Mass Spectrometric Analysis of Protein Markers for Ovarian Cancer
| Autor: | Zheng Wang, Xiao-Ying Meng, Yong Ying, Jing Wang, Christine Yip, Lee Lomas, Eric T. Fung, Tai-Tung Yip |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Analyte
Clinical Biochemistry Protein Array Analysis Enzyme-Linked Immunosorbent Assay Antibodies Mass Spectrometry Reference Values Alpha-Globulins Biomarkers Tumor medicine Humans Prealbumin Survival rate Apolipoproteins A Ovarian Neoplasms biology medicine.diagnostic_test Chemistry Biochemistry (medical) Cancer medicine.disease Molecular biology Transthyretin Immunoassay biology.protein Female Antibody Ovarian cancer |
| Zdroj: | Clinical Chemistry. 50:1939-1942 |
| ISSN: | 1530-8561 0009-9147 |
| DOI: | 10.1373/clinchem.2004.036871 |
| Popis: | Ovarian cancer is the fifth leading cause of death from cancer in women and is the leading cause of gynecologic death in developed countries. Although the overall 5-year survival rate of patients with ovarian cancer is only 25%, the survival rate of patients diagnosed with early-stage ovarian cancer (I/IIa) approaches 90% (1). Therefore, a noninvasive diagnostic test that can detect early-stage ovarian cancer would be highly desirable, particularly if it could be coupled to a second, noninvasive diagnostic test such as transvaginal ultrasound. In a recently completed multiinstitutional protein expression profiling study encompassing 503 women from four institutions, we developed a three-marker panel that could distinguish women with early-stage ovarian cancer from healthy controls with higher diagnostic accuracy than could CA125 (area under the curve, 92% vs 77%) (2). Purification and identification of the three markers revealed that they were a truncated form of transthyretin, full-length apolipoprotein A1, and an internal fragment of inter-α-trypsin inhibitor heavy chain 4 (ITIH4). Transthyretin is known to be cysteinylated and glutathionylated in addition to being truncated (3). ITIH4 is cleaved at multiple sites, generating numerous cleavage products (4). Conventional immunoassays generally cannot simultaneously distinguish or quantify multiple posttranslationally modified forms of a protein or its isoforms. Mass spectrometry (MS)-based assays have the advantage of being able to do so, but are often not considered to be quantitative. Because of the chromatographic nature of the ProteinChip® array surface, surface-enhanced laser desorption/ionization time-of-flight (SELDI-TOF)-MS has the advantage of being quantitative (5). When immunocapture is coupled with SELDI-TOF-MS, a single immunoassay can quantify multiple forms of an analyte. The immunocapture can be performed directly on the ProteinChip array surface (by use of a reactive surface array) or on beads coated with antibody. In the latter case, the bound material is eluted onto ProteinChip arrays. Several antibodies to … |
| Databáze: | OpenAIRE |
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