Proteomic profiling identifies breast tumor metastasis-associated factors in an isogenic model
dc.contributor.author | Kreunin, Paweena | en_US |
dc.contributor.author | Yoo, Chul | en_US |
dc.contributor.author | Urquidi, Virginia | en_US |
dc.contributor.author | Lubman, David M. | en_US |
dc.contributor.author | Goodison, Steve | en_US |
dc.date.accessioned | 2007-09-20T18:05:27Z | |
dc.date.available | 2008-04-03T18:47:30Z | en_US |
dc.date.issued | 2007-01 | en_US |
dc.identifier.citation | Kreunin, 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.issn | 1615-9853 | en_US |
dc.identifier.issn | 1615-9861 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/55918 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=17205601&dopt=citation | en_US |
dc.description.abstract | A 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.extent | 420620 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | WILEY-VCH Verlag | en_US |
dc.subject.other | Life and Medical Sciences | en_US |
dc.title | Proteomic profiling identifies breast tumor metastasis-associated factors in an isogenic model | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department 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, USA | en_US |
dc.contributor.affiliationother | Department of Medicine, University of Florida, Jacksonville, FL, USA | en_US |
dc.contributor.affiliationother | Department 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: +1-904-244-4667 | en_US |
dc.identifier.pmid | 17205601 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/55918/1/299_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/pmic.200600272 | en_US |
dc.identifier.source | PROTEOMICS | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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