scholarly journals Peer Review #1 of "Plasma proteomic analysis of systemic lupus erythematosus patients using liquid chromatography/tandem mass spectrometry with label-free quantification (v0.1)"

2018 ◽  
Keyword(s):  
Mass Spectrometry ◽  
Systemic Lupus Erythematosus ◽  
Lupus Erythematosus ◽  
Tandem Mass ◽  
Label Free ◽  
Systemic Lupus ◽  
Label Free Quantification ◽  
Chromatography Tandem Mass Spectrometry ◽  
Liquid Chromatography Tandem Mass ◽  
Free Quantification

scholarly journals Plasma proteomic analysis of systemic lupus erythematosus patients using liquid chromatography/tandem mass spectrometry with label-free quantification

PeerJ ◽  
2018 ◽  
Vol 6 ◽  
pp. e4730 ◽  
Author(s):  
Rashmi Madda ◽  
Shih-Chang Lin ◽  
Wei-Hsin Sun ◽  
Shir-Ly Huang
Keyword(s):  
Lupus Erythematosus ◽  
Inflammatory Responses ◽  
Tandem Mass ◽  
Healthy Controls ◽  
Label Free ◽  
Systemic Lupus ◽  
Label Free Quantification ◽  
Chromatography Tandem Mass Spectrometry ◽  
Liquid Chromatography Tandem Mass ◽  
Free Quantification

Context Systemic lupus erythematosus (SLE) is a chronic inflammatory autoimmune disease with unknown etiology. Objective Human plasma is comprised of over 10 orders of magnitude concentration of proteins and tissue leakages. The changes in the abundance of these proteins have played an important role in various human diseases. Therefore, the research objective of this study is to identify the significantly altered expression levels of plasma proteins from SLE patients compared with healthy controls using proteomic analysis. The plasma proteome profiles of both SLE patients and controls were compared. Methods A total of 19 active SLE patients and 12 healthy controls plasma samples were analyzed using high-resolution electrospray ionization liquid chromatography-tandem mass spectrometry (LC-ESI-MS/MS) followed by label-free quantification. Results A total of 19 proteins showed a significant level of expression in the comparative LC-ESI-MS/MS triplicate analysis; among these, 14 proteins had >1.5- to three-fold up-regulation and five had <0.2- to 0.6-fold down-regulation. Gene ontology and DAVID (Database Annotation Visualization, and Integrated Discovery) functional enrichment analysis revealed that these proteins are involved in several important biological processes including acute phase inflammatory responses, complement activation, hemostasis, and immune system regulation. Conclusion Our study identified a group of differentially expressed proteins in the plasma of SLE patients that are involved in the imbalance of the immune system and inflammatory responses. Therefore, these findings may have the potential to be used as prognostic/diagnostic markers for SLE disease assessment or disease monitoring.

Analysis of the uterine flush fluid proteome of healthy mares and mares with endometritis or fibrotic endometrial degeneration

2020 ◽  
Vol 32 (6) ◽  
pp. 572 ◽  
Author(s):  
Mariana Diel de Amorim ◽  
Firdous A. Khan ◽  
Tracey S. Chenier ◽  
Elizabeth L. Scholtz ◽  
M. Anthony Hayes
Keyword(s):  
Mass Spectrometry ◽  
Liquid Chromatography ◽  
Tandem Mass ◽  
Label Free ◽  
Chromatography Tandem Mass Spectrometry ◽  
Uterine Health ◽  
Liquid Chromatography Tandem Mass ◽  
Specific Proteins ◽  
Health And Disease ◽  
Flush Fluid

The objective of this study was to evaluate the differences in the uterine flush fluid proteome between healthy mares and mares with endometritis or fibrotic endometrial degeneration (FED). Uterine flush fluid samples were collected from healthy mares (n=8; oestrus n=5 and dioestrus n=3) and mares with endometritis (n=23; oestrus n=14 and dioestrus n=9) or FED (n=7; oestrus n=6 and dioestrus n=1). Proteomic analysis was performed using label-free liquid chromatography–tandem mass spectrometry. Of 216 proteins identified during oestrus, 127 were common to all three groups, one protein was exclusively detected in healthy mares, 47 proteins were exclusively detected in mares with endometritis and four proteins were exclusively detected in mares with FED. Of 188 proteins identified during dioestrus, 113 proteins were common between healthy mares and mares with endometritis, eight proteins were exclusively detected in healthy mares and 67 proteins were exclusively detected in mares with endometritis. Quantitative analysis revealed a subset of proteins differing in abundance between the three groups during oestrus and between healthy mares and mares with endometritis during dioestrus. These results provide a springboard for evaluation of specific proteins as biomarkers of uterine health and disease and for investigation of their roles in the establishment and maintenance of pregnancy.

Analysis of the human pituitary proteome by data independent label-free liquid chromatography tandem mass spectrometry

PROTEOMICS ◽  
2011 ◽  
Vol 11 (3) ◽  
pp. 495-500 ◽  
Author(s):  
Divya Krishnamurthy ◽  
Yishai Levin ◽  
Laura W. Harris ◽  
Yagnesh Umrania ◽  
Sabine Bahn ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Liquid Chromatography ◽  
Tandem Mass Spectrometry ◽  
Tandem Mass ◽  
Label Free ◽  
Human Pituitary ◽  
Chromatography Tandem Mass Spectrometry ◽  
Liquid Chromatography Tandem Mass

Simultaneous determination of cyclophosphamide and 4-hydroxycyclophosphamide in human plasma by high-performance liquid chromatography coupled with electrospray ionization tandem mass spectrometry – application to Chinese systemic lupus erythematosus patients

2011 ◽  
Vol 49 (12) ◽  
Author(s):  
Wenying Shu ◽  
Xueding Wang ◽  
Xiuyan Yang ◽  
Liuqin Liang ◽  
Jiali Li ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Systemic Lupus Erythematosus ◽  
Tandem Mass Spectrometry ◽  
Electrospray Ionization ◽  
Human Plasma ◽  
Lupus Erythematosus ◽  
Tandem Mass ◽  
Systemic Lupus ◽  
Limit Of Quantification ◽  
Ionization Tandem Mass Spectrometry

AbstractA pharmacogenomics study of cyclophosphamide in systemic lupus erythematosus patients is being conducted in our laboratory in which the plasma concentrations of cyclophosphamide and its active metabolite 4-hydroxycyclophosphamide should be assayed rapidly and sensitively.A rapid, stable and sensitive liquid chromato-graphy/electrospray ionization tandem mass spectrometry method was developed to simultaneously determine cyclophosphamide and 4-hydroxycyclophosphamide in human plasma with ifosfomide as an internal standard. After a protein precipitation with cold acetonitrile and stabilization of 4-hydroxycyclophosphamide by ansyldrazine and extraction with ethyl acetate, separation was performed on a C18 3.5 μm 2.1×50 mm column with mobile phase of acetonitrile and water (50:50, v/v) with 0.1% formic acid at 200 μL/min. The chromatographic run time was 3 min.The linear calibration curves ranged from 5 to 5000 ng/mL for cyclophosphamide and 5–500 ng/mL for 4-hydroxycyclophosphamide. The recoveries of the liquid extraction were 54.5%–58.5% for cyclophosphamide and 103.5%–105.5% for 4-hydroxycyclophosphamide. The lower limit of quantification was 5 ng/mL for both analytes. The intra- and inter-day precision was <15% for quality control samples at 4000, 500, 50 ng/mL for cyclophosphamide and 4-hydroxycyclophosphamide at 400, 100, 20 ng/mL. The method was applied in this pharmacogenomics study in Chinese systemic lupus erythematosus patients treated with low-dose cyclophosphamide.The method was efficient with shorter running time and lower limit of quantification compared to previous reports and has been successfully applied in this pharmacogenomics study.

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