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Journal article
New Enzymatic Approach to Distinguish Fucosylation Isomers of N-Linked Glycans in Tissues Using MALDI Imaging Mass Spectrometry
Journal of proteome research, v 19(8), pp 2989-2996
07 Aug 2020
PMID: 32441096
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Specific alterations in N-linked glycans, such as core fucosylation, are associated with many cancers and other disease states. Because of the many possible anomeric linkages associated with fucosylated
-glycans, determination of specific anomeric linkages and the site of fucosylation (i.e., core vs outer arm) can be difficult to elucidate. A new MALDI mass spectrometry imaging workflow in formalin-fixed clinical tissues is described using recombinant endoglycosidase F3 (Endo F3), an enzyme with a specific preference for cleaving core-fucosylated
-glycans attached to glycoproteins. In contrast to the broader substrate enzyme peptide-
-glycosidase F (PNGaseF), Endo F3 cleaves between the two core
-acetylglucosamine residues at the protein attachment site. On tissues, this results in a mass shift of 349.137 a.m.u. for core-fucosylated
-glycans when compared to
-glycans released with standard PNGaseF. Endo F3 can be used singly and in combination with PNGaseF digestion of the same tissue sections. Initial results in liver and prostate tissues indicate core-fucosylated glycans associated to specific tissue regions while still demonstrating a diverse mix of core- and outer arm-fucosylated glycans throughout all regions of tissue. By determining these specific linkages while preserving localization, more targeted diagnostic biomarkers for disease states are possible without the need for microdissection or solubilization of the tissue.
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Details
- Title
- New Enzymatic Approach to Distinguish Fucosylation Isomers of N-Linked Glycans in Tissues Using MALDI Imaging Mass Spectrometry
- Creators
- Connor A West - Medical University of South CarolinaHongyan Liang - Medical University of South CarolinaRichard R Drake - Medical University of South CarolinaAnand S Mehta - Medical University of South Carolina
- Publication Details
- Journal of proteome research, v 19(8), pp 2989-2996
- Publisher
- American Chemical Society (ACS)
- Grant note
- R01 CA237659 / NCI NIH HHS U01 CA226052 / NCI NIH HHS U01 CA168856 / NCI NIH HHS R01 CA120206 / NCI NIH HHS U54 MD010706 / NIMHD NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Medicine (Graduate)
- Web of Science ID
- WOS:000562081000009
- Scopus ID
- 2-s2.0-85089610869
- Other Identifier
- 991021932695004721
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- Web of Science research areas
- Biochemical Research Methods