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The current state of proteomics in GI oncology.

Lin Y, Dynan WS, Lee JR, Zhu ZH, Schade RR - Dig. Dis. Sci. (2008)

Bottom Line: Proteomics refers to the study of the entire set of proteins in a given cell or tissue.In this article, we introduce the commonly adopted proteomic technologies and describe results of a comprehensive review of studies that have applied these technologies to GI oncology, with a particular emphasis on developments in the last 3 years.We discuss reasons why the more than 130 studies to date have had little discernible clinical impact, and we outline steps that may allow proteomics to realize its promise for early detection of disease, monitoring of disease recurrence, and identification of targets for individualized therapy.

View Article: PubMed Central - PubMed

Affiliation: Institute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, GA 30912, USA.

ABSTRACT
Proteomics refers to the study of the entire set of proteins in a given cell or tissue. With the extensive development of protein separation, mass spectrometry, and bioinformatics technologies, clinical proteomics has shown its potential as a powerful approach for biomarker discovery, particularly in the area of oncology. More than 130 exploratory studies have defined candidate markers in serum, gastrointestinal (GI) fluids, or cancer tissue. In this article, we introduce the commonly adopted proteomic technologies and describe results of a comprehensive review of studies that have applied these technologies to GI oncology, with a particular emphasis on developments in the last 3 years. We discuss reasons why the more than 130 studies to date have had little discernible clinical impact, and we outline steps that may allow proteomics to realize its promise for early detection of disease, monitoring of disease recurrence, and identification of targets for individualized therapy.

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Related in: MedlinePlus

MALDI-MS and ESI-MS procedures. a In MALDI-MS, samples are co-crystallized with an organic matrix on a metal target plate. A pulsed laser irradiates the co-crystals, which causes rapid heating and desorption of ions into the gas phase. Ions go through the mass analyzer and the detector registers the numbers of ions at each individual mass-to-charge (m/z) value, then the peptide mass fingerprint is generated. MALDI-MS produces relatively simple spectra composed of ions with unit charge. b In ESI-MS, sample molecules are ionized directly in the analyte solution by passing through a heated capillary device, spraying droplets of solution into a vacuum chamber containing a high-strength electric field. The resulting ions pass through a mass analyzer and detector as in a. ESI-MS produces complex spectra with multiply charged ions
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Fig3: MALDI-MS and ESI-MS procedures. a In MALDI-MS, samples are co-crystallized with an organic matrix on a metal target plate. A pulsed laser irradiates the co-crystals, which causes rapid heating and desorption of ions into the gas phase. Ions go through the mass analyzer and the detector registers the numbers of ions at each individual mass-to-charge (m/z) value, then the peptide mass fingerprint is generated. MALDI-MS produces relatively simple spectra composed of ions with unit charge. b In ESI-MS, sample molecules are ionized directly in the analyte solution by passing through a heated capillary device, spraying droplets of solution into a vacuum chamber containing a high-strength electric field. The resulting ions pass through a mass analyzer and detector as in a. ESI-MS produces complex spectra with multiply charged ions

Mentions: Options for final MS analysis are similar in all approaches. A “soft ionization” procedure creates peptide ions in the gas phase, using mild conditions that maintain peptide bonds intact. In matrix-assisted laser desorption ionization (MALDI) (and its specialized variations, SELDI and IMS) a laser pulse is directed at a mixture of protein sample and an organic matrix (Fig. 3a) [22]. With electrospray ionization (ESI), the other common soft ionization method, a protein or peptide solution passes through a heated capillary, spraying droplets of solution into a vacuum chamber containing a strong electric field, where they then evaporate and ionize (Fig. 3b) [23]. The ions are passed through a mass analyzer, which separates them based on mass-to-charge (m/z) ratio.Fig. 3


The current state of proteomics in GI oncology.

Lin Y, Dynan WS, Lee JR, Zhu ZH, Schade RR - Dig. Dis. Sci. (2008)

MALDI-MS and ESI-MS procedures. a In MALDI-MS, samples are co-crystallized with an organic matrix on a metal target plate. A pulsed laser irradiates the co-crystals, which causes rapid heating and desorption of ions into the gas phase. Ions go through the mass analyzer and the detector registers the numbers of ions at each individual mass-to-charge (m/z) value, then the peptide mass fingerprint is generated. MALDI-MS produces relatively simple spectra composed of ions with unit charge. b In ESI-MS, sample molecules are ionized directly in the analyte solution by passing through a heated capillary device, spraying droplets of solution into a vacuum chamber containing a high-strength electric field. The resulting ions pass through a mass analyzer and detector as in a. ESI-MS produces complex spectra with multiply charged ions
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3045515&req=5

Fig3: MALDI-MS and ESI-MS procedures. a In MALDI-MS, samples are co-crystallized with an organic matrix on a metal target plate. A pulsed laser irradiates the co-crystals, which causes rapid heating and desorption of ions into the gas phase. Ions go through the mass analyzer and the detector registers the numbers of ions at each individual mass-to-charge (m/z) value, then the peptide mass fingerprint is generated. MALDI-MS produces relatively simple spectra composed of ions with unit charge. b In ESI-MS, sample molecules are ionized directly in the analyte solution by passing through a heated capillary device, spraying droplets of solution into a vacuum chamber containing a high-strength electric field. The resulting ions pass through a mass analyzer and detector as in a. ESI-MS produces complex spectra with multiply charged ions
Mentions: Options for final MS analysis are similar in all approaches. A “soft ionization” procedure creates peptide ions in the gas phase, using mild conditions that maintain peptide bonds intact. In matrix-assisted laser desorption ionization (MALDI) (and its specialized variations, SELDI and IMS) a laser pulse is directed at a mixture of protein sample and an organic matrix (Fig. 3a) [22]. With electrospray ionization (ESI), the other common soft ionization method, a protein or peptide solution passes through a heated capillary, spraying droplets of solution into a vacuum chamber containing a strong electric field, where they then evaporate and ionize (Fig. 3b) [23]. The ions are passed through a mass analyzer, which separates them based on mass-to-charge (m/z) ratio.Fig. 3

Bottom Line: Proteomics refers to the study of the entire set of proteins in a given cell or tissue.In this article, we introduce the commonly adopted proteomic technologies and describe results of a comprehensive review of studies that have applied these technologies to GI oncology, with a particular emphasis on developments in the last 3 years.We discuss reasons why the more than 130 studies to date have had little discernible clinical impact, and we outline steps that may allow proteomics to realize its promise for early detection of disease, monitoring of disease recurrence, and identification of targets for individualized therapy.

View Article: PubMed Central - PubMed

Affiliation: Institute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, GA 30912, USA.

ABSTRACT
Proteomics refers to the study of the entire set of proteins in a given cell or tissue. With the extensive development of protein separation, mass spectrometry, and bioinformatics technologies, clinical proteomics has shown its potential as a powerful approach for biomarker discovery, particularly in the area of oncology. More than 130 exploratory studies have defined candidate markers in serum, gastrointestinal (GI) fluids, or cancer tissue. In this article, we introduce the commonly adopted proteomic technologies and describe results of a comprehensive review of studies that have applied these technologies to GI oncology, with a particular emphasis on developments in the last 3 years. We discuss reasons why the more than 130 studies to date have had little discernible clinical impact, and we outline steps that may allow proteomics to realize its promise for early detection of disease, monitoring of disease recurrence, and identification of targets for individualized therapy.

Show MeSH
Related in: MedlinePlus