Profiling of rat plasma by surface-enhanced laser desorption/ionization time-of-flight mass spectrometry, a novel tool for biomarker discovery in nutrition research

Thomas Linke, A. Catharine Ross, Earl H. Harrison

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

The recent development of high-throughput proteomic technologies has given us new methods to analyze how an organism responds to changes in its nutritional environment. The analysis of plasma samples by surface-enhanced laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF-MS) was investigated as a novel approach to the identification of new biomarkers of nutrient status. Pre-fractionation of rat plasma by anion-exchange chromatography in 96-well filter plates markedly increased the total number of unique peptides and proteins that could be observed in SELDI-TOF mass spectra. Replicate fractionations generated nearly identical pH fractions, not only in terms of peptide and protein composition but also in respect to the ion signal intensity of replicate SELDI-TOF mass spectra. The feasibility of this approach was tested with samples from retinol-sufficient and retinol-deficient rats. The comparative analysis revealed reduced levels of three proteins with molecular masses between 10 000 and 20 000 in plasma of retinol-deficient rats. These results demonstrate that plasma profiling by anion-exchange fractionation and SELDI-TOF-MS may be a promising surveillance tool to detect changes in nutritional status and whole body physiology.

Original languageEnglish (US)
Pages (from-to)65-71
Number of pages7
JournalJournal of Chromatography A
Volume1043
Issue number1
DOIs
StatePublished - Jul 16 2004

Fingerprint

Biomarkers
Nutrition
Vitamin A
Ionization
Mass spectrometry
Rats
Desorption
Mass Spectrometry
Lasers
Fractionation
Plasmas
Anions
Research
Ion exchange
Peptides
Proteins
Plasma Exchange
Nutritional Status
Proteomics
Chromatography

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry

Cite this

@article{81ab65514a68480998f6f3a84406b0b1,
title = "Profiling of rat plasma by surface-enhanced laser desorption/ionization time-of-flight mass spectrometry, a novel tool for biomarker discovery in nutrition research",
abstract = "The recent development of high-throughput proteomic technologies has given us new methods to analyze how an organism responds to changes in its nutritional environment. The analysis of plasma samples by surface-enhanced laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF-MS) was investigated as a novel approach to the identification of new biomarkers of nutrient status. Pre-fractionation of rat plasma by anion-exchange chromatography in 96-well filter plates markedly increased the total number of unique peptides and proteins that could be observed in SELDI-TOF mass spectra. Replicate fractionations generated nearly identical pH fractions, not only in terms of peptide and protein composition but also in respect to the ion signal intensity of replicate SELDI-TOF mass spectra. The feasibility of this approach was tested with samples from retinol-sufficient and retinol-deficient rats. The comparative analysis revealed reduced levels of three proteins with molecular masses between 10 000 and 20 000 in plasma of retinol-deficient rats. These results demonstrate that plasma profiling by anion-exchange fractionation and SELDI-TOF-MS may be a promising surveillance tool to detect changes in nutritional status and whole body physiology.",
author = "Thomas Linke and Ross, {A. Catharine} and Harrison, {Earl H.}",
year = "2004",
month = "7",
day = "16",
doi = "10.1016/j.chroma.2004.05.007",
language = "English (US)",
volume = "1043",
pages = "65--71",
journal = "Journal of Chromatography A",
issn = "0021-9673",
number = "1",

}

TY - JOUR

T1 - Profiling of rat plasma by surface-enhanced laser desorption/ionization time-of-flight mass spectrometry, a novel tool for biomarker discovery in nutrition research

AU - Linke, Thomas

AU - Ross, A. Catharine

AU - Harrison, Earl H.

PY - 2004/7/16

Y1 - 2004/7/16

N2 - The recent development of high-throughput proteomic technologies has given us new methods to analyze how an organism responds to changes in its nutritional environment. The analysis of plasma samples by surface-enhanced laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF-MS) was investigated as a novel approach to the identification of new biomarkers of nutrient status. Pre-fractionation of rat plasma by anion-exchange chromatography in 96-well filter plates markedly increased the total number of unique peptides and proteins that could be observed in SELDI-TOF mass spectra. Replicate fractionations generated nearly identical pH fractions, not only in terms of peptide and protein composition but also in respect to the ion signal intensity of replicate SELDI-TOF mass spectra. The feasibility of this approach was tested with samples from retinol-sufficient and retinol-deficient rats. The comparative analysis revealed reduced levels of three proteins with molecular masses between 10 000 and 20 000 in plasma of retinol-deficient rats. These results demonstrate that plasma profiling by anion-exchange fractionation and SELDI-TOF-MS may be a promising surveillance tool to detect changes in nutritional status and whole body physiology.

AB - The recent development of high-throughput proteomic technologies has given us new methods to analyze how an organism responds to changes in its nutritional environment. The analysis of plasma samples by surface-enhanced laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF-MS) was investigated as a novel approach to the identification of new biomarkers of nutrient status. Pre-fractionation of rat plasma by anion-exchange chromatography in 96-well filter plates markedly increased the total number of unique peptides and proteins that could be observed in SELDI-TOF mass spectra. Replicate fractionations generated nearly identical pH fractions, not only in terms of peptide and protein composition but also in respect to the ion signal intensity of replicate SELDI-TOF mass spectra. The feasibility of this approach was tested with samples from retinol-sufficient and retinol-deficient rats. The comparative analysis revealed reduced levels of three proteins with molecular masses between 10 000 and 20 000 in plasma of retinol-deficient rats. These results demonstrate that plasma profiling by anion-exchange fractionation and SELDI-TOF-MS may be a promising surveillance tool to detect changes in nutritional status and whole body physiology.

UR - http://www.scopus.com/inward/record.url?scp=3242708773&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=3242708773&partnerID=8YFLogxK

U2 - 10.1016/j.chroma.2004.05.007

DO - 10.1016/j.chroma.2004.05.007

M3 - Article

C2 - 15317414

AN - SCOPUS:3242708773

VL - 1043

SP - 65

EP - 71

JO - Journal of Chromatography A

JF - Journal of Chromatography A

SN - 0021-9673

IS - 1

ER -