Surface-enhanced laser desorption/ionization time-of-flight mass spectroscopy (SELDI-TOF-MS) as a tool for molecular endpoint analysis of PX-12, a thioredoxin-1 inhibitor
| dc.contributor.advisor | Powis, Garth | en_US |
| dc.contributor.author | Tate, Wendy Rose | |
| dc.creator | Tate, Wendy Rose | en_US |
| dc.date.accessioned | 2013-05-16T09:43:52Z | |
| dc.date.available | 2013-05-16T09:43:52Z | |
| dc.date.issued | 2005 | en_US |
| dc.identifier.uri | http://hdl.handle.net/10150/291852 | |
| dc.description.abstract | Thioredoxin-1 is a redox protein upregulated in many cancers. Its functions include inhibition of apoptosis, increasing cellular growth and proliferation. It has been shown that cells displaying increased levels of Trx-1 have increased drug resistance. PX-12 is a Trx-1 inhibitor that shows anti-proloferative and cytotoxic activity in vitro and in vivo. We used surface enhanced laser desorption/ionization time-of-flight mass spectroscopy (SELDI-TOF-MS) to measure plasma Trx-1 levels of patients treated with PX-12 as a side study of a phase-I trial. SELDI-TOF-MS was able to measure a decrease in plasma Trx-1 after PX-12 treatment semi-quantitatively. In addition, SELDI measured 57 other protein peaks in plasma; seven which were found in all plasma samples analyzed. One of these peaks was located at 13.86kDa and identified through LC-MS/MS sequencing to be a variant of Transthyretin. Further studies into these additional peaks are necessary to determine their biological importance in relation to Trx-1 and PX-12. | |
| dc.language.iso | en_US | en_US |
| dc.publisher | The University of Arizona. | en_US |
| dc.rights | Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author. | en_US |
| dc.subject | Molecular and Cellular Biology | en_US |
| dc.title | Surface-enhanced laser desorption/ionization time-of-flight mass spectroscopy (SELDI-TOF-MS) as a tool for molecular endpoint analysis of PX-12, a thioredoxin-1 inhibitor | en_US |
| dc.type | text | en_US |
| dc.type | Thesis-Reproduction (electronic) | en_US |
| thesis.degree.grantor | University of Arizona | en_US |
| thesis.degree.level | masters | en_US |
| dc.identifier.proquest | 1427224 | en_US |
| thesis.degree.discipline | Graduate College | en_US |
| thesis.degree.discipline | Molecular and Cellular Biology | en_US |
| thesis.degree.name | M.S. | en_US |
| dc.identifier.bibrecord | .b49001310 | en_US |
| refterms.dateFOA | 2018-06-15T20:13:45Z | |
| html.description.abstract | Thioredoxin-1 is a redox protein upregulated in many cancers. Its functions include inhibition of apoptosis, increasing cellular growth and proliferation. It has been shown that cells displaying increased levels of Trx-1 have increased drug resistance. PX-12 is a Trx-1 inhibitor that shows anti-proloferative and cytotoxic activity in vitro and in vivo. We used surface enhanced laser desorption/ionization time-of-flight mass spectroscopy (SELDI-TOF-MS) to measure plasma Trx-1 levels of patients treated with PX-12 as a side study of a phase-I trial. SELDI-TOF-MS was able to measure a decrease in plasma Trx-1 after PX-12 treatment semi-quantitatively. In addition, SELDI measured 57 other protein peaks in plasma; seven which were found in all plasma samples analyzed. One of these peaks was located at 13.86kDa and identified through LC-MS/MS sequencing to be a variant of Transthyretin. Further studies into these additional peaks are necessary to determine their biological importance in relation to Trx-1 and PX-12. |
