N-Linked Oligosaccharides of Vomeromodulin, a Putative Pheromone Transporter in Rat

Mechref, Yehia; Ma, Weidong; Hao, Gang; Novotný, Miloš V.

doi:10.1006/bbrc.1999.0176

Cited by 16 publications

(10 citation statements)

References 16 publications

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“…It has indeed been observed that another lipocalin, the rat major urinary protein, remains active [14] and able to induce receptor‐mediated G protein activation of some vomeronasal receptor cells [15] when deprived of natural volatiles. Glycosylation of some olfactory active proteins suggests a potential role of oligosaccharide chains in the recognition process at the receptor site [16–22]. The lectin‐assisted blockage of rat olfaction supports a potential role of carbohydrates in mediating ligand binding protein or binding protein–receptor interactions [23].…”

Section: Introductionmentioning

confidence: 84%

Odorant and pheromone binding by aphrodisin, a hamster aphrodisiac protein

et al. 2000

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Aphrodisin is a soluble glycoprotein of hamster vaginal discharges, which stimulates male copulatory behavior. Natural aphrodisin was purified and its post-translational modifications characterized by MALDI-MS peptide mapping. To evaluate its ability to bind small volatile ligands, the aphrodisiac protein was expressed in the yeast Pichia pastoris as two major isoforms differing in their glycosylation degree, but close in conformation to the natural protein. Dimeric recombinant aphrodisins were equally able to efficiently bind odors (2-isobutyl-3-methoxypyrazine and methyl thiobutyrate) and a pheromone (dimethyl disulfide), suggesting that they could act as pheromone carriers instead of, or in addition to, direct vomeronasal neuron receptor activators. ß

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Section: Introductionmentioning

confidence: 84%

Odorant and pheromone binding by aphrodisin, a hamster aphrodisiac protein

et al. 2000

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“…LC‐MS/MS analysis was performed as previously described . The dried permethylated N‐glycans or free oligosaccharides were resuspended in 80 μL 20% ACN, 0.1% formic acid solution, then analyzed using UltiMate 3000 nano‐LC system (Dionex, Sunnyvale, CA, USA) coupled with LTQ Orbitrap Velos (Thermo Scientific, San Jose, CA, USA).…”

Section: Methodsmentioning

confidence: 99%

LC‐MS/MS analysis of permethylated free oligosaccharides and N‐glycans derived from human, bovine, and goat milk samples

2016

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Oligosaccharides in milk not only provide nutrition to the infants, but also have significant immune biofunctions such as inhibition of pathogen binding to the host cell. The main component in milk oligosaccharides is free oligosaccharides. Since the proteins in milk are highly glycosylated, N-glycans in milk also play an import role. In this study, we investigated the permethylated free oligosaccharides and N-glycans extracted from bovine, goat and human milk using LC-MS/MS. Quantitation profiles of free oligosaccharides and N-glycans were reported. The number of free oligosaccharides observed in bovine, goat and human milk samples (without isomeric consideration) were 11, 8 and 11 respectively. Human milk had more complex free oligosaccharides structures than the other two milk samples. Totally 58, 21, and 43 N-glycan structures (without isomeric consideration) were associated with whey proteins extracted from bovine, goat and human milk samples, respectively. Bovine milk free oligosaccharides and N-glycans from whey proteins were highly sialylated and to a lesser extend fucosylated. Goat and human milk free oligosaccharides and N-glycans from whey proteins were both highly fucosylated. Also, the isomeric glycans in milk samples were determined by PGC LC at elevated temperatures. For example, separation of human milk free oligosaccharide Gal-GlcNAc-(Fuc)-Gal-Glc and Gal-GlcNAc-Gal-Glc-Fuc isomers was achieved using PGC column. Permethylation of the glycan structures facilitated the interpretation of tandem MS. For example, internal cleavage and glycosidic bond cleavage are readily distinguished in the tandem mass spectra of permethylated glycans. This feature resulted in the identification of several isomers.

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“…This is particularly obvious in the sample‐limited situations where high‐sensitivity MS measurements can be seriously impaired by limitations in glycan cleavage conditions and sample preconcentration prior to MS. For the class of asparagine‐linked (N‐linked) oligosaccharides, we have successfully demonstrated2 the feasibility of the on‐plate enzymatic cleavage with N ‐glycanase and a subsequent sequencing with various exoglycosidases. Using this approach, low‐microgram amounts only were needed for a complete structural analysis of the glycoproteins isolated from rodent vomeronasal tissues 3,. 4…”

Section: Methodsmentioning

confidence: 99%

Matrix‐assisted laser desorption/ionization mass spectrometry compatible β‐elimination of O‐linked oligosaccharides

Huang

Konse

Mechref

et al. 2002

Rapid Comm Mass Spectrometry

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A new beta-elimination procedure has been introduced to cleave O-linked oligosaccharides from low- to sub-microgram amounts of glycoproteins prior to analysis by mass spectrometry. Borane-ammonia complex in aqueous ammonia is used as a cleaving solution alternative to the sodium borohydride/sodium hydroxide medium conventionally used in beta-elimination. The procedure results in minimum sample purification, leading to minimal sample loss and consequently an overall enhancement in sensitivity. It was applied successfully in the analysis of bovine fetuin and submaxillary mucin, as well as to a complex bile-salt-stimulated lipase glycoprotein isolated from human milk.

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N-Linked Oligosaccharides of Vomeromodulin, a Putative Pheromone Transporter in Rat

Cited by 16 publications

References 16 publications

Odorant and pheromone binding by aphrodisin, a hamster aphrodisiac protein

Odorant and pheromone binding by aphrodisin, a hamster aphrodisiac protein

LC‐MS/MS analysis of permethylated free oligosaccharides and N‐glycans derived from human, bovine, and goat milk samples

Matrix‐assisted laser desorption/ionization mass spectrometry compatible β‐elimination of O‐linked oligosaccharides

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