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A multiplexed bead assay for profiling glycosylation patterns on serum protein biomarkers of pancreatic cancer

dc.contributor.authorGuttman, Andrasen_US
dc.date.accessioned2011-11-10T15:35:53Z
dc.date.available2012-10-01T18:34:34Zen_US
dc.date.issued2011-08en_US
dc.identifier.citationGuttman, Andras (2011). "A multiplexed bead assay for profiling glycosylation patterns on serum protein biomarkers of pancreatic cancer ." ELECTROPHORESIS 32(15): 2028-2035. <http://hdl.handle.net/2027.42/87003>en_US
dc.identifier.issn0173-0835en_US
dc.identifier.issn1522-2683en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/87003
dc.description.abstractA multiplexed bead‐based immunoassay was developed to simultaneously profile glycosylation patterns of serum proteins to investigate their usefulness as biomarkers for pancreatic cancer. The multiplex assay utilized protein‐specific capture antibodies chemically coupled individually to beads labeled with specific amounts of fluorescent dye. Captured proteins were detected based on the extent and specific type of glycosylation as determined by successive binding of fluorescent lectin probes. Advantages to this technique include the fact that antibodies coupled to the beads had minimal nonspecific binding to the lectins ConA/SNA, avoiding the step of chemically blocking the antibody glycans and the bead assays were performed in a 96‐well filter plate enabling high‐throughput screening applications with improved reproducibility. The assay was tested with ConA and SNA lectins to examine the glycosylation patterns of α‐1‐β glycoprotein (A1BG) and serum amyloid p (SAP) component for use as potential biomarkers for the detection of pancreatic cancer based on the results from prior biomarker studies. The results showed that the SNA response on the captured A1BG protein could distinguish chronic pancreatitis samples from pancreatic cancer with a p ‐value of 0.035 and for the SAP protein with SNA, a p ‐value of 0.026 was found between the signal of normal controls and the pancreatic cancer samples. For the ConA response, a decline in the signal for both proteins in the serum samples was found to distinguish pancreatic cancer from normal controls and renal cell carnoma samples (A1BG, p <0.05; and SAP, p <0.0001).en_US
dc.publisherWILEY‐VCH Verlagen_US
dc.subject.otherAntibodyen_US
dc.subject.otherBead‐Based Multiplexed Assayen_US
dc.subject.otherBiomarkeren_US
dc.subject.otherCanceren_US
dc.subject.otherGlycoproteinsen_US
dc.titleA multiplexed bead assay for profiling glycosylation patterns on serum protein biomarkers of pancreatic canceren_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Chemistry, The University of Michigan, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumDepartment of Internal Medicine, The University of Michigan Medical Center, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumDepartment of Surgery and Physiology, The University of Michigan Medical Center, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumDepartment of Surgery, The University of Michigan Medical Center, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumComprehensive Cancer Center, The University of Michigan, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumDepartment of Surgery, The University of Michigan Medical Center, 1150 West Medical Center Dr. Building MSRB1 Rm A510B, Ann Arbor, MI 48109, USA Fax: +1‐734‐615‐2088en_US
dc.contributor.affiliationotherDepartment of Urology, The University of Texas, San Antonio, TX, USAen_US
dc.contributor.affiliationotherAssay Designs, Inc., Ann Arbor, MI, USAen_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/87003/1/2028_ftp.pdf
dc.identifier.doi10.1002/elps.201000693en_US
dc.identifier.sourceELECTROPHORESISen_US
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dc.owningcollnameInterdisciplinary and Peer-Reviewed


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