Defining glycoprotein cancer biomarkers by MS in conjunction with glycoprotein enrichment. (September 2015)

• Record Type: Journal Article
• Authors: Song, Ehwang; Mechref, Yehia
• Is Part Of: Biomarkers in medicine. Volume 9:Number 9(2015)
• Page Start: 835
• Page End: 844
• Publication Date: 2015-09
• Subjects: cancer biomarkers -- click-chemistry enrichment -- glycoproteomics -- glycoprotein enrichment -- HILIC enrichment -- hydrazide chemistry -- immunoaffinity-based enrichment -- LC-MS/MS -- lectin chromatography; Biochemical markers -- Periodicals; 610.28
• DOI: 10.2217/bmm.15.55
• Languages: English
• ISSNs: 1752-0363

Abstract

Protein glycosylation is an important and common post-translational modification. More than 50% of human proteins are believed to be glycosylated to modulate the functionality of proteins. Aberrant glycosylation has been correlated to several diseases, such as inflammatory skin diseases, diabetes mellitus, cardiovascular disorders, rheumatoid arthritis, Alzheimer's and prion diseases, and cancer. Many approved cancer biomarkers are glycoproteins which are not highly abundant proteins. Therefore, effective qualitative and quantitative assessment of glycoproteins entails enrichment methods. This chapter summarizes glycoprotein enrichment methods, including lectin affinity, immunoaffinity, hydrazide chemistry, hydrophilic interaction liquid chromatography, and click chemistry. The use of these enrichment approaches in assessing the qualitative and quantitative changes of glycoproteins in different types of cancers are presented and discussed. This chapter highlights the importance of glycoprotein enrichment techniques for the identification and characterization of new reliable cancer biomarkers.