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 | |
| State | Accepted/In press - Sep 3 2016 |
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Keywords
- Cancer
- Disease biomarker
- Glycomics
- Glycoproteomics
- Mass spectrometry
- Site-specific glycosylation
ASJC Scopus subject areas
- Analytical Chemistry
- Biochemistry
Cite this
Glycans and glycoproteins as specific biomarkers for cancer. / Kailemia, Muchena J.; Park, Dayoung; Lebrilla, Carlito B.
In: Analytical and Bioanalytical Chemistry, 03.09.2016, p. 1-16.Research output: Contribution to journal › Article
}
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 -