PMID- 22083816
OWN - NLM
STAT- MEDLINE
DCOM- 20120302
LR  - 20151119
IS  - 1940-6029 (Electronic)
IS  - 1064-3745 (Linking)
VI  - 818
DP  - 2012
TI  - Biomarker discovery in serum/plasma using surface enhanced laser desorption 
      ionization time of flight (SELDI-TOF) mass spectrometry.
PG  - 67-79
LID - 10.1007/978-1-61779-418-6_5 [doi]
AB  - Proteins and peptides that undergo variations in concentration or state as a 
      result of a biological process or disease may be used as biomarkers for the 
      diagnosis or prognosis of diseases and/or for the monitoring of therapy. 
      Serum/plasma is one of the most easily obtained patient specimens and contains 
      thousands of proteins produced and secreted from cells and tissues. While 
      serum/plasma is a valuable specimen for protein biomarker research, especially in 
      the area of infectious diseases, the dynamic range of the proteome presents a 
      technical challenge. Serum/plasma is dominated by high abundance proteins, such 
      as albumin, immunoglobulins, haptogloblulin, which constitute almost 90% of the 
      total serum/plasma protein by weight and make the detection of the low abundance 
      proteins difficult. Therefore, effective fractionation and separation methods are 
      essential to detect potential biomarker proteins present in small quantities for 
      mass spectrometry.The current tests for blood-borne protozoan diseases are 
      inadequate by monitoring treatment efficacy or for prognosis and also lack 
      sensitivity and specificity. To overcome these limitations, we began a program to 
      develop novel assays for infectious diseases using mass spectrometric data 
      directly as well as "next generation" assays that exploit the richness of the MS 
      data converted to standard platforms. Here we focus on high-throughput 
      fractionation and proteomic analysis using Surface Enhanced Laser Desorption 
      Ionization Time of Flight (SELDI-TOF) mass spectrometry platform. Separation and 
      enrichment is achieved using stepwise anion exchange fractionation prior to 
      analysis on multiple ProteinChip array chemistries. We have used this approach 
      successfully to identify proteins/peptides or protein "profiles" (biomarkers) in 
      subjects chronically infected with blood-borne protozoan parasites (i.e. Chagas 
      disease, babesia, toxoplasma, malaria), fascioliosis, and cysticercosis.
FAU - Ndao, Momar
AU  - Ndao M
AD  - National Reference Centre for Parasitology, Research Institute of the McGill 
      University Health Centre, Montreal General Hospital, Montreal, QC, Canada. 
      Momar.ndao@mcgill.ca
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Methods Mol Biol
JT  - Methods in molecular biology (Clifton, N.J.)
JID - 9214969
RN  - 0 (Biomarkers)
RN  - 0 (Blood Proteins)
SB  - IM
MH  - Adsorption
MH  - Analytic Sample Preparation Methods
MH  - Biomarkers/blood
MH  - Blood Proteins/*analysis/chemistry/isolation & purification
MH  - Chromatography, Affinity
MH  - Chromatography, Reverse-Phase
MH  - Humans
MH  - Ion Exchange
MH  - Protein Array Analysis
MH  - Robotics
MH  - Spectrometry, Mass, Matrix-Assisted Laser 
      Desorption-Ionization/instrumentation/*methods
EDAT- 2011/11/16 06:00
MHDA- 2012/03/03 06:00
CRDT- 2011/11/16 06:00
PHST- 2011/11/16 06:00 [entrez]
PHST- 2011/11/16 06:00 [pubmed]
PHST- 2012/03/03 06:00 [medline]
AID - 10.1007/978-1-61779-418-6_5 [doi]
PST - ppublish
SO  - Methods Mol Biol. 2012;818:67-79. doi: 10.1007/978-1-61779-418-6_5.