Proteomic Approaches within the NCI Early Detection Research Network for the Discovery and Identification of Cancer Biomarkers
dc.contributor.author | Verma, Mukesh | en_US |
dc.contributor.author | Wright, George L. | en_US |
dc.contributor.author | Hanash, Samir M. | en_US |
dc.contributor.author | Gopal-Srivastava, Rashmi | en_US |
dc.contributor.author | Srivastava, Sudhir | en_US |
dc.date.accessioned | 2010-06-01T20:13:56Z | |
dc.date.available | 2010-06-01T20:13:56Z | |
dc.date.issued | 2001-09 | en_US |
dc.identifier.citation | VERMA, MUKESH; WRIGHT, GEORGE L.; HANASH, SAMIR M.; GOPAL-SRIVASTAVA, RASHMI; SRIVASTAVA, SUDHIR (2001). "Proteomic Approaches within the NCI Early Detection Research Network for the Discovery and Identification of Cancer Biomarkers." Annals of the New York Academy of Sciences 945(1 CIRCULATING NUCLEIC ACIDS IN PLASMA OR SERUM II ): 103-115. <http://hdl.handle.net/2027.42/73353> | en_US |
dc.identifier.issn | 0077-8923 | en_US |
dc.identifier.issn | 1749-6632 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/73353 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=11708463&dopt=citation | en_US |
dc.description.abstract | In the postgenome era, proteomics provides a powerful approach for the analysis of normal and transformed cell functions, for the identification of disease-specific targets, and for uncovering novel endpoints for the evaluation of chemoprevention agents and drug toxicity. Unfortunately, the genomic information that has greatly expounded the genetic basis of cancer does not allow an accurate prediction of what is actually occurring at the protein level within a given cell type at any given time. The gene expression program of a given cell is affected by numerous factors in the in vivo environment resulting from tissue complexity and organ system orchestration, with cells acting in concert with each other and responding to changes in their microenvironment. Repositories of genomic information can be considered master “inventory lists” of genes and their maps, which need to be supplemented with protein-derived information. The National Cancer Institute's Early Detection Research Network is employing proteomics, or “protein walking”, in the discovery and evaluation of biomarkers for cancer detection and for the identification of high-risk subjects. Armed with microdissection techniques, including the use of Laser Capture Microdissection (LCM) to procure pure populations of cells directly from human tissue, the Network is facilitating the development of technologies that can overcome the problem of tissue heterogeneity and address the need to identify markers in easily accessible biological fluids. Proteomic approaches complement plasma-based assays of circulating DNA for cancer detection and risk assessment. LCM, coupled with downstream proteomics applications, such as two-dimensional polyacrylamide gel electrophoresis and SELDI (surface enhanced laser desorption ionization) separation followed by mass spectrometry (MS) analysis, may greatly facilitate the characterization and identification of protein expression changes that track normal and disease phenotypes. We highlight recent work from Network investigators to demonstrate the potential of proteomics to identify proteins present in cancer tissues and body fluids that are relevant for cancer screening. | en_US |
dc.format.extent | 3354572 bytes | |
dc.format.extent | 3109 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Blackwell Publishing Ltd | en_US |
dc.rights | 2001 by the New York Academy of Sciences | en_US |
dc.subject.other | Biomarkers | en_US |
dc.subject.other | EDRN | en_US |
dc.subject.other | LCM | en_US |
dc.subject.other | MALDI | en_US |
dc.subject.other | ProteinChip | en_US |
dc.subject.other | Proteomics | en_US |
dc.subject.other | SELDI | en_US |
dc.title | Proteomic Approaches within the NCI Early Detection Research Network for the Discovery and Identification of Cancer Biomarkers | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Science (General) | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Pediatrics, University of Michigan, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationother | Cancer Biomarkers Research Group, Division of Cancer Prevention, National Cancer Institute, Bethesda, Maryland, USA | en_US |
dc.contributor.affiliationother | Department of Microbiology and Molecular Cell Biology and Virginia Prostate Center, Eastern Virginia Medical School, Norfolk, Virginia, USA | en_US |
dc.contributor.affiliationother | Division of Extramural Activities, National Cancer Institute, Bethesda, Maryland, USA | en_US |
dc.identifier.pmid | 11708463 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/73353/1/j.1749-6632.2001.tb03870.x.pdf | |
dc.identifier.doi | 10.1111/j.1749-6632.2001.tb03870.x | en_US |
dc.identifier.source | Annals of the New York Academy of Sciences | en_US |
dc.identifier.citedreference | Collins, F.S. & V.A. McKusick, 2001. Implications of the human genome project for medical science. JAMA 285: 540 – 544. | en_US |
dc.identifier.citedreference | Venter, J.C., M.D. Adams, E.W. Myers et al. 2001. The sequence of the human genome. Science 291: 1304 – 1351. | en_US |
dc.identifier.citedreference | Wasinger, V.C., S.J. Cordwell, A. Cerpa-Poljak et al. 1995. Progress with gene-product mapping of the Mollicutes: Mycoplasma genitalium. Electrophoresis 16: 1090 – 1094. | en_US |
dc.identifier.citedreference | Jungblut, P.R., U. Zimny-Arndt, E. Zeindl-Eberhart et al. 1999. Proteomics in human disease: cancer, heart, and infectious diseases. Electrophoresis 20: 2100 – 2110. | en_US |
dc.identifier.citedreference | Herbert, B. 1999. Advances in protein solubilization for two-dimensional electrophoresis. Electrophoresis 20: 660 – 663. | en_US |
dc.identifier.citedreference | Godovac-Zimmermann, J., V. Soskic, S. Poznanovic et al. 1999. Functional proteomics of signal transduction by membrane receptors. Electrophoresis 20: 952 – 961. | en_US |
dc.identifier.citedreference | Hatzimanikatis, V., L.H. Choe & K.H. Lee. 1999. Proteomics: theoretical and experimental considerations. Biotechnol. Prog. 5: 312 – 318. | en_US |
dc.identifier.citedreference | Fabris, D., M. Vestling, M. Cordero et al. 1995. Sequencing electroblotted proteins by tandem mass spectrometry. Rapid Commun. Mass Spectrom. 9: 1051 – 1055. | en_US |
dc.identifier.citedreference | Yates, J.R., J.K. Eng & A.L. McCormack. 1995. Mining genomes: correlating tandem mass spectra of modified and unmodified peptides to sequences in nucleotide databases. Anal. Chem. 67: 3202 – 3210. | en_US |
dc.identifier.citedreference | Feras, E.R., D.J. Stephens, C.E. Walters et al. 1999. The role of cholesterol in the biosynthesis of beta-amyloid. Neuroreport 10: 1699 – 1705. | en_US |
dc.identifier.citedreference | Humphery-Smith, I., S.J. Cordwell & W.P. Blackstock. 1997. Proteome research: complementarity and limitations with respect to the RNA and DNA worlds. Electrophoresis 18: 1217 – 1242. | en_US |
dc.identifier.citedreference | Dove, A. 1999. Proteomics: translating genomics into products ? Nat. Biotechnol. 17: 233 – 236. | en_US |
dc.identifier.citedreference | Aicher, L., D. Wahl, A. Arce et al. 1998. New insights into cyclosporine A nephrotoxicity by proteome analysis. Electrophoresis 19: 1998 – 2003. | en_US |
dc.identifier.citedreference | Hutchens, T.W. & T.T. Yip, 1993. New desorption strategies for the mass analysis of macromolecules. Rapid Commun. Mass Spectrom. 7: 576 – 580. | en_US |
dc.identifier.citedreference | Merchant, M. & S.R. Weinberger, 2000. Recent advancements in surface-enhanced laser desorption/ionization-time of flight mass spectrometry. Electrophoresis 21: 1164 – 1177. | en_US |
dc.identifier.citedreference | Fung, E.T., G.L. Wright, Jr. & E.A. Dalmasso. 2000. Proteomic strategies for biomarker identification: progress and challenges. Curr. Opin. Mol. Ther. 2: 643 – 650. | en_US |
dc.identifier.citedreference | Yip, T.T., J. Van de Water, M.E. Gerswin et al. 1996. Cryptic antigenic determinants on the extracellular pyruvate dehydrogenase complex/mimeotope found in primary biliary cirrhosis. J. Biol. Chem. 271: 32825 – 32833. | en_US |
dc.identifier.citedreference | Banks, R.E., M.J. Dunn, M.A. Forbes et al. 1999. The potential use of laser capture microdissection to selectively obtain distinct populations of cells for proteomic analysis-preliminary findings. Electrophoresis 20: 689 – 700. | en_US |
dc.identifier.citedreference | Wright, G.L., Jr., L.H. Cazares, S.M. Leung et al. 1999. ProteinChip surface enhanced laser desorption/ionization (SELDI) mass spectrometry: a novel protein biochip technology for detection of prostate cancer biomarkers in complex protein mixtures. Prostate Cancer Prostatic Dis. 2: 264 – 276. | en_US |
dc.identifier.citedreference | Ornstein, D.K., C. Englert, J.W. Gillespie et al. 2000. Characterization of intracellular prostate-specific antigen from laser capture microdissected benign and malignant prostatic epithelium. Clin. Cancer Res. 6: 353 – 356. | en_US |
dc.identifier.citedreference | Paweletz, C.P., J.W. Gillespie, D.K. Ornstein et al. 2000. Rapid protein display profiling of cancer progression directly from human tissue using a protein biochip. Drug Dev. Res. 49: 34 – 42. | en_US |
dc.identifier.citedreference | 22 Vlahou, A., P.F. Schellhammer, S. Mendrinos et al. 2001. Development of a novel proteomic approach for the detection of transitional cell carcinoma of the bladder in urine. Am. J. Pathol. In press. | en_US |
dc.identifier.citedreference | Xiao, Z., X. Jiang, M.L. Beckett et al. 2000. Generation of a baculovirus recombinant prostate-specific membrane antigen and its use in the development of a novel protein biochip quantitative immunoassay. Protein Expression Purif. 19: 12 – 21. | en_US |
dc.identifier.citedreference | Liszeski, K. 1999. New twists in gene therapy. Genet. Eng. News 19: 8 – 34. | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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