Isotypes of autoantibodies against differentially expressed novel malondialdehyde-modified peptide adducts in serum of Taiwanese women with rheumatoid arthritis

Chen Chung Liao, Yu Sheng Chang, Chao Wen Cheng, Wei Ming Chi, Kai Leun Tsai, Wei Jung Chen, Ting Shuan Kung, Chih Chun Tai, Yi Fang Lin, Hung Tse Lin, Yi Ying Lu, Ching Yu Lin

研究成果: 雜誌貢獻文章

1 引文 (Scopus)

摘要

This study identified and validated four differentially expressed novel malondialdehyde (MDA)-modified peptide adducts and evaluated autoantibodies against native and MDA-modified peptides among Taiwanese women patients with rheumatoid arthritis (RA), osteoarthritis (OA) and healthy controls (HCs). Ig kappa chain C region76–99, alpha-1-antitrypsin284–298, alpha-2-macroglobulin824–841, and apolipoprotein B-1004022–4040 exhibiting 2-fold differences in relative modification ratios were identified by concanavalin A (Con A) affinity chromatography, 1D SDS-PAGE, in-gel digestion, nano-LC/MS/MS and nano-LC/MS using pooled serum-derived Con A-captured proteins from 9 RA and 9 age-matched HCs. Furthermore, the levels of proteins, serum MDA, and MDA-modified protein adducts were further validated against individual serum from 20 RA and 20 HCs, and autoantibodies against native and their MDA-modified peptides used 45 RA, 30 OA and 45 HCs. Levels of serum MDA and MDA-modified protein adducts were significantly higher in RA than HCs but protein levels were not significantly different. Serum Igs G and M against MDA-modified peptides showed better diagnostic performance in differentiating among patients with RA, OA and HCs, with an area under the receiver operating characteristic curve of 0.96–0.98, sensitivity of 88.9%–97.8%, and specificity of 88.9%–100%. Autoantibodies against MDA-modified epitopes become useful clinical biomarkers for RA. Biological significance By using a label-free relative quantitative proteomic analysis of concanavalin A (Con A)-bound serum samples, the current study discovered and validated malondialdehyde (MDA)-modified peptide adducts as novel biomarkers for differentiating between rheumatoid arthritis (RA) patients and healthy controls (HCs). In addition, the serum levels of MDA, proteins, and MDA-modified protein adducts as well as the MDA modification of proteins were determined. Isotypes of autoantibodies against MDA-modified peptide adducts can be used as serological biomarkers for further discriminating among RA patients, osteoarthritis patients and HCs. This strategy can become the basis for identifying potential diagnostic and pathological biomarkers for RA.
原文英語
頁(從 - 到)141-150
頁數10
期刊Journal of Proteomics
170
DOIs
出版狀態已發佈 - 一月 6 2018

指紋

Malondialdehyde
Autoantibodies
Rheumatoid Arthritis
Peptides
Serum
Biomarkers
Osteoarthritis
Concanavalin A
Proteins
Affinity chromatography
Level control
Apolipoproteins B
Affinity Chromatography
ROC Curve
Proteomics
Labels
Blood Proteins
Epitopes
Polyacrylamide Gel Electrophoresis
Digestion

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

引用此文

Isotypes of autoantibodies against differentially expressed novel malondialdehyde-modified peptide adducts in serum of Taiwanese women with rheumatoid arthritis. / Liao, Chen Chung; Chang, Yu Sheng; Cheng, Chao Wen; Chi, Wei Ming; Tsai, Kai Leun; Chen, Wei Jung; Kung, Ting Shuan; Tai, Chih Chun; Lin, Yi Fang; Lin, Hung Tse; Lu, Yi Ying; Lin, Ching Yu.

於: Journal of Proteomics, 卷 170, 06.01.2018, p. 141-150.

研究成果: 雜誌貢獻文章

Liao, Chen Chung ; Chang, Yu Sheng ; Cheng, Chao Wen ; Chi, Wei Ming ; Tsai, Kai Leun ; Chen, Wei Jung ; Kung, Ting Shuan ; Tai, Chih Chun ; Lin, Yi Fang ; Lin, Hung Tse ; Lu, Yi Ying ; Lin, Ching Yu. / Isotypes of autoantibodies against differentially expressed novel malondialdehyde-modified peptide adducts in serum of Taiwanese women with rheumatoid arthritis. 於: Journal of Proteomics. 2018 ; 卷 170. 頁 141-150.
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abstract = "This study identified and validated four differentially expressed novel malondialdehyde (MDA)-modified peptide adducts and evaluated autoantibodies against native and MDA-modified peptides among Taiwanese women patients with rheumatoid arthritis (RA), osteoarthritis (OA) and healthy controls (HCs). Ig kappa chain C region76–99, alpha-1-antitrypsin284–298, alpha-2-macroglobulin824–841, and apolipoprotein B-1004022–4040 exhibiting 2-fold differences in relative modification ratios were identified by concanavalin A (Con A) affinity chromatography, 1D SDS-PAGE, in-gel digestion, nano-LC/MS/MS and nano-LC/MS using pooled serum-derived Con A-captured proteins from 9 RA and 9 age-matched HCs. Furthermore, the levels of proteins, serum MDA, and MDA-modified protein adducts were further validated against individual serum from 20 RA and 20 HCs, and autoantibodies against native and their MDA-modified peptides used 45 RA, 30 OA and 45 HCs. Levels of serum MDA and MDA-modified protein adducts were significantly higher in RA than HCs but protein levels were not significantly different. Serum Igs G and M against MDA-modified peptides showed better diagnostic performance in differentiating among patients with RA, OA and HCs, with an area under the receiver operating characteristic curve of 0.96–0.98, sensitivity of 88.9{\%}–97.8{\%}, and specificity of 88.9{\%}–100{\%}. Autoantibodies against MDA-modified epitopes become useful clinical biomarkers for RA. Biological significance By using a label-free relative quantitative proteomic analysis of concanavalin A (Con A)-bound serum samples, the current study discovered and validated malondialdehyde (MDA)-modified peptide adducts as novel biomarkers for differentiating between rheumatoid arthritis (RA) patients and healthy controls (HCs). In addition, the serum levels of MDA, proteins, and MDA-modified protein adducts as well as the MDA modification of proteins were determined. Isotypes of autoantibodies against MDA-modified peptide adducts can be used as serological biomarkers for further discriminating among RA patients, osteoarthritis patients and HCs. This strategy can become the basis for identifying potential diagnostic and pathological biomarkers for RA.",
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AU - Chang, Yu Sheng

AU - Cheng, Chao Wen

AU - Chi, Wei Ming

AU - Tsai, Kai Leun

AU - Chen, Wei Jung

AU - Kung, Ting Shuan

AU - Tai, Chih Chun

AU - Lin, Yi Fang

AU - Lin, Hung Tse

AU - Lu, Yi Ying

AU - Lin, Ching Yu

PY - 2018/1/6

Y1 - 2018/1/6

N2 - This study identified and validated four differentially expressed novel malondialdehyde (MDA)-modified peptide adducts and evaluated autoantibodies against native and MDA-modified peptides among Taiwanese women patients with rheumatoid arthritis (RA), osteoarthritis (OA) and healthy controls (HCs). Ig kappa chain C region76–99, alpha-1-antitrypsin284–298, alpha-2-macroglobulin824–841, and apolipoprotein B-1004022–4040 exhibiting 2-fold differences in relative modification ratios were identified by concanavalin A (Con A) affinity chromatography, 1D SDS-PAGE, in-gel digestion, nano-LC/MS/MS and nano-LC/MS using pooled serum-derived Con A-captured proteins from 9 RA and 9 age-matched HCs. Furthermore, the levels of proteins, serum MDA, and MDA-modified protein adducts were further validated against individual serum from 20 RA and 20 HCs, and autoantibodies against native and their MDA-modified peptides used 45 RA, 30 OA and 45 HCs. Levels of serum MDA and MDA-modified protein adducts were significantly higher in RA than HCs but protein levels were not significantly different. Serum Igs G and M against MDA-modified peptides showed better diagnostic performance in differentiating among patients with RA, OA and HCs, with an area under the receiver operating characteristic curve of 0.96–0.98, sensitivity of 88.9%–97.8%, and specificity of 88.9%–100%. Autoantibodies against MDA-modified epitopes become useful clinical biomarkers for RA. Biological significance By using a label-free relative quantitative proteomic analysis of concanavalin A (Con A)-bound serum samples, the current study discovered and validated malondialdehyde (MDA)-modified peptide adducts as novel biomarkers for differentiating between rheumatoid arthritis (RA) patients and healthy controls (HCs). In addition, the serum levels of MDA, proteins, and MDA-modified protein adducts as well as the MDA modification of proteins were determined. Isotypes of autoantibodies against MDA-modified peptide adducts can be used as serological biomarkers for further discriminating among RA patients, osteoarthritis patients and HCs. This strategy can become the basis for identifying potential diagnostic and pathological biomarkers for RA.

AB - This study identified and validated four differentially expressed novel malondialdehyde (MDA)-modified peptide adducts and evaluated autoantibodies against native and MDA-modified peptides among Taiwanese women patients with rheumatoid arthritis (RA), osteoarthritis (OA) and healthy controls (HCs). Ig kappa chain C region76–99, alpha-1-antitrypsin284–298, alpha-2-macroglobulin824–841, and apolipoprotein B-1004022–4040 exhibiting 2-fold differences in relative modification ratios were identified by concanavalin A (Con A) affinity chromatography, 1D SDS-PAGE, in-gel digestion, nano-LC/MS/MS and nano-LC/MS using pooled serum-derived Con A-captured proteins from 9 RA and 9 age-matched HCs. Furthermore, the levels of proteins, serum MDA, and MDA-modified protein adducts were further validated against individual serum from 20 RA and 20 HCs, and autoantibodies against native and their MDA-modified peptides used 45 RA, 30 OA and 45 HCs. Levels of serum MDA and MDA-modified protein adducts were significantly higher in RA than HCs but protein levels were not significantly different. Serum Igs G and M against MDA-modified peptides showed better diagnostic performance in differentiating among patients with RA, OA and HCs, with an area under the receiver operating characteristic curve of 0.96–0.98, sensitivity of 88.9%–97.8%, and specificity of 88.9%–100%. Autoantibodies against MDA-modified epitopes become useful clinical biomarkers for RA. Biological significance By using a label-free relative quantitative proteomic analysis of concanavalin A (Con A)-bound serum samples, the current study discovered and validated malondialdehyde (MDA)-modified peptide adducts as novel biomarkers for differentiating between rheumatoid arthritis (RA) patients and healthy controls (HCs). In addition, the serum levels of MDA, proteins, and MDA-modified protein adducts as well as the MDA modification of proteins were determined. Isotypes of autoantibodies against MDA-modified peptide adducts can be used as serological biomarkers for further discriminating among RA patients, osteoarthritis patients and HCs. This strategy can become the basis for identifying potential diagnostic and pathological biomarkers for RA.

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