A multiplexed bead assay for profiling glycosylation patterns on serum protein biomarkers of pancreatic cancer
dc.contributor.author | Guttman, Andras | en_US |
dc.date.accessioned | 2011-11-10T15:35:53Z | |
dc.date.available | 2012-10-01T18:34:34Z | en_US |
dc.date.issued | 2011-08 | en_US |
dc.identifier.citation | Guttman, 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.issn | 0173-0835 | en_US |
dc.identifier.issn | 1522-2683 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/87003 | |
dc.description.abstract | A 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.publisher | WILEY‐VCH Verlag | en_US |
dc.subject.other | Antibody | en_US |
dc.subject.other | Bead‐Based Multiplexed Assay | en_US |
dc.subject.other | Biomarker | en_US |
dc.subject.other | Cancer | en_US |
dc.subject.other | Glycoproteins | en_US |
dc.title | A multiplexed bead assay for profiling glycosylation patterns on serum protein biomarkers of pancreatic cancer | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Chemistry, The University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Internal Medicine, The University of Michigan Medical Center, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Surgery and Physiology, The University of Michigan Medical Center, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Surgery, The University of Michigan Medical Center, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Comprehensive Cancer Center, The University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Surgery, The University of Michigan Medical Center, 1150 West Medical Center Dr. Building MSRB1 Rm A510B, Ann Arbor, MI 48109, USA Fax: +1‐734‐615‐2088 | en_US |
dc.contributor.affiliationother | Department of Urology, The University of Texas, San Antonio, TX, USA | en_US |
dc.contributor.affiliationother | Assay Designs, Inc., Ann Arbor, MI, USA | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/87003/1/2028_ftp.pdf | |
dc.identifier.doi | 10.1002/elps.201000693 | en_US |
dc.identifier.source | ELECTROPHORESIS | en_US |
dc.identifier.citedreference | Kameyama, A., Kaneda, Y., Yamanaka, H., Yoshimine, H., Narimatsu, H., Shinohara, Y., Anal. Chem. 2004, 76, 4537 – 4542. | en_US |
dc.identifier.citedreference | Nilsson, B., Mol. Biotechnol. 1994, 2, 243 – 280. | en_US |
dc.identifier.citedreference | Wada, Y., Tajiri, M., Yoshida, S., Anal. Chem. 2004, 76, 6560 – 6565. | en_US |
dc.identifier.citedreference | Imre, T., Schlosser, G., Pocsfalvi, G., Siciliano, R., J. Mass Spectrom. 2005, 40, 1472 – 1483. | en_US |
dc.identifier.citedreference | Kameyama, A., Kikuchi, N., Nakaya, S., Ito, H., Sato, T., Shikanai, T., Takahashi, Y., Takahashi, K., Narimatsu, H., Anal. Chem. 2005, 77, 4719 – 4725. | en_US |
dc.identifier.citedreference | Palm, A. K., Novotny, M. V., Rapid Commun. Mass Spectrom. 2005, 19, 1730 – 1738. | en_US |
dc.identifier.citedreference | Yu, Y. Q., Gilar, M., Kaska, J., Gebler, J. C., Rapid Commun. Mass Spectrom. 2005, 19, 2331 – 2336. | en_US |
dc.identifier.citedreference | Zhao, J., Simeone, D. M., Heidt, D., Anderson, M. A., Lubman, D. M., J. Proteome Res. 2006, 5, 1792 – 1802. | en_US |
dc.identifier.citedreference | Reis, C. A., Osorio, H., Silva, L., Gomes, C., David, L., J. Clin. Pathol. 2010, 63, 322 – 329. | en_US |
dc.identifier.citedreference | Plavina, T., Wakshull, E., Hancock, W. S., Hincapie, M. J., Proteome Res. 2007, 2, 662 – 671. | en_US |
dc.identifier.citedreference | Gorelik, E., Galili, U., Raz, A., Cancer Metastasis Rev. 2001, 20, 245 – 277. | en_US |
dc.identifier.citedreference | Hakomori, S., Adv. Cancer Res. 1989, 52, 257 – 331. | en_US |
dc.identifier.citedreference | Drake, R. R., Schwegler, E. E., Malik, G., Diaz, J., Block, T., Mehta, A., Semmes, O. J., Mol. Cell. Proteomics 2006, 10, 1957 – 1967. | en_US |
dc.identifier.citedreference | Kobata, A., Amano, J., Immunol. Cell Biol. 2005, 83, 429 – 439. | en_US |
dc.identifier.citedreference | Balzarini, J., Nat. Rev. Microbiol. 2007, 8, 583 – 597. | en_US |
dc.identifier.citedreference | Kellokumpu, S., Sormunen, R., Kellokumpu, M., FEBS Lett. 2002, 516, 217 – 224. | en_US |
dc.identifier.citedreference | Peracaula, R., Tabares, G., Royle, L., Harvey, D. J., Dwek, R. A., Rudd, P. M., de Llorens, R. A., Glycobiology 2003, 13, 457 – 470. | en_US |
dc.identifier.citedreference | Jemal, A., Tiwari, R. C., Murray, T., Ghafoor, A., Samuels, A., Ward, E., Feuer, E. J., Thun, M. J., CA Cancer J. Clin. 2004, 54, 8 – 29. | en_US |
dc.identifier.citedreference | Sohn, T. A., Lillemoe, K. D., Cameron, J. L., Huang, J. J., Pitt, H. A., Yeo, C. J. J., Am. Coll. Surg. 1999, 188, 658 – 666. | en_US |
dc.identifier.citedreference | Larghi, A., Verna, E. C., Lecca, P. G., Costamagna, G., Clin. Cancer Res. 2009, 15, 1907 – 1914. | en_US |
dc.identifier.citedreference | Dalgleish, A. G., Br. Med. J. 2000, 321, 380 – 380. | en_US |
dc.identifier.citedreference | Nazli, O., Bozdag, A. D., Tansug, T., Kir, R., Kaymak, E., Hepatogastroenterology 2000, 47, 1750 – 1752. | en_US |
dc.identifier.citedreference | Goggins, M., J. Clin. Oncol. 2005, 23, 4524 – 4531. | en_US |
dc.identifier.citedreference | Grantzdorffer, I., Carl–McGrath, S., Ebert, M. P., Rocken, C., Pancreas 2008, 36, 329 – 336. | en_US |
dc.identifier.citedreference | Vimalachandran, D., Costello, E., Expert. Rev. Proteomics 2004, 1, 493 – 501. | en_US |
dc.identifier.citedreference | Yu, K. H., Barry, C. G., Austin, D., Busch, C. M., Sangar, V., Rustgi, A. K., Blair, I. A., J. Proteome. Res. 2009, 8, 1565 – 1576. | en_US |
dc.identifier.citedreference | Faca, V. M., Song, K. S., Wang, H., Zhang, Q., Krasnoselsky, A. L., Newcomb, L. F., Plentz, R. R., Gurumurthy, S., Redston, M. S., Pitteri, S. J., Pereira–Faca, S. R., Ireton, R. C., Katayama, H., Glukhova, V., Phanstiel, D., Brenner, D. E., Anderson, M. A., Misek, D., Scholler, N., Urban, N. D., Barnett, M. J., Edelstein, C., Goodman, G. E., Thornquist, M. D., McIntosh, M. W., DePinho, R. A., Bardeesy, N., Hanash, S. M., PLoS. Med. 2008, 5, e123. | en_US |
dc.identifier.citedreference | Zhao, J., Patwa, T. H., Qiu, W. L., Shedden, K., Hinderer, R., Misek, D. E., Anderson, M. A., Simeone, D. M., Lubman, D. M., J. Proteome Res. 2007, 5, 1864 – 1874. | en_US |
dc.identifier.citedreference | Wu, Y. M., Nowack, D. D., Omenn, G. S., Haab, B. B., J. Proteome Res. 2009, 8, 1876 – 1886. | en_US |
dc.identifier.citedreference | Li, C., Simeone, D. M., Brenner, D. E., Anderson, M. A., Shedden, K. A., Ruffin, M. T., Lubman, D. M., J. Proteome Res. 2009, 8, 483 – 492. | en_US |
dc.identifier.citedreference | Chen, S. M., LaRoche, T., Hamelinck, D., Bergsma, D., Brenner, D., Simeone, D., Brand, R. E., Haab, B. B., Nat. Methods 2007, 5, 437 – 444. | en_US |
dc.identifier.citedreference | Joos, T. O., Stoll, D., Templin, M. F., Curr. Opin. Chem. Biol. 2002, 6, 76 – 80. | en_US |
dc.identifier.citedreference | Morgan, E., Varro, R., Sepulveda, H., Ember, J. A., Apgar, J., Wilson, J., Lowe, L., Chen, R., Shivraj, L., Agadir, A., Campos, R., Ernst, D., Gaur, A., Clin. Immunol. 2004, 110, 252 – 266. | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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