title: A quantitative investigation of fucosylated serum glycoproteins with application to esophageal adenocarcinoma.
abstract: Although glycoproteomic studies provide unique opportunities for cancer research, it has been necessary to develop specific methods for analysis of oncologically interesting glycoproteins. We describe a general, multimethodological approach for quantitative glycoproteomic analysis of fucosylated glycoproteins in human blood serum. A total of 136 putative fucosylated glycoproteins were identified with very high confidence in three clinically relevant sample pools (N=5 for each), with a mean CV of 3.1% observed for replicate analyses. Two samples were collected from subjects diagnosed with esophagus disease states, high-grade dysplasia plus esophageal adenocarcinoma, while the third sample was representative of a disease-free condition. Some glycoproteins, observed to be significantly upregulated in esophageal adenocarcinoma, i.e. more than twofold higher than in the disease-free condition, are briefly discussed. Further investigation will be necessary to validate these findings; however, the method itself is demonstrated to be an effective tool for quantitative glycoproteomics of clinical samples.
authors.affiliation: Department of Chemistry, Indiana University, Bloomington, IN 47405, USA.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Mann
authors.forename: Milan
authors.initials: M
authors.lastname: Madera
authors.forename: Iveta
authors.initials: I
authors.lastname: Klouckova
authors.forename: Yehia
authors.initials: Y
authors.lastname: Mechref
authors.forename: Lacey E
authors.initials: LE
authors.lastname: Dobrolecki
authors.forename: Robert J
authors.initials: RJ
authors.lastname: Hickey
authors.forename: Zane T
authors.initials: ZT
authors.lastname: Hammoud
authors.forename: Milos V
authors.initials: MV
authors.lastname: Novotny
mesh_terms: D000230:Adenocarcinoma / Q000097:blood*; D024042:Collagen Type I / Q000032:analysis / Q000097:blood; D000090602:Collagen Type I, alpha 1 Chain; D004938:Esophageal Neoplasms / Q000097:blood*; D060752:Fetuin-B; D005643:Fucose / Q000097:blood*; D006023:Glycoproteins / Q000032:analysis / Q000097:blood*; D006801:Humans; D037102:Lectins / Q000737:chemistry; D010446:Peptide Fragments / Q000032:analysis / Q000378:metabolism; D020543:Proteome / Q000032:analysis*; D014357:Trypsin / Q000378:metabolism; D000509:alpha-Fetoproteins / Q000032:analysis / Q000378:metabolism
chemical_list: D024042:Collagen Type I; D000090602:Collagen Type I, alpha 1 Chain; C426245:EMILIN2 protein, human; C504687:FETUB protein, human; D060752:Fetuin-B; D006023:Glycoproteins; D037102:Lectins; D010446:Peptide Fragments; D020543:Proteome; D000509:alpha-Fetoproteins; C027112:fucose-binding lectin; C064549:lectin, Aleuria aurantia; D005643:Fucose; D014357:Trypsin
references.citation: Nat Biotechnol. 2003 Jun;21(6):660-6
references.pmid: 12754519
references.citation: J Sep Sci. 2008 Aug;31(14):2722-32
references.pmid: 18623281
references.citation: Dis Markers. 2008;25(4-5):219-32
references.pmid: 19126966
references.citation: Anal Chem. 2003 Sep 15;75(18):4818-26
references.pmid: 14674459
references.citation: Gut. 1991 Jan;32(1):16-20
references.pmid: 1991632
references.citation: J Proteome Res. 2006 Feb;5(2):277-86
references.pmid: 16457593
references.citation: Clin Chem. 2008 Jul;54(7):1166-75
references.pmid: 18487288
references.citation: Anal Chem. 2004 Nov 15;76(22):6560-5
references.pmid: 15538777
references.citation: J Proteome Res. 2005 Jan-Feb;4(1):153-60
references.pmid: 15707370
references.citation: Int J Cancer. 2008 Mar 1;122(5):1019-29
references.pmid: 17957794
references.citation: Science. 2001 Mar 23;291(5512):2370-6
references.pmid: 11269318
references.citation: J Chromatogr A. 2004 Oct 22;1053(1-2):79-88
references.pmid: 15543974
references.citation: Anticancer Drug Des. 1987 Oct;2(2):211-29
references.pmid: 2835061
references.citation: Glycobiology. 1993 Apr;3(2):97-130
references.pmid: 8490246
references.citation: J Biol Chem. 1982 Oct 10;257(19):11235-40
references.pmid: 7118881
references.citation: FEBS Lett. 2009 Jun 5;583(11):1703-12
references.pmid: 19306877
references.citation: Glycobiology. 2006 Feb;16(2):132-45
references.pmid: 16177264
references.citation: J Pathol. 2004 Nov;204(3):333-9
references.pmid: 15476275
references.citation: Rapid Commun Mass Spectrom. 2008 Dec;22(23):3823-34
references.pmid: 18985620
references.citation: Anal Chem. 2005 Jul 1;77(13):4081-90
references.pmid: 15987113
references.citation: J Proteome Res. 2007 Feb;6(2):662-71
references.pmid: 17269723
references.citation: Gastrointest Endosc. 2001 Jun;53(7):751-7
references.pmid: 11375583
references.citation: Clin Cancer Res. 2003 Oct 15;9(13):4819-25
references.pmid: 14581353
references.citation: Glycobiology. 2008 Dec;18(12):1105-18
references.pmid: 18818422
references.citation: Front Biosci (Landmark Ed). 2009 Jan 01;14:2911-22
references.pmid: 19273244
references.citation: J Biol Chem. 1954 Dec;211(2):969-80
references.pmid: 13221602
references.citation: Hum Pathol. 2002 Jan;33(1):29-38
references.pmid: 11823971
references.citation: Electrophoresis. 2009 Sep;30(17):2957-2966
references.pmid: 19711376
references.citation: J Urol. 2001 Dec;166(6):2472-83
references.pmid: 11696814
references.citation: Physiol Rev. 1996 Jan;76(1):69-125
references.pmid: 8592733
references.citation: Pathol Int. 1998 Jan;48(1):1-9
references.pmid: 9589457
references.citation: Mol Cell Biol. 2007 Oct;27(20):7176-87
references.pmid: 17698584
references.citation: Mol Cell Proteomics. 2006 Apr;5(4):714-25
references.pmid: 16401633
references.citation: Glycobiology. 2007 Dec;17(12):1344-56
references.pmid: 17884841
references.citation: J Proteome Res. 2009 Jun;8(6):2656-66
references.pmid: 19441788
references.citation: Biotechniques. 2004 Oct;37(4):621-4, 626-33, 636 passim
references.pmid: 15517975