Targeted Measurements of O- and N-Glycopeptides Show That Proteins in High Density Lipoprotein Particles Are Enriched with Specific Glycosylation Compared to Plasma

Muchena J. Kailemia, Wanghui Wei, Khoa Nguyen, Elizabeth Beals, Lisa Sawrey-Kubicek, Christopher Rhodes, Chenghao Zhu, Romina Sacchi, Angela M. Zivkovic, Carlito B Lebrilla

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

High density lipoprotein (HDL) particles are believed to be protective due to their inverse correlation with the prevalence of cardiovascular diseases. However, recent studies show that in some conditions such as heart disease and diabetes, HDL particles can become dysfunctional. Great attention has been directed toward HDL particle composition because the relative abundances of HDL constituents determine HDL's functional properties. A key factor to consider when studying the structure and composition of plasma particles is the protein glycosylation. Here, we profile the O- and N-linked glycosylation of HDL associated-proteins including the truncated form of Apo CIII and their glycan heterogeneity in a site-specific manner. Apolipoprotein CIII, fetuin A, and alpha 1 antitrypsin are glycoproteins associated with lipoproteins and are implicated in many cardiovascular and other disease conditions. A targeted method (UHPLC-QQQ) was used to measure the glycoprotein concentrations and site-specific glycovariations of the proteins in human plasma and compared with HDL particles isolated from the same plasma samples. The proteins found in the plasma are differentially glycosylated compared to those isolated in HDL. The results of this study suggest that glycosylation may play a role in protein partitioning in the blood, with possible functional implications.

Original languageEnglish (US)
Pages (from-to)834-845
Number of pages12
JournalJournal of Proteome Research
Volume17
Issue number2
DOIs
StatePublished - Feb 2 2018

Fingerprint

Glycosylation
Glycopeptides
HDL Lipoproteins
Plasmas
Proteins
Glycoproteins
Cardiovascular Diseases
alpha-2-HS-Glycoprotein
Apolipoprotein C-III
Plasma (human)
alpha 1-Antitrypsin
Medical problems
Chemical analysis
Lipoproteins
Polysaccharides
Heart Diseases
Blood

Keywords

  • Apo CIII
  • fetuin A
  • glycopeptides
  • glycosylation
  • HDL
  • high density lipoprotein
  • MRM
  • tandem mass spectrometry
  • UPLC

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

Cite this

Targeted Measurements of O- and N-Glycopeptides Show That Proteins in High Density Lipoprotein Particles Are Enriched with Specific Glycosylation Compared to Plasma. / Kailemia, Muchena J.; Wei, Wanghui; Nguyen, Khoa; Beals, Elizabeth; Sawrey-Kubicek, Lisa; Rhodes, Christopher; Zhu, Chenghao; Sacchi, Romina; Zivkovic, Angela M.; Lebrilla, Carlito B.

In: Journal of Proteome Research, Vol. 17, No. 2, 02.02.2018, p. 834-845.

Research output: Contribution to journalArticle

Kailemia, MJ, Wei, W, Nguyen, K, Beals, E, Sawrey-Kubicek, L, Rhodes, C, Zhu, C, Sacchi, R, Zivkovic, AM & Lebrilla, CB 2018, 'Targeted Measurements of O- and N-Glycopeptides Show That Proteins in High Density Lipoprotein Particles Are Enriched with Specific Glycosylation Compared to Plasma', Journal of Proteome Research, vol. 17, no. 2, pp. 834-845. https://doi.org/10.1021/acs.jproteome.7b00604
Kailemia, Muchena J. ; Wei, Wanghui ; Nguyen, Khoa ; Beals, Elizabeth ; Sawrey-Kubicek, Lisa ; Rhodes, Christopher ; Zhu, Chenghao ; Sacchi, Romina ; Zivkovic, Angela M. ; Lebrilla, Carlito B. / Targeted Measurements of O- and N-Glycopeptides Show That Proteins in High Density Lipoprotein Particles Are Enriched with Specific Glycosylation Compared to Plasma. In: Journal of Proteome Research. 2018 ; Vol. 17, No. 2. pp. 834-845.
@article{0e8bc80e4ace451ba3d0974094baf2c2,
title = "Targeted Measurements of O- and N-Glycopeptides Show That Proteins in High Density Lipoprotein Particles Are Enriched with Specific Glycosylation Compared to Plasma",
abstract = "High density lipoprotein (HDL) particles are believed to be protective due to their inverse correlation with the prevalence of cardiovascular diseases. However, recent studies show that in some conditions such as heart disease and diabetes, HDL particles can become dysfunctional. Great attention has been directed toward HDL particle composition because the relative abundances of HDL constituents determine HDL's functional properties. A key factor to consider when studying the structure and composition of plasma particles is the protein glycosylation. Here, we profile the O- and N-linked glycosylation of HDL associated-proteins including the truncated form of Apo CIII and their glycan heterogeneity in a site-specific manner. Apolipoprotein CIII, fetuin A, and alpha 1 antitrypsin are glycoproteins associated with lipoproteins and are implicated in many cardiovascular and other disease conditions. A targeted method (UHPLC-QQQ) was used to measure the glycoprotein concentrations and site-specific glycovariations of the proteins in human plasma and compared with HDL particles isolated from the same plasma samples. The proteins found in the plasma are differentially glycosylated compared to those isolated in HDL. The results of this study suggest that glycosylation may play a role in protein partitioning in the blood, with possible functional implications.",
keywords = "Apo CIII, fetuin A, glycopeptides, glycosylation, HDL, high density lipoprotein, MRM, tandem mass spectrometry, UPLC",
author = "Kailemia, {Muchena J.} and Wanghui Wei and Khoa Nguyen and Elizabeth Beals and Lisa Sawrey-Kubicek and Christopher Rhodes and Chenghao Zhu and Romina Sacchi and Zivkovic, {Angela M.} and Lebrilla, {Carlito B}",
year = "2018",
month = "2",
day = "2",
doi = "10.1021/acs.jproteome.7b00604",
language = "English (US)",
volume = "17",
pages = "834--845",
journal = "Journal of Proteome Research",
issn = "1535-3893",
publisher = "American Chemical Society",
number = "2",

}

TY - JOUR

T1 - Targeted Measurements of O- and N-Glycopeptides Show That Proteins in High Density Lipoprotein Particles Are Enriched with Specific Glycosylation Compared to Plasma

AU - Kailemia, Muchena J.

AU - Wei, Wanghui

AU - Nguyen, Khoa

AU - Beals, Elizabeth

AU - Sawrey-Kubicek, Lisa

AU - Rhodes, Christopher

AU - Zhu, Chenghao

AU - Sacchi, Romina

AU - Zivkovic, Angela M.

AU - Lebrilla, Carlito B

PY - 2018/2/2

Y1 - 2018/2/2

N2 - High density lipoprotein (HDL) particles are believed to be protective due to their inverse correlation with the prevalence of cardiovascular diseases. However, recent studies show that in some conditions such as heart disease and diabetes, HDL particles can become dysfunctional. Great attention has been directed toward HDL particle composition because the relative abundances of HDL constituents determine HDL's functional properties. A key factor to consider when studying the structure and composition of plasma particles is the protein glycosylation. Here, we profile the O- and N-linked glycosylation of HDL associated-proteins including the truncated form of Apo CIII and their glycan heterogeneity in a site-specific manner. Apolipoprotein CIII, fetuin A, and alpha 1 antitrypsin are glycoproteins associated with lipoproteins and are implicated in many cardiovascular and other disease conditions. A targeted method (UHPLC-QQQ) was used to measure the glycoprotein concentrations and site-specific glycovariations of the proteins in human plasma and compared with HDL particles isolated from the same plasma samples. The proteins found in the plasma are differentially glycosylated compared to those isolated in HDL. The results of this study suggest that glycosylation may play a role in protein partitioning in the blood, with possible functional implications.

AB - High density lipoprotein (HDL) particles are believed to be protective due to their inverse correlation with the prevalence of cardiovascular diseases. However, recent studies show that in some conditions such as heart disease and diabetes, HDL particles can become dysfunctional. Great attention has been directed toward HDL particle composition because the relative abundances of HDL constituents determine HDL's functional properties. A key factor to consider when studying the structure and composition of plasma particles is the protein glycosylation. Here, we profile the O- and N-linked glycosylation of HDL associated-proteins including the truncated form of Apo CIII and their glycan heterogeneity in a site-specific manner. Apolipoprotein CIII, fetuin A, and alpha 1 antitrypsin are glycoproteins associated with lipoproteins and are implicated in many cardiovascular and other disease conditions. A targeted method (UHPLC-QQQ) was used to measure the glycoprotein concentrations and site-specific glycovariations of the proteins in human plasma and compared with HDL particles isolated from the same plasma samples. The proteins found in the plasma are differentially glycosylated compared to those isolated in HDL. The results of this study suggest that glycosylation may play a role in protein partitioning in the blood, with possible functional implications.

KW - Apo CIII

KW - fetuin A

KW - glycopeptides

KW - glycosylation

KW - HDL

KW - high density lipoprotein

KW - MRM

KW - tandem mass spectrometry

KW - UPLC

UR - http://www.scopus.com/inward/record.url?scp=85041459201&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85041459201&partnerID=8YFLogxK

U2 - 10.1021/acs.jproteome.7b00604

DO - 10.1021/acs.jproteome.7b00604

M3 - Article

C2 - 29212317

AN - SCOPUS:85041459201

VL - 17

SP - 834

EP - 845

JO - Journal of Proteome Research

JF - Journal of Proteome Research

SN - 1535-3893

IS - 2

ER -