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dc.contributor.authorKreunin, Paweenaen_US
dc.contributor.authorYoo, Chulen_US
dc.contributor.authorUrquidi, Virginiaen_US
dc.contributor.authorLubman, David M.en_US
dc.contributor.authorGoodison, Steveen_US
dc.date.accessioned2007-09-20T18:05:27Z
dc.date.available2008-04-03T18:47:30Zen_US
dc.date.issued2007-01en_US
dc.identifier.citationKreunin, Paweena; Yoo, Chul; Urquidi, Virginia; Lubman, David M.; Goodison, Steve (2007). "Proteomic profiling identifies breast tumor metastasis-associated factors in an isogenic model." PROTEOMICS 7(2): 299-312. <http://hdl.handle.net/2027.42/55918>en_US
dc.identifier.issn1615-9853en_US
dc.identifier.issn1615-9861en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/55918
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=17205601&dopt=citationen_US
dc.description.abstractA combination of LC and MS was applied to an isogenic breast tumor metastasis model to identify proteins associated with a cellular phenotype. Chromatofocusing followed by nonporous-RP-HPLC/ESI-TOF MS was applied to cell lysates of a pair of monoclonal cell lines from the human breast carcinoma cell line MDA-MB-435 that have different metastatic phenotypes in immune-compromised mice. This method was developed to separate proteins based on p I and hydrophobicity. The high resolution and mass accuracy of ESI-TOF measurements provided a good correlation of theoretical MW and experimental M r values of intact proteins measured in mass maps obtained in the pH range 3.8–6.4. The isolated proteins were digested by trypsin and analyzed by MALDI-TOF MS, MALDI-QIT-TOF MS, and monolith-based HPLC/MS/MS. The unique combination of the techniques provided valuable information including quantitation and modification of proteins. We identified 89 selected proteins, of which 43 were confirmed as differentially expressed. Metastasis-associated proteins included galectin-1, whereas annexin I and annexin II were associated with the nonmetastatic phenotype. In this study, we demonstrate that combining a variety of MS tools with a multidimensional liquid-phase separation provides the ability to map cellular protein content, to search for modified proteins, and to correlate protein expression with cellular phenotype.en_US
dc.format.extent420620 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherWILEY-VCH Verlagen_US
dc.subject.otherLife and Medical Sciencesen_US
dc.titleProteomic profiling identifies breast tumor metastasis-associated factors in an isogenic modelen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MI, USA ; Comprehensive Cancer Center, University of Michigan Medical Center, Ann Arbor, MI, USA ; Department of Surgery, University of Michigan Medical Center, Ann Arbor, MI, USAen_US
dc.contributor.affiliationotherDepartment of Medicine, University of Florida, Jacksonville, FL, USAen_US
dc.contributor.affiliationotherDepartment of Surgery, University of Florida, Jacksonville, FL, USA ; University of Florida, Department of Surgery, Shands Health Science Center, 653 West 8th Street, Jacksonville, FL 32209, USA Fax: +1-904-244-4667en_US
dc.identifier.pmid17205601en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/55918/1/299_ftp.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1002/pmic.200600272en_US
dc.identifier.sourcePROTEOMICSen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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