A novel phosphoprotein analysis scheme for assessing changes in premalignant and malignant breast cell lines using 2-D liquid separations, protein microarrays, and tandem mass spectrometry
dc.contributor.author | Patwa, Tasneem H. | en_US |
dc.contributor.author | Wang, Yanfei | en_US |
dc.contributor.author | Miller, Fred R. | en_US |
dc.contributor.author | Goodison, Steve | en_US |
dc.contributor.author | Pennathur, Subramaniam | en_US |
dc.contributor.author | Barder, Timothy J. | en_US |
dc.contributor.author | Lubman, David M. | en_US |
dc.date.accessioned | 2009-02-03T16:17:55Z | |
dc.date.available | 2010-03-01T21:10:28Z | en_US |
dc.date.issued | 2009-01 | en_US |
dc.identifier.citation | Patwa, Tasneem H.; Wang, Yanfei; Miller, Fred R.; Goodison, Steve; Pennathur, Subramaniam; Barder, Timothy J.; Lubman, David M. (2009). "A novel phosphoprotein analysis scheme for assessing changes in premalignant and malignant breast cell lines using 2-D liquid separations, protein microarrays, and tandem mass spectrometry." PROTEOMICS - Clinical Applications 3(1): 51-66. <http://hdl.handle.net/2027.42/61541> | en_US |
dc.identifier.issn | 1862-8346 | en_US |
dc.identifier.issn | 1862-8354 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/61541 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=19194518&dopt=citation | en_US |
dc.description.abstract | An analysis of phosphorylation changes that occur during cancer progression would provide insights into the molecular pathways responsible for a malignant phenotype. In this study we employed a novel coupling of 2-D liquid separations and protein microarray technology to reveal changes in phosphoprotein status between premalignant (AT1) and malignant (CA1a) cell lines derived from the human MCF10A breast cell lines. Intact proteins were first separated according to their p I and hydrophobicities, then arrayed on SuperAmine glass slides. Phosphoproteins were detected using the universal, inorganic phospho-sensor dye, Pro-Q Diamond. Using this dye, out of 140 spots that were positive for phosphorylation, a total of 85 differentially expressed spots were detected over a pH range of 7.2–4.0. Proteins were identified and their peptides sequenced by MS. The strategy enabled the identification of 75 differentially expressed phosphoproteins, from which 51 phosphorylation sites in 27 unique proteins were confirmed. Interestingly, the majority of differentially expressed phosphorylated proteins observed were nuclear proteins. Three regulators of apoptosis, Bad, Bax, and Acinus, were also differentially phosphorylated in the two cell lines. Further development of this strategy will facilitate an understanding of the mechanisms involved in malignancy progression and other disease-related phenotypes. | en_US |
dc.format.extent | 694377 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 Sciences | en_US |
dc.subject.other | Molecular Cell Biology | en_US |
dc.title | A novel phosphoprotein analysis scheme for assessing changes in premalignant and malignant breast cell lines using 2-D liquid separations, protein microarrays, and tandem mass spectrometry | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Medicine (General) | en_US |
dc.subject.hlbtoplevel | Health Sciences | 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 Internal Medicine, Division of Nephrology, University of Michigan Medical Center, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, MI, USA ; Department of Surgery, University of Michigan Medical Center, Ann Arbor, MI, USA ; Comprehensive Cancer Center, University of Michigan Medical Center, Ann Arbor, MI, USA ; Department of Surgery, The University of Michigan Medical Center, MSRB1, Rm A510B, 1150 West Medical Center Drive, Ann Arbor, MI 48109-0656, USA Fax: +1-734-615-2088 | en_US |
dc.contributor.affiliationother | Department of Pathology, Barbara Ann Karmanos Cancer Institute, Wayne State University School of Medicine, Detroit, MI, USA | en_US |
dc.contributor.affiliationother | Department of Surgery, University of Florida, Jacksonville, FL, USA | en_US |
dc.contributor.affiliationother | Eprogen Inc., Darien, IL, USA | en_US |
dc.identifier.pmid | 19194518 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/61541/1/51_ftp.pdf | |
dc.identifier.doi | http://dx.doi.org/10.1002/prca.200800097 | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.