Glycans and glycoproteins as specific biomarkers for cancer

Muchena J. Kailemia; Dayoung Park; Carlito B Lebrilla

doi:10.1007/s00216-016-9880-6

Glycans and glycoproteins as specific biomarkers for cancer

Muchena J. Kailemia, Dayoung Park, Carlito B Lebrilla

Biochemistry and Molecular Medicine

Research output: Contribution to journal › Article › peer-review

140 Scopus citations

Abstract

Protein glycosylation and other post-translational modifications are involved in potentially all aspects of human growth and development. Defective glycosylation has adverse effects on human physiological conditions and accompanies many chronic and infectious diseases. Altered glycosylation can occur at the onset and/or during tumor progression. Identifying these changes at early disease stages may aid in making decisions regarding treatments, as early intervention can greatly enhance survival. This review highlights some of the efforts being made to identify N- and O-glycosylation profile shifts in cancer using mass spectrometry. The analysis of single or panels of potential glycoprotein cancer markers are covered. Other emerging technologies such as global glycan release and site-specific glycosylation analysis and quantitation are also discussed. [Figure not available: see fulltext.]

Original language	English (US)
Pages (from-to)	1-16
Number of pages	16
Journal	Analytical and Bioanalytical Chemistry
DOIs	https://doi.org/10.1007/s00216-016-9880-6
State	Accepted/In press - Sep 3 2016

Keywords

Cancer
Disease biomarker
Glycomics
Glycoproteomics
Mass spectrometry
Site-specific glycosylation

ASJC Scopus subject areas

Analytical Chemistry
Biochemistry

Access to Document

10.1007/s00216-016-9880-6

Fingerprint Dive into the research topics of 'Glycans and glycoproteins as specific biomarkers for cancer'. Together they form a unique fingerprint.

Cite this

@article{77aa8a5269d04431acf76d0a3dec44f3,

title = "Glycans and glycoproteins as specific biomarkers for cancer",

abstract = "Protein glycosylation and other post-translational modifications are involved in potentially all aspects of human growth and development. Defective glycosylation has adverse effects on human physiological conditions and accompanies many chronic and infectious diseases. Altered glycosylation can occur at the onset and/or during tumor progression. Identifying these changes at early disease stages may aid in making decisions regarding treatments, as early intervention can greatly enhance survival. This review highlights some of the efforts being made to identify N- and O-glycosylation profile shifts in cancer using mass spectrometry. The analysis of single or panels of potential glycoprotein cancer markers are covered. Other emerging technologies such as global glycan release and site-specific glycosylation analysis and quantitation are also discussed. [Figure not available: see fulltext.]",

keywords = "Cancer, Disease biomarker, Glycomics, Glycoproteomics, Mass spectrometry, Site-specific glycosylation",

author = "Kailemia, {Muchena J.} and Dayoung Park and Lebrilla, {Carlito B}",

year = "2016",

month = sep,

day = "3",

doi = "10.1007/s00216-016-9880-6",

language = "English (US)",

pages = "1--16",

journal = "Fresenius Zeitschrift fur Analytische Chemie",

issn = "0016-1152",

publisher = "Springer Verlag",

}

TY - JOUR

T1 - Glycans and glycoproteins as specific biomarkers for cancer

AU - Kailemia, Muchena J.

AU - Park, Dayoung

AU - Lebrilla, Carlito B

PY - 2016/9/3

Y1 - 2016/9/3

N2 - Protein glycosylation and other post-translational modifications are involved in potentially all aspects of human growth and development. Defective glycosylation has adverse effects on human physiological conditions and accompanies many chronic and infectious diseases. Altered glycosylation can occur at the onset and/or during tumor progression. Identifying these changes at early disease stages may aid in making decisions regarding treatments, as early intervention can greatly enhance survival. This review highlights some of the efforts being made to identify N- and O-glycosylation profile shifts in cancer using mass spectrometry. The analysis of single or panels of potential glycoprotein cancer markers are covered. Other emerging technologies such as global glycan release and site-specific glycosylation analysis and quantitation are also discussed. [Figure not available: see fulltext.]

AB - Protein glycosylation and other post-translational modifications are involved in potentially all aspects of human growth and development. Defective glycosylation has adverse effects on human physiological conditions and accompanies many chronic and infectious diseases. Altered glycosylation can occur at the onset and/or during tumor progression. Identifying these changes at early disease stages may aid in making decisions regarding treatments, as early intervention can greatly enhance survival. This review highlights some of the efforts being made to identify N- and O-glycosylation profile shifts in cancer using mass spectrometry. The analysis of single or panels of potential glycoprotein cancer markers are covered. Other emerging technologies such as global glycan release and site-specific glycosylation analysis and quantitation are also discussed. [Figure not available: see fulltext.]

KW - Cancer

KW - Disease biomarker

KW - Glycomics

KW - Glycoproteomics

KW - Mass spectrometry

KW - Site-specific glycosylation

UR - http://www.scopus.com/inward/record.url?scp=84984918427&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84984918427&partnerID=8YFLogxK

U2 - 10.1007/s00216-016-9880-6

DO - 10.1007/s00216-016-9880-6

M3 - Article

C2 - 27590322

AN - SCOPUS:84984918427

SP - 1

EP - 16

JO - Fresenius Zeitschrift fur Analytische Chemie

JF - Fresenius Zeitschrift fur Analytische Chemie

SN - 0016-1152

ER -