Journal article
Novel Combined Enzymatic Approach to Analyze Nonsialylated N-Linked Glycans through MALDI Imaging Mass Spectrometry
Journal of proteome research, v 21(8), pp 1930-1938
05 Aug 2022
PMID: 35766466
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Alterations to N-glycan expression are relevant to the progression of various diseases, particularly cancer. In many cases, specific N-glycan structural features such as sialylation, fucosylation, and branching are of specific interest. A novel MALDI imaging mass spectrometry workflow has been recently developed to analyze these features of N-glycosylation through the utilization of endoglycosidase enzymes to cleave N-glycans from associated glycoproteins. Enzymes that have previously been utilized to cleave N-glycans include peptide-N-glycosidase F (PNGase F) to target N-glycans indiscriminately and endoglycosidase F3 (Endo F3) to target core fucosylated N-glycans. In addition to these endoglycosidases, additional N-glycan cleaving enzymes could be used to target specific structural features. Sialidases, also termed neuraminidases, are a family of enzymes that remove terminal sialic acids from glycoconjugates. This work aims to utilize sialidase, in conjunction with PNGase F/Endo F3, to enzymatically remove sialic acids from N-glycans in an effort to increase sensitivity for nonsialylated N-glycan MALDI-IMS peaks. Improving detection of nonsialylated N-glycans allows for a more thorough analysis of specific structural features such as fucosylation or branching, particularly of low abundant structures. Sialidase utilization in MALDI-IMS dramatically increases sensitivity and increases on-tissue endoglycosidase efficiency, making it a very useful companion technique to specifically detect nonsialylated N-glycans.
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Details
- Title
- Novel Combined Enzymatic Approach to Analyze Nonsialylated N-Linked Glycans through MALDI Imaging Mass Spectrometry
- Creators
- Andrew T. DelaCourt - Medical University of South CarolinaHongyan Liang - Medical University of South CarolinaRichard R. Drake - Medical University of South CarolinaPeggi M. Angel - Medical University of South CarolinaAnand S. Mehta - Medical University of South Carolina
- Publication Details
- Journal of proteome research, v 21(8), pp 1930-1938
- Publisher
- Amer Chemical Soc
- Number of pages
- 9
- Grant note
- CA226052 / National Cancer Institute; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Cancer Institute (NCI)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Medicine (Graduate)
- Web of Science ID
- WOS:000823201900001
- Scopus ID
- 2-s2.0-85134799283
- Other Identifier
- 991021932695604721
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- Web of Science research areas
- Biochemical Research Methods