Pancreatic cancer is a highly lethal disease that is very difficult to diagnose and treat. The effective treatment of pancreatic cancer is critically relying on the diagnosis of the disease at an early stage. Because the current methods for diagnosing very early pancreatic cancer are ineffective, there is an urgent need for new biomarkers. These biomarkers would be particularly useful in patients who are at increased risk of developing pancreatic cancer and who have an abnormal pancreas because of chronic pancreatitis or cystic lesions. Such lesions can be difficult to manage because of the uncertainty regarding neoplastic progression. Pancreatic juice is a proximal body fluid and represents an opportune specimen for identifying biomarkers of pancreatic cancer. Cancer cells are preferentially shed into the ductal lumen, making juice a rich source of cancer associated markers. In the past few years, a large number of pancreatic cancer biomarker candidates have been identified by proteomics and other techniques. Validation of these biomarker candidates is an important step to close the gap between bench research and clinical application, and has been the major bottleneck for biomarker development for pancreatic cancer diagnosis. In the proposed study, we plan to characterize a selected group of pancreatic cancer biomarker candidates for their performance in pancreatic juice for pancreatic cancer detection. Our patient cohort will include those with cancer and the early stages of pre-cancer versus diseased controls with cystic lesions and pancreatitis. A complementary approach of biomarker development will combine state-of-the-art immunoassays and targeted proteomic assays. These assays will be applied to evaluate the protein candidates in clinical pancreatic juice specimens. Biomarkers developed from this study could be used to aide in assessment of high-risk patients undergoing endoscopic procedures. It is also possible that these biomarkers could be further developed into blood based test for early detection of pancreatic cancer.

Public Health Relevance

We plan to investigate biomarkers for early detection of pancreatic cancer. If we are successful in this goal, it is likely that we could make a significant impact in the detection and management of this deadly cancer.

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Exploratory/Developmental Grants (R21)
Project #
1R21CA161575-01
Application #
8166376
Study Section
Cancer Biomarkers Study Section (CBSS)
Program Officer
Wagner, Paul D
Project Start
2011-08-01
Project End
2013-07-31
Budget Start
2011-08-01
Budget End
2012-07-31
Support Year
1
Fiscal Year
2011
Total Cost
$214,333
Indirect Cost
Name
University of Washington
Department
Internal Medicine/Medicine
Type
Schools of Medicine
DUNS #
605799469
City
Seattle
State
WA
Country
United States
Zip Code
98195
Chen, Ru; Dawson, David W; Pan, Sheng et al. (2015) Proteins associated with pancreatic cancer survival in patients with resectable pancreatic ductal adenocarcinoma. Lab Invest 95:43-55
Pan, Sheng; Brentnall, Teresa A; Chen, Ru (2015) Proteomics analysis of bodily fluids in pancreatic cancer. Proteomics 15:2705-15
Pan, Sheng; Chen, Ru; Tamura, Yasuko et al. (2014) Quantitative glycoproteomics analysis reveals changes in N-glycosylation level associated with pancreatic ductal adenocarcinoma. J Proteome Res 13:1293-306
Pan, Sheng; Brentnall, Teresa A; Kelly, Kimberly et al. (2013) Tissue proteomics in pancreatic cancer study: discovery, emerging technologies, and challenges. Proteomics 13:710-21
Chen, Ru; Pan, Sheng; Ottenhof, Niki A et al. (2012) Stromal galectin-1 expression is associated with long-term survival in resectable pancreatic ductal adenocarcinoma. Cancer Biol Ther 13:899-907
Pan, Sheng; Chen, Ru; Brand, Randall E et al. (2012) Multiplex targeted proteomic assay for biomarker detection in plasma: a pancreatic cancer biomarker case study. J Proteome Res 11:1937-48
Pan, Sheng; Tamura, Yasuko; Chen, Ru et al. (2012) Large-scale quantitative glycoproteomics analysis of site-specific glycosylation occupancy. Mol Biosyst 8:2850-6