Analysis of differentially expressed novel post-translational modifications of plasma apolipoprotein E in Taiwanese females with breast cancer

Yih Huei Uen, Chen Chung Liao, Jung Chun Lin, Yi Hsuan Pan, Yi Chung Liu, You Chia Chen, Wei Jung Chen, Chih Chun Tai, Kuan Wei Lee, Yun Ru Liu, Hung Tse Lin, Ching Yu Lin

研究成果: 雜誌貢獻文章

8 引文 (Scopus)

摘要

APOE ε2 or ε4 alleles being used as indicators of breast cancer risk are controversial in Taiwanese females. We provide a concept for relative comparisons of post-translational modifications (PTMs) of plasma apolipoprotein E (ApoE) between normal controls and breast cancer patients to investigate the association of ApoE with breast cancer risk. APOE polymorphisms (ApoE isoforms) were not assessed in this study. The relative modification ratio (%) of 15 targeted and 21 modified peptides were evaluated by 1D SDS-PAGE, in-gel digestion, and label-free nano-LC/MS to compare normal controls with breast cancer patients. Plasma levels of the ApoE protein did not significantly differ between normal controls and breast cancer patients. Eleven sites with novel PTMs were identified from 7 pairs of differentially expressed targeted and modified peptides according to the relative modification ratio including methylation at the E3 (↑1.45-fold), E7 (↑1.45-fold), E11 (↑1.19-fold), E77 (↑2.02-fold), E87 (↑2.02-fold), and Q98 (↑1.62-fold) residues; dimethylation at the Q187 (↑1.44-fold) residue; dihydroxylation at the R92 (↑1.25-fold), K95 (↑1.25-fold), and R103 (↑1.25-fold) residues; and glycosylation at the S129 (↑1.14-fold) residue. The clustered methylation and dihydroxylation of plasma ApoE proteins may play a role in breast cancer.
原文英語
頁(從 - 到)252-262
頁數11
期刊Journal of Proteomics
126
DOIs
出版狀態已發佈 - 八月 3 2015

指紋

Apolipoproteins E
Post Translational Protein Processing
Breast Neoplasms
Plasmas
Methylation
Glycosylation
Peptides
Polymorphism
Labels
Protein Isoforms
Proteins
Gels
Association reactions
Polyacrylamide Gel Electrophoresis
Digestion
Alleles

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics

引用此文

Analysis of differentially expressed novel post-translational modifications of plasma apolipoprotein E in Taiwanese females with breast cancer. / Uen, Yih Huei; Liao, Chen Chung; Lin, Jung Chun; Pan, Yi Hsuan; Liu, Yi Chung; Chen, You Chia; Chen, Wei Jung; Tai, Chih Chun; Lee, Kuan Wei; Liu, Yun Ru; Lin, Hung Tse; Lin, Ching Yu.

於: Journal of Proteomics, 卷 126, 03.08.2015, p. 252-262.

研究成果: 雜誌貢獻文章

Uen, Yih Huei ; Liao, Chen Chung ; Lin, Jung Chun ; Pan, Yi Hsuan ; Liu, Yi Chung ; Chen, You Chia ; Chen, Wei Jung ; Tai, Chih Chun ; Lee, Kuan Wei ; Liu, Yun Ru ; Lin, Hung Tse ; Lin, Ching Yu. / Analysis of differentially expressed novel post-translational modifications of plasma apolipoprotein E in Taiwanese females with breast cancer. 於: Journal of Proteomics. 2015 ; 卷 126. 頁 252-262.
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abstract = "APOE ε2 or ε4 alleles being used as indicators of breast cancer risk are controversial in Taiwanese females. We provide a concept for relative comparisons of post-translational modifications (PTMs) of plasma apolipoprotein E (ApoE) between normal controls and breast cancer patients to investigate the association of ApoE with breast cancer risk. APOE polymorphisms (ApoE isoforms) were not assessed in this study. The relative modification ratio ({\%}) of 15 targeted and 21 modified peptides were evaluated by 1D SDS-PAGE, in-gel digestion, and label-free nano-LC/MS to compare normal controls with breast cancer patients. Plasma levels of the ApoE protein did not significantly differ between normal controls and breast cancer patients. Eleven sites with novel PTMs were identified from 7 pairs of differentially expressed targeted and modified peptides according to the relative modification ratio including methylation at the E3 (↑1.45-fold), E7 (↑1.45-fold), E11 (↑1.19-fold), E77 (↑2.02-fold), E87 (↑2.02-fold), and Q98 (↑1.62-fold) residues; dimethylation at the Q187 (↑1.44-fold) residue; dihydroxylation at the R92 (↑1.25-fold), K95 (↑1.25-fold), and R103 (↑1.25-fold) residues; and glycosylation at the S129 (↑1.14-fold) residue. The clustered methylation and dihydroxylation of plasma ApoE proteins may play a role in breast cancer.",
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author = "Uen, {Yih Huei} and Liao, {Chen Chung} and Lin, {Jung Chun} and Pan, {Yi Hsuan} and Liu, {Yi Chung} and Chen, {You Chia} and Chen, {Wei Jung} and Tai, {Chih Chun} and Lee, {Kuan Wei} and Liu, {Yun Ru} and Lin, {Hung Tse} and Lin, {Ching Yu}",
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T1 - Analysis of differentially expressed novel post-translational modifications of plasma apolipoprotein E in Taiwanese females with breast cancer

AU - Uen, Yih Huei

AU - Liao, Chen Chung

AU - Lin, Jung Chun

AU - Pan, Yi Hsuan

AU - Liu, Yi Chung

AU - Chen, You Chia

AU - Chen, Wei Jung

AU - Tai, Chih Chun

AU - Lee, Kuan Wei

AU - Liu, Yun Ru

AU - Lin, Hung Tse

AU - Lin, Ching Yu

PY - 2015/8/3

Y1 - 2015/8/3

N2 - APOE ε2 or ε4 alleles being used as indicators of breast cancer risk are controversial in Taiwanese females. We provide a concept for relative comparisons of post-translational modifications (PTMs) of plasma apolipoprotein E (ApoE) between normal controls and breast cancer patients to investigate the association of ApoE with breast cancer risk. APOE polymorphisms (ApoE isoforms) were not assessed in this study. The relative modification ratio (%) of 15 targeted and 21 modified peptides were evaluated by 1D SDS-PAGE, in-gel digestion, and label-free nano-LC/MS to compare normal controls with breast cancer patients. Plasma levels of the ApoE protein did not significantly differ between normal controls and breast cancer patients. Eleven sites with novel PTMs were identified from 7 pairs of differentially expressed targeted and modified peptides according to the relative modification ratio including methylation at the E3 (↑1.45-fold), E7 (↑1.45-fold), E11 (↑1.19-fold), E77 (↑2.02-fold), E87 (↑2.02-fold), and Q98 (↑1.62-fold) residues; dimethylation at the Q187 (↑1.44-fold) residue; dihydroxylation at the R92 (↑1.25-fold), K95 (↑1.25-fold), and R103 (↑1.25-fold) residues; and glycosylation at the S129 (↑1.14-fold) residue. The clustered methylation and dihydroxylation of plasma ApoE proteins may play a role in breast cancer.

AB - APOE ε2 or ε4 alleles being used as indicators of breast cancer risk are controversial in Taiwanese females. We provide a concept for relative comparisons of post-translational modifications (PTMs) of plasma apolipoprotein E (ApoE) between normal controls and breast cancer patients to investigate the association of ApoE with breast cancer risk. APOE polymorphisms (ApoE isoforms) were not assessed in this study. The relative modification ratio (%) of 15 targeted and 21 modified peptides were evaluated by 1D SDS-PAGE, in-gel digestion, and label-free nano-LC/MS to compare normal controls with breast cancer patients. Plasma levels of the ApoE protein did not significantly differ between normal controls and breast cancer patients. Eleven sites with novel PTMs were identified from 7 pairs of differentially expressed targeted and modified peptides according to the relative modification ratio including methylation at the E3 (↑1.45-fold), E7 (↑1.45-fold), E11 (↑1.19-fold), E77 (↑2.02-fold), E87 (↑2.02-fold), and Q98 (↑1.62-fold) residues; dimethylation at the Q187 (↑1.44-fold) residue; dihydroxylation at the R92 (↑1.25-fold), K95 (↑1.25-fold), and R103 (↑1.25-fold) residues; and glycosylation at the S129 (↑1.14-fold) residue. The clustered methylation and dihydroxylation of plasma ApoE proteins may play a role in breast cancer.

KW - Apolipoprotein E

KW - Breast cancer

KW - Extracted ion chromatogram

KW - Label-free relative quantification

KW - Plasma

KW - Post-translational modification

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