Glycomic mapping of <Emphasis Type="Italic">O-</Emphasis> and <Emphasis Type="Italic">N-</Emphasis>linked glycans from major rat sublingual mucin |
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Authors: | Shin-Yi Yu Kay-Hooi Khoo Zhangung Yang Anthony Herp Albert M Wu |
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Institution: | (1) Institute of Biochemical Sciences, National Taiwan University, Taipei, 106, Taiwan;(2) National Core Facilities for Proteomics and Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei, 115, Taiwan;(3) Glyco-Immunochemistry Research Laboratory, Institute of Molecular and Cellular Biology, Chang-Gung University, 333, Kwei-san Tao-yuan, Taiwan |
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Abstract: | Carbohydrate moieties of salivary mucins play various roles in life processes, especially as a microbial trapping agent. While
structural details of the salivary O-glycans from several mammalian sources are well studied, very little information is currently available for the corresponding
N-glycans. The existence of N-glycans alongside O-glycans on mucin isolated from rat sublingual gland has previously been implicated by total glycosyl compositional analysis
but the respective structural data are both lacking. The advent of facile glycomic mapping and sequencing methods by mass
spectrometry (MS) has enabled a structural reinvestigation into many previously unsolved issues. For the first time, high
energy collision induced dissociation (CID) MALDI-MS/MS as implemented on a TOF/TOF instrument was applied to permethyl derivatives
of mucin type O-glycans and N-glycans, from which the linkage specific fragmentation pattern could be established. The predominant O-glycans carried on the rat sublingual mucin were defined as sialylated core 3 and 4 types whereas the N-glycans were determined to be non-bisected hybrid types similarly carrying a sialylated type II chain. The masking effect
of terminal sialylation on the tight binding of rat sublingual mucin to Galβ1→4GlcNAc specific lectins and three oligomannose
specific lectins were clearly demonstrated in this study. |
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Keywords: | Lectin binding N-glycans Rat sublingual gland Salivary mucin Mass spectrometry |
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