Differential capture of serum proteins for expression profiling and biomarker discovery in pre- and posttreatment head and neck cancer samples.
Introduction: A long-term goal of our group is to develop proteomic-based approaches to the detection and use of protein biomarkers for improvement in diagnosis, prognosis, and tailoring of treatment for head and neck squamous cell cancer (HNSCC). We have previously demonstrated that protein express...
| Publicado en: | Laryngoscope Vol. 118; no. 1; pp. 61 - 69 |
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| Autores principales: | , , , , , , , , , , , , , , , , , , , |
| Formato: | research tables/charts tracings Journal Article |
| Publicado: |
Wiley-Blackwell
2008
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=105870674&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 105870674 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 0023852X 1GR jtl: Laryngoscope issn: 0023852X maglogo: Y pubinfo: dt: 2008 vid: 118 iid: 1 pid: 480 pub: Wiley-Blackwell place: Malden, Massachusetts artinfo: ui: 105870674 105870674 NLM18043497 2009826573 NLM18043497 105870674 ppf: 61 ppct: 8 formats: tig: atl: Differential capture of serum proteins for expression profiling and biomarker discovery in pre- and posttreatment head and neck cancer samples. aug: au: Freed GL Cazares LH Fichandler CE Fuller TW Sawyer CA Stack BC Jr. Schraff S Semmes OJ Wadsworth JT Drake RR Freed, Gary L Cazares, Lisa H Fichandler, Craig E Fuller, Thomas W Sawyer, Christopher A Stack, Brendan C Jr Schraff, Scott Semmes, O John Wadsworth, J Trad Drake, Richard R affil: Department of Microbiology and Molecular Cell Biology, Center for Biomedical Proteomics, Eastern Virginia Medical School, 700 W. Olney Road, Norfolk, VA 23507, U.S.A sug: subj: Blood Proteins Analysis Carcinoma, Squamous Cell Therapy Genetic Techniques Methods Head and Neck Neoplasms Therapy Tumor Markers, Biological Blood Affinity Labels Diagnostic Use Aged Aged, 80 and Over Algorithms Biological Markers Blood Carcinoma, Squamous Cell Blood Case Control Studies Descriptive Statistics Female Funding Source Head and Neck Neoplasms Blood Information Science Male Middle Age Molecular Probe Techniques Neoplasm Staging Prognosis Prospective Studies Sample Size Smoking Blood Software Mass Spectrometry Human Aged: 65+ years Aged, 80 & over Middle Aged: 45-64 years Female Male ab: Introduction: A long-term goal of our group is to develop proteomic-based approaches to the detection and use of protein biomarkers for improvement in diagnosis, prognosis, and tailoring of treatment for head and neck squamous cell cancer (HNSCC). We have previously demonstrated that protein expression profiling of serum can identify multiple protein biomarker events that can serve as molecular fingerprints for the assessment of HNSCC disease state and prognosis.Methods: An automated Bruker Daltonics (Billerica, MA) ClinProt matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometer was used. Magnetic chemical affinity beads were used to differentially capture serum proteins prior to MALDI-TOF analysis. The resulting spectra were analyzed using postprocessing software and a pattern recognition genetic algorithm (ClinProt 2.0). An HNSCC cohort of 48 sera samples from 24 patients consisting of matched pretreatment and 6 to 12 month posttreatment samples was used for further analysis. Low-mass differentially expressed peptides were identified using MALDI-TOF/TOF.Results: In the working mass range of 1,000 to 10,000 m/z, approximately 200 peaks were resolved for ionic bead capture approaches. For spectra generated from weak cation bead capture, a k-nearest neighbor genetic algorithm was able to correctly classify 94% normal from pretreatment HNSCC samples, 80% of pretreatment from posttreatment samples, and 87% of normal from posttreatment samples. These peptides were then analyzed by MALDI-TOF/TOF mass spectometry for sequence identification directly from serum processed with the same magnetic bead chemistry or alternatively after gel electrophoresis separation of the captured proteins. We were able to compare this with similar studies using surface-enhanced laser desorption ionization (SELDI)-TOF to show this method as a valid tool for this process with some improvement in the identification of our groups.Conclusions: This initial study using new high-resolution MALDI-TOF mass spectrometry coupled with bead fractionation is suitable for automated protein profiling and has the capability to simultaneously identify potential biomarker proteins for HNSCC. In addition, we were able to show improvement with the MALDI-TOF in identifying groups with HNSCC when compared with our prior data using SELDI-TOF. Using this MALDI-TOF technology as a discovery platform, we anticipate generating biomarker panels for use in more accurate prediction of prognosis and treatment efficacies for HNSCC. pubtype: Academic Journal doctype: research tables/charts tracings Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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