Identification of glycoproteins in human cerebrospinal fluid with a complementary proteomic approach

Sheng Pan, Yan Wang, Joseph Quinn, Elaine R. Peskind, Dana Waichunas, Jake T. Wimberger, Jinghua Jin, Jane G. Li, David Zhu, Catherine Pan, Jing Zhang

Research output: Contribution to journalArticle

77 Citations (Scopus)

Abstract

Biomarkers are pressingly needed to assist with the clinical diagnosis of neurodegenerative diseases and/or the monitoring of disease progression. Glycoproteins are enriched in bodily fluids such as human cerebrospinal fluid (CSF), an ideal source for discovering biomarkers due to its proximity to the central nervous system (CNS), and consequently can serve as diagnostic and/or therapeutic markers for CNS diseases. We report here an in-depth identification of glycoproteins in human CSF using a complementary proteomic approach which integrated hydrazide chemistry and lectin affinity column for glycoprotein enrichment, followed by multidimensional chromatography separation and tandem mass spectrometric analysis. Using stringent criteria, a total of 216 glycoproteins, including many low-abundance proteins, was identified with high confidence. Approximately one-third of these proteins was already known to be relevant to the CNS structurally or functionally. This investigation, for the first time, not only categorized many glycoproteins in human CSF but also expanded the existing overall CSF protein database.

Original languageEnglish (US)
Pages (from-to)2769-2779
Number of pages11
JournalJournal of Proteome Research
Volume5
Issue number10
DOIs
StatePublished - Oct 2006

Fingerprint

Cerebrospinal fluid
Proteomics
Cerebrospinal Fluid
Glycoproteins
Neurology
Biomarkers
Central Nervous System
Neurodegenerative diseases
Cerebrospinal Fluid Proteins
Protein Databases
Central Nervous System Diseases
Chromatography
Lectins
Neurodegenerative Diseases
Disease Progression
Proteins
Fluids
Monitoring

Keywords

  • Cerebrospinal fluid
  • Glycoprotein
  • Hydrazide chemistry
  • Lectin affinity column
  • Mass spectrometry
  • Proteomics

ASJC Scopus subject areas

  • Genetics
  • Biotechnology
  • Biochemistry

Cite this

Identification of glycoproteins in human cerebrospinal fluid with a complementary proteomic approach. / Pan, Sheng; Wang, Yan; Quinn, Joseph; Peskind, Elaine R.; Waichunas, Dana; Wimberger, Jake T.; Jin, Jinghua; Li, Jane G.; Zhu, David; Pan, Catherine; Zhang, Jing.

In: Journal of Proteome Research, Vol. 5, No. 10, 10.2006, p. 2769-2779.

Research output: Contribution to journalArticle

Pan, S, Wang, Y, Quinn, J, Peskind, ER, Waichunas, D, Wimberger, JT, Jin, J, Li, JG, Zhu, D, Pan, C & Zhang, J 2006, 'Identification of glycoproteins in human cerebrospinal fluid with a complementary proteomic approach', Journal of Proteome Research, vol. 5, no. 10, pp. 2769-2779. https://doi.org/10.1021/pr060251s
Pan, Sheng ; Wang, Yan ; Quinn, Joseph ; Peskind, Elaine R. ; Waichunas, Dana ; Wimberger, Jake T. ; Jin, Jinghua ; Li, Jane G. ; Zhu, David ; Pan, Catherine ; Zhang, Jing. / Identification of glycoproteins in human cerebrospinal fluid with a complementary proteomic approach. In: Journal of Proteome Research. 2006 ; Vol. 5, No. 10. pp. 2769-2779.
@article{aedaf1e704d54f58a635794dc207b62b,
title = "Identification of glycoproteins in human cerebrospinal fluid with a complementary proteomic approach",
abstract = "Biomarkers are pressingly needed to assist with the clinical diagnosis of neurodegenerative diseases and/or the monitoring of disease progression. Glycoproteins are enriched in bodily fluids such as human cerebrospinal fluid (CSF), an ideal source for discovering biomarkers due to its proximity to the central nervous system (CNS), and consequently can serve as diagnostic and/or therapeutic markers for CNS diseases. We report here an in-depth identification of glycoproteins in human CSF using a complementary proteomic approach which integrated hydrazide chemistry and lectin affinity column for glycoprotein enrichment, followed by multidimensional chromatography separation and tandem mass spectrometric analysis. Using stringent criteria, a total of 216 glycoproteins, including many low-abundance proteins, was identified with high confidence. Approximately one-third of these proteins was already known to be relevant to the CNS structurally or functionally. This investigation, for the first time, not only categorized many glycoproteins in human CSF but also expanded the existing overall CSF protein database.",
keywords = "Cerebrospinal fluid, Glycoprotein, Hydrazide chemistry, Lectin affinity column, Mass spectrometry, Proteomics",
author = "Sheng Pan and Yan Wang and Joseph Quinn and Peskind, {Elaine R.} and Dana Waichunas and Wimberger, {Jake T.} and Jinghua Jin and Li, {Jane G.} and David Zhu and Catherine Pan and Jing Zhang",
year = "2006",
month = "10",
doi = "10.1021/pr060251s",
language = "English (US)",
volume = "5",
pages = "2769--2779",
journal = "Journal of Proteome Research",
issn = "1535-3893",
publisher = "American Chemical Society",
number = "10",

}

TY - JOUR

T1 - Identification of glycoproteins in human cerebrospinal fluid with a complementary proteomic approach

AU - Pan, Sheng

AU - Wang, Yan

AU - Quinn, Joseph

AU - Peskind, Elaine R.

AU - Waichunas, Dana

AU - Wimberger, Jake T.

AU - Jin, Jinghua

AU - Li, Jane G.

AU - Zhu, David

AU - Pan, Catherine

AU - Zhang, Jing

PY - 2006/10

Y1 - 2006/10

N2 - Biomarkers are pressingly needed to assist with the clinical diagnosis of neurodegenerative diseases and/or the monitoring of disease progression. Glycoproteins are enriched in bodily fluids such as human cerebrospinal fluid (CSF), an ideal source for discovering biomarkers due to its proximity to the central nervous system (CNS), and consequently can serve as diagnostic and/or therapeutic markers for CNS diseases. We report here an in-depth identification of glycoproteins in human CSF using a complementary proteomic approach which integrated hydrazide chemistry and lectin affinity column for glycoprotein enrichment, followed by multidimensional chromatography separation and tandem mass spectrometric analysis. Using stringent criteria, a total of 216 glycoproteins, including many low-abundance proteins, was identified with high confidence. Approximately one-third of these proteins was already known to be relevant to the CNS structurally or functionally. This investigation, for the first time, not only categorized many glycoproteins in human CSF but also expanded the existing overall CSF protein database.

AB - Biomarkers are pressingly needed to assist with the clinical diagnosis of neurodegenerative diseases and/or the monitoring of disease progression. Glycoproteins are enriched in bodily fluids such as human cerebrospinal fluid (CSF), an ideal source for discovering biomarkers due to its proximity to the central nervous system (CNS), and consequently can serve as diagnostic and/or therapeutic markers for CNS diseases. We report here an in-depth identification of glycoproteins in human CSF using a complementary proteomic approach which integrated hydrazide chemistry and lectin affinity column for glycoprotein enrichment, followed by multidimensional chromatography separation and tandem mass spectrometric analysis. Using stringent criteria, a total of 216 glycoproteins, including many low-abundance proteins, was identified with high confidence. Approximately one-third of these proteins was already known to be relevant to the CNS structurally or functionally. This investigation, for the first time, not only categorized many glycoproteins in human CSF but also expanded the existing overall CSF protein database.

KW - Cerebrospinal fluid

KW - Glycoprotein

KW - Hydrazide chemistry

KW - Lectin affinity column

KW - Mass spectrometry

KW - Proteomics

UR - http://www.scopus.com/inward/record.url?scp=33750130282&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33750130282&partnerID=8YFLogxK

U2 - 10.1021/pr060251s

DO - 10.1021/pr060251s

M3 - Article

C2 - 17022648

AN - SCOPUS:33750130282

VL - 5

SP - 2769

EP - 2779

JO - Journal of Proteome Research

JF - Journal of Proteome Research

SN - 1535-3893

IS - 10

ER -