  
Milk Whey ◽  
Spectrometry Analysis ◽  
Kegg Pathways

Abstract Background: Donkey milk (DM), similar to human milk (HM) in compositions, has been suggested as the best potential hypoallergenic replacement diet for babies suffering from cow milk (CM) protein allergens. Despite advances in proteomics technologies, studies of the DM whey proteome are relatively sparse. In this study, label-free mass spectrometry analysis was conducted to quantitatively identify the differentially expressed whey proteins (DEPs) in DM vs HM group and DM vs CM group. Results: In total, 249 and 418 DEPs were found in these two groups respectively. DEPs were then subjected to intensive bioinformatic analysis. Results revealed that the majority of DEPs participated in lipid metabolic process, regulation of cytokine production, chemical homeostasis and catabolic process. Kyoto Encyclopedia of Gene and Genomes (KEGG) pathways analysis found that these DEPs mainly participated in complement and coagulation cascades, and cholesterol metabolism. Conclusion: These results may provide valuable information in the composition of milk whey proteins in DM, HM and CM, especially for low abundant components, and expand our knowledge of different biological functions between DM and HM or CM.

scholarly journals Urinary biomarkers for the diagnosis of cervical cancer by quantitative label‑free mass spectrometry analysis

2019 ◽  
Author(s):  
Daranee Chokchaichamnankit ◽  
Kamolwan Watcharatanyatip ◽  
Pantipa Subhasitanont ◽  
Churat Weeraphan ◽  
Siriporn Keeratichamroen ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Cervical Cancer ◽  
Urinary Biomarkers ◽  
Mass Spectrometry Analysis ◽  
Label Free ◽  
Spectrometry Analysis

scholarly journals Possible proteomic biomarkers for the detection of pancreatic cancer in oral fluids

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
O. Deutsch ◽  
Y. Haviv ◽  
G. Krief ◽  
N. Keshet ◽  
R. Westreich ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Pancreatic Cancer ◽  
Mass Spectrometry Analysis ◽  
Label Free ◽  
Two Dimensional Gel Electrophoresis ◽  
Spectrometry Analysis ◽  
Oral Fluids ◽  
Liquid Chromatography Tandem Mass ◽  
Differential Expression Profile ◽  
Auc Value

AbstractThe 80% mortality rate of pancreatic-cancer (PC) makes early diagnosis a challenge. Oral fluids (OF) may be considered the ultimate body fluid for non-invasive examinations. We have developed techniques to improve visualization of minor OF proteins thereby overcoming major barriers to using OF as a diagnostic fluid. The aim of this study was to establish a short discriminative panel of OF biomarkers for the detection of PC. Unstimulated OF were collected from PC patients and controls (n = 30). High-abundance-proteins were depleted and the remaining proteins were analyzed by two-dimensional-gel-electrophoresis and quantitative dimethylation-liquid-chromatography-tandem mass-spectrometry. Label-free quantitative-mass-spectrometry analysis (qMS) was performed on 20 individual samples (n = 20). More than 100 biomarker candidates were identified in OF samples, and 21 had a highly differential expression profile. qMS analysis yielded a ROC-plot AUC value of 0.91 with 90.0% sensitivity and specificity for a combination of five biomarker candidates. We found a combination of five biomarkers for PC. Most of these proteins are known to be related to PC or other gastric cancers, but have never been detected in OF. This study demonstrates the importance of novel OF depletion methodologies for increased protein visibility and highlights the clinical applicability of OF as a diagnostic fluid.

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