Journal
JOURNAL OF PROTEOME RESEARCH
Volume 9, Issue 6, Pages 3062-3072Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr901210r
Keywords
cancer; sialic acid; permethylation; amidation; lactonization
Categories
Funding
- National Cancer Institute, National Institutes of Health [UO1 CA128535-03]
- National Institute of General Medical Sciences, U.S. Department of Health and Human Services [GM24349]
- National Center for Research Resources, National Institutes of Health (NIH-NCRR) [RR018942]
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A number of alterations to the normal glycomic profile have been previously described for a number of diseases and disorders, thus underscoring the medical importance of studying the glycans associated with proteins present in biological samples. An important alteration in cancer progression is an increased level of alpha 2,6-sialylation, which aids in increasing the metastatic potential of tumor cells. Here we report a glycomic method that selectively amidates alpha 2,6-linked sialic acids, while those that are alpha 2,3-linked undergo spontaneous lactonization. Following subsequent permethylation, MALDI-TOF MS analysis revealed that many sialylated glycans present on glycoproteins found in blood serum featured increased levels of alpha 2,6-sialylation in breast cancer samples. On the basis of the altered ratios of alpha 2,3-linked to alpha 2,6-linked sialic acids, many of these glycans became diagnostically relevant when they did not act as such indicators when based on traditional glycomic profiling alone.
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