Rapid discovery and identification of a tissue-specific tumor biomarker from 39 human cancer cell lines using the SELDI ProteinChip platform
Useful biomarkers are needed for early detection of cancers. To demonstrate the potential diagnostic usefulness of a new proteomic technology, we performed Expression Difference Mapping analysis on 39 cancer cell lines from 9 different tissues using ProteinChip technology. A protein biomarker candid...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2003-09, Vol.309 (1), p.18-25 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Shiwa, Mieko Nishimura, Yumiko Wakatabe, Rumi Fukawa, Ai Arikuni, Hisashi Ota, Hiroyuki Kato, Yo Yamori, Takao |
| description | Useful biomarkers are needed for early detection of cancers. To demonstrate the potential diagnostic usefulness of a new proteomic technology, we performed Expression Difference Mapping analysis on 39 cancer cell lines from 9 different tissues using ProteinChip technology. A protein biomarker candidate of 12
kDa was found in colon cancer cells. We then optimized the purification conditions for this biomarker by utilizing Retentate Chromatography mass spectrometry (RC-MS). The optimized purification conditions developed “on-chip” were directly transferred to conventional chromatography to purify the biomarker, which was identified as prothymosin-α by ProteinChip time-of-flight mass spectrometry (TOF MS) and ProteinChip-Tandem MS systems. The relative expression level of prothymosin-α between colon cancer cells and normal colon mucosal cells was evaluated on the same ProteinChip platform. Prothymosin-α expression in colon cancer cells was clearly higher than in normal colon cells. These results indicate that prothymosin-α could be a potential biomarker for colon cancer, and that the ProteinChip platform could perform the whole process of biomarker discovery from screening to evaluation of the identified marker. |
| doi_str_mv | 10.1016/S0006-291X(03)01520-1 |
| format | Article |
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kDa was found in colon cancer cells. We then optimized the purification conditions for this biomarker by utilizing Retentate Chromatography mass spectrometry (RC-MS). The optimized purification conditions developed “on-chip” were directly transferred to conventional chromatography to purify the biomarker, which was identified as prothymosin-α by ProteinChip time-of-flight mass spectrometry (TOF MS) and ProteinChip-Tandem MS systems. The relative expression level of prothymosin-α between colon cancer cells and normal colon mucosal cells was evaluated on the same ProteinChip platform. Prothymosin-α expression in colon cancer cells was clearly higher than in normal colon cells. These results indicate that prothymosin-α could be a potential biomarker for colon cancer, and that the ProteinChip platform could perform the whole process of biomarker discovery from screening to evaluation of the identified marker.</description><subject>Biomarker</subject><subject>Biomarkers, Tumor</subject><subject>Colon - cytology</subject><subject>Colon - metabolism</subject><subject>Colon cancer</subject><subject>Dose-Response Relationship, Drug</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Expression Difference Mapping</subject><subject>Humans</subject><subject>Mass Spectrometry</subject><subject>Protein Array Analysis - methods</subject><subject>Protein Precursors - biosynthesis</subject><subject>ProteinChip</subject><subject>RC-MS</subject><subject>SELDI</subject><subject>Thymosin - analogs & derivatives</subject><subject>Thymosin - biosynthesis</subject><subject>Trypsin - pharmacology</subject><subject>Tumor Cells, Cultured</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1DAQhi0EokvhEUA-oXIIjGMnXp8Q2haotFIRBYmb5Thj1pDEwXYq9R14aLzdFT32NJLn-2c8_0_ISwZvGbD23TUAtFWt2I8z4G-ANTVU7BFZMVBQ1QzEY7L6j5yQZyn9AmBMtOopOWG1Erxt5Ir8_Wpm39PeJxtuMN5SM_XU9zhl77w12YeJBkcNzT6lBas0o913aF7GEGnnw2jib4zUxTBSruhuGc1ErZlsebQ4DHTwEya6JD_9pHmH9Ppie35Jv8SQ0U-bnZ_pPJjsQhyfkyfODAlfHOsp-f7x4tvmc7W9-nS5-bCtrGjWuUIwnImuE1J2rWtAQGvQiA6MFLBupOjLfarlqkZQNeOWAUonnYHaKYWcn5LXh7lzDH8WTFmP5f7yVzNhWJKWvCly3j4IMrluQLb7ic0BtDGkFNHpOfrizK1moPd56bu89D4MDVzf5aVZ0b06Lli6Eft71TGgArw_AFj8uPEYdbIei7m9j2iz7oN_YMU_uVal0A</recordid><startdate>20030912</startdate><enddate>20030912</enddate><creator>Shiwa, Mieko</creator><creator>Nishimura, Yumiko</creator><creator>Wakatabe, Rumi</creator><creator>Fukawa, Ai</creator><creator>Arikuni, Hisashi</creator><creator>Ota, Hiroyuki</creator><creator>Kato, Yo</creator><creator>Yamori, Takao</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20030912</creationdate><title>Rapid discovery and identification of a tissue-specific tumor biomarker from 39 human cancer cell lines using the SELDI ProteinChip platform</title><author>Shiwa, Mieko ; 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To demonstrate the potential diagnostic usefulness of a new proteomic technology, we performed Expression Difference Mapping analysis on 39 cancer cell lines from 9 different tissues using ProteinChip technology. A protein biomarker candidate of 12
kDa was found in colon cancer cells. We then optimized the purification conditions for this biomarker by utilizing Retentate Chromatography mass spectrometry (RC-MS). The optimized purification conditions developed “on-chip” were directly transferred to conventional chromatography to purify the biomarker, which was identified as prothymosin-α by ProteinChip time-of-flight mass spectrometry (TOF MS) and ProteinChip-Tandem MS systems. The relative expression level of prothymosin-α between colon cancer cells and normal colon mucosal cells was evaluated on the same ProteinChip platform. Prothymosin-α expression in colon cancer cells was clearly higher than in normal colon cells. These results indicate that prothymosin-α could be a potential biomarker for colon cancer, and that the ProteinChip platform could perform the whole process of biomarker discovery from screening to evaluation of the identified marker.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12943657</pmid><doi>10.1016/S0006-291X(03)01520-1</doi><tpages>8</tpages></addata></record> |
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| subjects | Biomarker Biomarkers, Tumor Colon - cytology Colon - metabolism Colon cancer Dose-Response Relationship, Drug Electrophoresis, Polyacrylamide Gel Expression Difference Mapping Humans Mass Spectrometry Protein Array Analysis - methods Protein Precursors - biosynthesis ProteinChip RC-MS SELDI Thymosin - analogs & derivatives Thymosin - biosynthesis Trypsin - pharmacology Tumor Cells, Cultured |
| title | Rapid discovery and identification of a tissue-specific tumor biomarker from 39 human cancer cell lines using the SELDI ProteinChip platform |
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