Murine submandibular mucin (MSM): a mucin carrying N- and O-glycosylically bound carbohydrate-chains

Amerongen, A. van Nieuw; Oderkerk, C.H.; Roukema, P.A.; Wolf, J.H.; Lisman, Jan J.W.; Overdijk, B.

doi:10.1016/0008-6215(83)88162-2

Cited by 13 publications

(1 citation statement)

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“…In early reports, absence of N-linked glycans was considered as a distinct salivary mucin feature [7]. Since then, however, several salivary mucins were reported to carry N-glycosylation, but mostly based on variable amounts of mannose content detected and not defined structures [1,13,14]. It remains unclear to summarize if the salivary mucins secreted by a particular gland carry a distinctive N-glycosylation pattern.…”

Section: Introductionmentioning

confidence: 94%

Glycomic mapping of O- and N-linked glycans from major rat sublingual mucin

Khoo

Yang

et al. 2007

Glycoconj J

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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 Galbeta1-->4GlcNAc specific lectins and three oligomannose specific lectins were clearly demonstrated in this study.

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