Screening for serological biomarkers of pancreatic cancer by two-dimensional electrophoresis and liquid chromatography-tandem mass spectrometry

Wang, Yufeng; Kuramitsu, Yasuhiro; Yoshino, Shigefumi; Takashima, Motonari; Zhang, Xiulian; Ueno, Tomio; Suzuki, Nobuaki; Oka, M.; Nakamura, Kazuyuki

doi:10.3892/or.2011.1278

Cited by 6 publications

(2 citation statements)

References 18 publications

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“…Seven protein spots were differentially expressed. Serum isoforms of alpha-1-antitrypsin (AAT), also confirmed by western blot, were described as upregulated and potential serum biomarkers for pancreatic cancer [90]. …”

Section: Mass Spectrometry: the Cancer Biomarker Discovery Toolmentioning

confidence: 99%

Serum Biomarkers Identification by Mass Spectrometry in High-Mortality Tumors

Tessitore

Gaggiano

Cicciarelli

et al. 2013

International Journal of Proteomics

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Cancer affects millions of people worldwide. Tumor mortality is substantially due to diagnosis at stages that are too late for therapies to be effective. Advances in screening methods have improved the early diagnosis, prognosis, and survival for some cancers. Several validated biomarkers are currently used to diagnose and monitor the progression of cancer, but none of them shows adequate specificity, sensitivity, and predictive value for population screening. So, there is an urgent need to isolate novel sensitive, specific biomarkers to detect the disease early and improve prognosis, especially in high-mortality tumors. Proteomic techniques are powerful tools to help in diagnosis and monitoring of treatment and progression of the disease. During the last decade, mass spectrometry has assumed a key role in most of the proteomic analyses that are focused on identifying cancer biomarkers in human serum, making it possible to identify and characterize at the molecular level many proteins or peptides differentially expressed. In this paper we summarize the results of mass spectrometry serum profiling and biomarker identification in high mortality tumors, such as ovarian, liver, lung, and pancreatic cancer.

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Section: Mass Spectrometry: the Cancer Biomarker Discovery Toolmentioning

confidence: 99%

Serum Biomarkers Identification by Mass Spectrometry in High-Mortality Tumors

Tessitore

Gaggiano

Cicciarelli

et al. 2013

International Journal of Proteomics

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“…RCN1 has been demonstrated to be highly expressed in a variety of tumor cells and is correlated with patient prognosis in renal cell carcinoma, prostate cancer, glioblastoma, non-small cell lung cancer, oral squamous cell carcinoma, nasopharyngeal cancer, colon cancer, laryngeal cancer, highly aggressive breast cancer, sorafenib-resistant hepatocellular carcinoma cells, and gemcitabine-insensitive human pancreatic adenocarcinoma cells, among others [20][21][22]24,25,27,[55][56][57][58][59][60][61][62][63]. Yoshida et al [64] reported that RCN1 was expressed in lymphatic endothelial cells (T-LECs) and lung cancer cells in lung tumors, but not in lymphatic endothelial cells (N-LECs) in nontumor tissues.…”

Section: Discussionmentioning

confidence: 99%

Downregulation of RCN1 promotes pyroptosis in acute myeloid leukemia cells

Deng,

Pan,

et al. 2023

Molecular Oncology

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Reticulocalbin‐1 (RCN1) is expressed aberrantly and at a high level in various tumors, including acute myeloid leukemia (AML), yet its impact on AML remains unclear. In this study, we demonstrate that RCN1 knockdown significantly suppresses the viability of bone marrow mononuclear cells (BMMNCs) from AML patients but does not affect the viability of granulocyte colony‐stimulating factor (G‐CSF)‐mobilized peripheral blood stem cells (PBSCs) from healthy donors in vitro. Downregulation of RCN1 also reduces the viability of AML cell lines. Further studies showed that the RCN1 knockdown upregulates type I interferon (IFN‐1) expression and promotes AML cell pyroptosis through caspase‐1 and gasdermin D (GSDMD) signaling. Deletion of the mouse Rcn1 gene inhibits the viability of mouse AML cell lines but not the hematopoiesis of mouse bone marrow. In addition, RCN1 downregulation in human AML cells significantly inhibited tumor growth in the NSG mouse xenograft model. Taken together, our results suggest that RCN1 may be a potential target for AML therapy.

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Proteomics analysis of bodily fluids in pancreatic cancer

2015

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Proteomics study of pancreatic cancer using bodily fluids emphasizes biomarker discovery and clinical application, presenting unique prospect and challenges. Depending on the physiological nature of the bodily fluid and its proximity to pancreatic cancer, the proteomes of bodily fluids, such as pancreatic juice, pancreatic cyst fluid, blood, bile and urine, can be substantially different in terms of protein constitution and the dynamic range of protein concentration. Thus, a comprehensive discovery and specific detection of cancer-associated proteins within these varied fluids is a complex task, requiring rigorous experiment design and a concerted approach. While major challenges still remain, fluid proteomics studies in pancreatic cancer to date have provided a wealth of information in revealing proteome alterations associated with pancreatic cancer in various bodily fluids.

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Screening for serological biomarkers of pancreatic cancer by two-dimensional electrophoresis and liquid chromatography-tandem mass spectrometry

Cited by 6 publications

References 18 publications

Serum Biomarkers Identification by Mass Spectrometry in High-Mortality Tumors

Serum Biomarkers Identification by Mass Spectrometry in High-Mortality Tumors

Downregulation of RCN1 promotes pyroptosis in acute myeloid leukemia cells

Proteomics analysis of bodily fluids in pancreatic cancer

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