Comparative glycomic profiling in esophageal adenocarcinoma

Zane T. Hammoud, Yehia Mechref, Ahmed Hussein, Slavka Bekesova, Min Zhang, Kenneth Kesler, Milos V. Novotny

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Objective: Aberrant glycosylation has been implicated in various types of cancers. Cancerous cells with altered glycosylation of their surface proteins shed such proteins into the circulating fluids. Glycomic profiling of such fluids shows the altered glycosylation. We performed glycomic profiling of serum from patients with no known disease, Barrett's without dysplasia, with high-grade dysplasia, and with esophageal adenocarcinoma in an attempt to delineate distinct differences in glycosylation among these groups. Methods: Serum samples from patients with Barrett's metaplasia (N = 5), high-grade dysplasia (N = 11), and esophageal adenocarcinoma (N = 50) were collected; samples from 18 healthy volunteers were used as control. Serum N-glycans were enzymatically released and then applied to both C18 Sep-Pak (Waters, Milford, MA) cartridges and activated charcoal cartridges. N-glycans were permethylated and then spotted directly onto a matrix-assisted laser desorption ionization plate. Mass spectra were acquired using the Applied Biosystems 4800 MALDI TOF/TOF Analyzer (Applied Biosystems Inc, Framingham, Mass). The obtained matrix-assisted laser desorption ionization-mass spectrometry data were processed using DataExplorer files (Applied Biosystems Inc) listing m/z values and intensities. Results: The intensities of 98 glycans were significantly different among the 3 groups; 26 of these corresponded to known glycan structures. Pairwise comparisons showed that 8 glycans were significantly different in all 3 pairwise comparisons. Conclusion: We demonstrated that comparative glycomic profiling of esophageal adenocarcinoma reveals a subset of glycans that can be selected as candidate biomarkers. These markers can differentiate normal from high-grade dysplasia, normal from esophageal adenocarcinoma, and high-grade dysplasia from esophageal adenocarcinoma. Further validation will be necessary to determine the clinical utility of these glycan biomarkers.

Original languageEnglish
Pages (from-to)1216-1223
Number of pages8
JournalJournal of Thoracic and Cardiovascular Surgery
Volume139
Issue number5
DOIs
StatePublished - May 2010

Fingerprint

Glycomics
Polysaccharides
Adenocarcinoma
Glycosylation
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Biomarkers
Serum
Barrett Esophagus
Charcoal
Healthy Volunteers
Membrane Proteins
Lasers
Water

ASJC Scopus subject areas

  • Cardiology and Cardiovascular Medicine
  • Surgery
  • Pulmonary and Respiratory Medicine

Cite this

Hammoud, Z. T., Mechref, Y., Hussein, A., Bekesova, S., Zhang, M., Kesler, K., & Novotny, M. V. (2010). Comparative glycomic profiling in esophageal adenocarcinoma. Journal of Thoracic and Cardiovascular Surgery, 139(5), 1216-1223. https://doi.org/10.1016/j.jtcvs.2009.12.045

Comparative glycomic profiling in esophageal adenocarcinoma. / Hammoud, Zane T.; Mechref, Yehia; Hussein, Ahmed; Bekesova, Slavka; Zhang, Min; Kesler, Kenneth; Novotny, Milos V.

In: Journal of Thoracic and Cardiovascular Surgery, Vol. 139, No. 5, 05.2010, p. 1216-1223.

Research output: Contribution to journalArticle

Hammoud, ZT, Mechref, Y, Hussein, A, Bekesova, S, Zhang, M, Kesler, K & Novotny, MV 2010, 'Comparative glycomic profiling in esophageal adenocarcinoma', Journal of Thoracic and Cardiovascular Surgery, vol. 139, no. 5, pp. 1216-1223. https://doi.org/10.1016/j.jtcvs.2009.12.045
Hammoud, Zane T. ; Mechref, Yehia ; Hussein, Ahmed ; Bekesova, Slavka ; Zhang, Min ; Kesler, Kenneth ; Novotny, Milos V. / Comparative glycomic profiling in esophageal adenocarcinoma. In: Journal of Thoracic and Cardiovascular Surgery. 2010 ; Vol. 139, No. 5. pp. 1216-1223.
@article{877cf7ba9eb8453a980690fda8b4ba78,
title = "Comparative glycomic profiling in esophageal adenocarcinoma",
abstract = "Objective: Aberrant glycosylation has been implicated in various types of cancers. Cancerous cells with altered glycosylation of their surface proteins shed such proteins into the circulating fluids. Glycomic profiling of such fluids shows the altered glycosylation. We performed glycomic profiling of serum from patients with no known disease, Barrett's without dysplasia, with high-grade dysplasia, and with esophageal adenocarcinoma in an attempt to delineate distinct differences in glycosylation among these groups. Methods: Serum samples from patients with Barrett's metaplasia (N = 5), high-grade dysplasia (N = 11), and esophageal adenocarcinoma (N = 50) were collected; samples from 18 healthy volunteers were used as control. Serum N-glycans were enzymatically released and then applied to both C18 Sep-Pak (Waters, Milford, MA) cartridges and activated charcoal cartridges. N-glycans were permethylated and then spotted directly onto a matrix-assisted laser desorption ionization plate. Mass spectra were acquired using the Applied Biosystems 4800 MALDI TOF/TOF Analyzer (Applied Biosystems Inc, Framingham, Mass). The obtained matrix-assisted laser desorption ionization-mass spectrometry data were processed using DataExplorer files (Applied Biosystems Inc) listing m/z values and intensities. Results: The intensities of 98 glycans were significantly different among the 3 groups; 26 of these corresponded to known glycan structures. Pairwise comparisons showed that 8 glycans were significantly different in all 3 pairwise comparisons. Conclusion: We demonstrated that comparative glycomic profiling of esophageal adenocarcinoma reveals a subset of glycans that can be selected as candidate biomarkers. These markers can differentiate normal from high-grade dysplasia, normal from esophageal adenocarcinoma, and high-grade dysplasia from esophageal adenocarcinoma. Further validation will be necessary to determine the clinical utility of these glycan biomarkers.",
author = "Hammoud, {Zane T.} and Yehia Mechref and Ahmed Hussein and Slavka Bekesova and Min Zhang and Kenneth Kesler and Novotny, {Milos V.}",
year = "2010",
month = "5",
doi = "10.1016/j.jtcvs.2009.12.045",
language = "English",
volume = "139",
pages = "1216--1223",
journal = "Journal of Thoracic and Cardiovascular Surgery",
issn = "0022-5223",
publisher = "Mosby Inc.",
number = "5",

}

TY - JOUR

T1 - Comparative glycomic profiling in esophageal adenocarcinoma

AU - Hammoud, Zane T.

AU - Mechref, Yehia

AU - Hussein, Ahmed

AU - Bekesova, Slavka

AU - Zhang, Min

AU - Kesler, Kenneth

AU - Novotny, Milos V.

PY - 2010/5

Y1 - 2010/5

N2 - Objective: Aberrant glycosylation has been implicated in various types of cancers. Cancerous cells with altered glycosylation of their surface proteins shed such proteins into the circulating fluids. Glycomic profiling of such fluids shows the altered glycosylation. We performed glycomic profiling of serum from patients with no known disease, Barrett's without dysplasia, with high-grade dysplasia, and with esophageal adenocarcinoma in an attempt to delineate distinct differences in glycosylation among these groups. Methods: Serum samples from patients with Barrett's metaplasia (N = 5), high-grade dysplasia (N = 11), and esophageal adenocarcinoma (N = 50) were collected; samples from 18 healthy volunteers were used as control. Serum N-glycans were enzymatically released and then applied to both C18 Sep-Pak (Waters, Milford, MA) cartridges and activated charcoal cartridges. N-glycans were permethylated and then spotted directly onto a matrix-assisted laser desorption ionization plate. Mass spectra were acquired using the Applied Biosystems 4800 MALDI TOF/TOF Analyzer (Applied Biosystems Inc, Framingham, Mass). The obtained matrix-assisted laser desorption ionization-mass spectrometry data were processed using DataExplorer files (Applied Biosystems Inc) listing m/z values and intensities. Results: The intensities of 98 glycans were significantly different among the 3 groups; 26 of these corresponded to known glycan structures. Pairwise comparisons showed that 8 glycans were significantly different in all 3 pairwise comparisons. Conclusion: We demonstrated that comparative glycomic profiling of esophageal adenocarcinoma reveals a subset of glycans that can be selected as candidate biomarkers. These markers can differentiate normal from high-grade dysplasia, normal from esophageal adenocarcinoma, and high-grade dysplasia from esophageal adenocarcinoma. Further validation will be necessary to determine the clinical utility of these glycan biomarkers.

AB - Objective: Aberrant glycosylation has been implicated in various types of cancers. Cancerous cells with altered glycosylation of their surface proteins shed such proteins into the circulating fluids. Glycomic profiling of such fluids shows the altered glycosylation. We performed glycomic profiling of serum from patients with no known disease, Barrett's without dysplasia, with high-grade dysplasia, and with esophageal adenocarcinoma in an attempt to delineate distinct differences in glycosylation among these groups. Methods: Serum samples from patients with Barrett's metaplasia (N = 5), high-grade dysplasia (N = 11), and esophageal adenocarcinoma (N = 50) were collected; samples from 18 healthy volunteers were used as control. Serum N-glycans were enzymatically released and then applied to both C18 Sep-Pak (Waters, Milford, MA) cartridges and activated charcoal cartridges. N-glycans were permethylated and then spotted directly onto a matrix-assisted laser desorption ionization plate. Mass spectra were acquired using the Applied Biosystems 4800 MALDI TOF/TOF Analyzer (Applied Biosystems Inc, Framingham, Mass). The obtained matrix-assisted laser desorption ionization-mass spectrometry data were processed using DataExplorer files (Applied Biosystems Inc) listing m/z values and intensities. Results: The intensities of 98 glycans were significantly different among the 3 groups; 26 of these corresponded to known glycan structures. Pairwise comparisons showed that 8 glycans were significantly different in all 3 pairwise comparisons. Conclusion: We demonstrated that comparative glycomic profiling of esophageal adenocarcinoma reveals a subset of glycans that can be selected as candidate biomarkers. These markers can differentiate normal from high-grade dysplasia, normal from esophageal adenocarcinoma, and high-grade dysplasia from esophageal adenocarcinoma. Further validation will be necessary to determine the clinical utility of these glycan biomarkers.

UR - http://www.scopus.com/inward/record.url?scp=77950889301&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77950889301&partnerID=8YFLogxK

U2 - 10.1016/j.jtcvs.2009.12.045

DO - 10.1016/j.jtcvs.2009.12.045

M3 - Article

VL - 139

SP - 1216

EP - 1223

JO - Journal of Thoracic and Cardiovascular Surgery

JF - Journal of Thoracic and Cardiovascular Surgery

SN - 0022-5223

IS - 5

ER -