ArticleJournal of chromatography. B, Analytical technologies in the biomedical and life sciences2012
Purification, identification and profiling of serum amyloid A proteins from sera of advanced-stage cancer patients.
Article in Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Proteomic Analyses of the Mouse Brain.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Acute-phase serum amyloid A for early detection of hepatocellular carcinoma in cirrhotic patients with low AFP level.Scientific reports · 2022Article
- Use of Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry Analysis of Serum Peptidome to Classify and Predict Coronavirus Disease 2019 Severity.Open forum infectious diseases · 2021Article
- Cloning, Purification, and Characterization of the Catalytic C-Terminal Domain of the Human 3-Hydroxy-3-methyl glutaryl-CoA Reductase: An Effective, Fast, and Easy Method for Testing Hypocholesterolemic Compounds.Molecular biotechnology · 2020Article
- [Research Progress of Biomakers Proteomics-based in Lung Cancer].Zhongguo fei ai za zhi = Chinese journal of lung cancer · 2015Review
- Discovery of serum biomarkers of ovarian cancer using complementary proteomic profiling strategies.Proteomics. Clinical applications · 2014Article
- Comparative proteomic profiles indicating genetic factors may involve in hepatocellular carcinoma familial aggregation.Cancer science · 2012Article
- Review
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Surface-enhanced laser desorption/ionization time of flight mass spectrometry (SELDI-TOF-MS) is a powerful tool for screening potential biomarkers of various pathological conditions. However, low resolution and mass accuracy of SELDI-TOF-MS remain a major obstacle for determination of biological identities of potential protein biomarkers. We report here a refined workflow that combines ZipTip desalting, acetonitrile precipitation, high-performance liquid chromatography (HPLC) separation and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF-MS) analysis for the profiling, purification and identification of the targeted serum proteins found by SELDI-TOF-MS. By using this workflow, we purified ten targeted proteins from the sera of patients with various types of advanced stage (stage III-IV) cancers. These proteins were identified as isoforms of the human serum amyloid protein A (SAA) family with or without truncations at their N-terminals. This was confirmed by Western blot analysis. Different SAA expression patterns were observed by MALDI-TOF-MS profiling. SAA has long been reported as a biomarker for various cancer types such as lung cancer, ovarian cancer, and breast cancer. However, in this study we found increased SAA expression in the sera of advanced-stage cancer patients with different cancer types. Our results suggest that maybe SAA should not be used alone as a biomarker for any specific cancer type.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.