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

doi:10.1016/j.jprot.2015.05.038

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

Research output: Contribution to journal › Article › peer-review

18 Citations (Scopus)

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.

Original language	English
Pages (from-to)	252-262
Number of pages	11
Journal	Journal of Proteomics
Volume	126
DOIs	https://doi.org/10.1016/j.jprot.2015.05.038
Publication status	Published - Aug 3 2015

Keywords

Apolipoprotein E
Breast cancer
Extracted ion chromatogram
Label-free relative quantification
Plasma
Post-translational modification

ASJC Scopus subject areas

Biophysics
Biochemistry

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.jprot.2015.05.038

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Uen, Y. H., Liao, C. C., Lin, J. C., Pan, Y. H., Liu, Y. C., Chen, Y. C., Chen, W. J., Tai, C. C., Lee, K. W., Liu, Y. R., Lin, H. T., & Lin, C. Y. (2015). Analysis of differentially expressed novel post-translational modifications of plasma apolipoprotein E in Taiwanese females with breast cancer. Journal of Proteomics, 126, 252-262. https://doi.org/10.1016/j.jprot.2015.05.038

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

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.",

keywords = "Apolipoprotein E, Breast cancer, Extracted ion chromatogram, Label-free relative quantification, Plasma, Post-translational modification",

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}",

note = "Publisher Copyright: {\textcopyright} 2015 Elsevier B.V.",

year = "2015",

month = aug,

day = "3",

doi = "10.1016/j.jprot.2015.05.038",

language = "English",

volume = "126",

pages = "252--262",

journal = "Journal of Proteomics",

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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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DO - 10.1016/j.jprot.2015.05.038

M3 - Article

C2 - 26079612

AN - SCOPUS:84938568492

SN - 1874-3919

VL - 126

SP - 252

EP - 262

JO - Journal of Proteomics

JF - Journal of Proteomics

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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