Marcadores tumorales y reactantes de fase aguda en el diagnóstico del cáncer de páncreas

Oyarzabal, AM Irigoyen; García, JA Amiguet; Vivanco, Guillermo López; Subirats, Jose Genollá; Villafranca, MC Muñoz; Martínez, E.; Irurzun, P. Liso

doi:10.1157/13055132

Cited by 3 publications

(2 citation statements)

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“…The serine protease inhibitors (serpins), a-1-antitrypsin and a-1-antichymotrypsin, have been specifically linked to pancreatic cancer. [71][72][73][74][75][76] The serpin peptides are consistently observed in most of the samples (>80%) and, with the exception of m/z 1778.9 from a-1-antitrypsin, do not differ significantly between sample groups. While increased expression and secretion of protease inhibitors is consistent with pancreatic cancer and increased protease expression and release, these species have not been specific enough to have clinical utility for diagnosis, because they are involved with the acute phase response, which modulates not only host-tumor interactions, but also inflammation and response to bacterial infection.…”

Section: Discussionmentioning

confidence: 99%

Diagnostic protein discovery using proteolytic peptide targeting and identification

Koomen

Zhao

et al. 2004

Rapid Comm Mass Spectrometry

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Plasma protein profiling with mass spectrometry is currently being evaluated as a diagnostic tool for cancer and other diseases. These experiments consist of three steps: plasma protein fractionation, analysis with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS), and comparisons of the MALDI profiles to develop diagnostic fingerprints using bioinformatic techniques. While preliminary results appear promising in small sample groups, the method is limited by the sensitivity of MALDI-MS for intact proteins, the limited mass range of MALDI-MS, and difficulties associated with isolating individual proteins for identification to validate the diagnostic fingerprint. Here we present an alternative and improved method directed toward diagnostic protein discovery, which incorporates proteolytic peptide profiling, bioinformatic targeting of ion signals, and MALDI tandem mass spectrometry (MS/MS) peptide sequencing, rather than fingerprinting. Pancreatic cancer patients, pancreatitis patients, and controls are used as the model system. Profiling peptides after enzymatic digestion improves sensitivity and extends the accessible protein molecular weight range when compared to intact protein profiling. The first step is to extract and fractionate the proteins from plasma. Each fraction is digested with trypsin and subsequently analyzed by MALDI-MS. Rather than using bioinformatic analysis as a pattern-matching technique, peptides are targeted based on the disease to control peak intensity ratios measured in the averages of all mass spectra in each group and t-tests of the intensity of each individual peak. The targeted peptide ion signals are subsequently identified using MALDI-MS/MS in quadrupole-TOF and tandem-TOF instruments. This study found not only the proteins targeted and identified by a previous protein profiling experiment, but also detected additional proteins. These initial results are consistent with the known biology of pancreatic cancer or pancreatitis, but are not specific to those diseases.

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Section: Discussionmentioning

confidence: 99%

Diagnostic protein discovery using proteolytic peptide targeting and identification

Koomen

Zhao

et al. 2004

Rapid Comm Mass Spectrometry

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“…S4). In addition, 17 of these proteins have been previously shown to be up-regulated in pancreatic cancer in at least four studies (61), and 10 have been shown to be elevated in pancreatic cancer serum in comparison to controls (60,(63)(64)(65)(66)(67)(68)(69)(70)(71) (Table III). The unstudied proteins might yield promising new candidate biomarkers for pancreatic cancer.…”

Section: Differential Expression Of Proteins In Cancer Versus Normalmentioning

confidence: 94%

Integrated Proteomic Profiling of Cell Line Conditioned Media and Pancreatic Juice for the Identification of Pancreatic Cancer Biomarkers

Makawita

Smith

Batruch

et al. 2011

Molecular & Cellular Proteomics

100

102

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Pancreatic cancer is one of the leading causes of cancerrelated deaths, for which serological biomarkers are urgently needed. Most discovery-phase studies focus on the use of one biological source for analysis. The present study details the combined mining of pancreatic cancerrelated cell line conditioned media and pancreatic juice for identification of putative diagnostic leads. Using strong cation exchange chromatography, followed by LC-MS/MS on an LTQ-Orbitrap mass spectrometer, we extensively characterized the proteomes of conditioned media from six pancreatic cancer cell lines (BxPc3, MIAPaCa2, PANC1, CAPAN1, CFPAC1, and SU.86.86), the normal human pancreatic ductal epithelial cell line HPDE, and two pools of six pancreatic juice samples from ductal adenocarcinoma patients. All samples were analyzed in triplicate. Between 1261 and 2171 proteins were identified with two or more peptides in each of the cell lines, and an average of 521 proteins were identified in the pancreatic juice pools. In total, 3479 nonredundant proteins were identified with high confidence, of which ϳ40% were extracellular or cell membrane-bound based on Genome Ontology classifications. Three strategies were employed for identification of candidate biomarkers: (1) examination of differential protein expression between the cancer and normal cell lines using label-free protein quantification, (2) integrative analysis, focusing on the overlap of proteins among the multiple biological fluids, and (3) tissue specificity analysis through mining of publically available databases. Preliminary verification of anterior gradient homolog 2, syncollin, olfactomedin-4, polymeric immunoglobulin receptor, and collagen alpha-1(VI) chain in plasma samples from pancreatic cancer patients and healthy controls using ELISA, showed a significant increase (p < 0.01) of these proteins in plasma from pancreatic cancer patients. The combination of these five proteins showed an improved area under the receiver operating characteristic curve to CA19.9 alone.

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Production and Characterization of Monoclonal Antibodies against Human Ceruloplasmin

Eum¹,

Choi²,

Kim³

et al. 2005

BMB Reports

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Ceruloplasmin (CP) is the major plasma antioxidant and copper transport protein. Monoclonal antibodies (mAbs) against human CP were produced and characterized. A total of five hybridoma cell lines were established (CP2, CP10, CP20, CP25, CP30). From the epitope mapping analysis, two subgroups of mAbs recognize different peptide fragments were identified. When the purified CP was incubated with the mAbs, the ferroxidase activity of CP was inhibited up to a maximum 57 %. Immunoblotting with various tissue homogenates indicated that all the mAbs specifically recognize a single protein band of 130 kDa. They also appear to be extensively cross-reactive among different mammalian including human and avian sources. These results demonstrated that only one type of immunologically similar CP is present in all of the mammalian tissues including human. The CP mAbs could be of great benefit to design the diagnostic kit for CP-related diseases such as Wilson's disease.

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Marcadores tumorales y reactantes de fase aguda en el diagnóstico del cáncer de páncreas

Cited by 3 publications

References 0 publications

Diagnostic protein discovery using proteolytic peptide targeting and identification

Diagnostic protein discovery using proteolytic peptide targeting and identification

Integrated Proteomic Profiling of Cell Line Conditioned Media and Pancreatic Juice for the Identification of Pancreatic Cancer Biomarkers

Production and Characterization of Monoclonal Antibodies against Human Ceruloplasmin

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