About: Characterisation of N-glycans in the epithelial-like tissue of the rat cochlea

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About: Characterisation of N-glycans in the epithelial-like tissue of the rat cochlea Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Characterisation of N-glycans in the epithelial-like tissue of the rat cochlea
Creator	Hanzawa, Ken Hibino, Hiroshi Higuchi, Taiga Horii, Arata Inohara, Hidenori Miyoshi, Eiji Natsuka, Shunji Nin, Fumiaki Nishikaze, Takashi Nonomura, Yoriko Okuda, Shujiro Sawamura, Seishiro Takahashi, Sugata Uetsuka, Satoru Sekiya,
topic	covid:575ce9765e914a2bdb2a02b265905f9e7e781c67#this
source	PMC
abstract	Membrane proteins (such as ion channels, transporters, and receptors) and secreted proteins are essential for cellular activities. N-linked glycosylation is involved in stability and function of these proteins and occurs at Asn residues. In several organs, profiles of N-glycans have been determined by comprehensive analyses. Nevertheless, the cochlea of the mammalian inner ear, a tiny organ mediating hearing, has yet to be examined. Here, we focused on the stria vascularis, an epithelial-like tissue in the cochlea, and characterised N-glycans by liquid chromatography with mass spectrometry. This hypervascular tissue not only expresses several ion transporters and channels to control the electrochemical balance in the cochlea but also harbours different transporters and receptors that maintain structure and activity of the organ. Seventy-nine N-linked glycans were identified in the rat stria vascularis. Among these, in 55 glycans, the complete structures were determined; in the other 24 species, partial glycosidic linkage patterns and full profiles of the monosaccharide composition were identified. In the process of characterisation, several sialylated glycans were subjected sequentially to two different alkylamidation reactions; this derivatisation helped to distinguish α2,3-linkage and α2,6-linkage sialyl isomers with mass spectrometry. These data should accelerate elucidation of the molecular architecture of the cochlea.
has issue date	2019-02-07(xsd:dateTime)
bibo:doi	10.1038/s41598-018-38079-0
bibo:pmid	30733536
has license	cc-by
sha1sum (hex)	575ce9765e914a2bdb2a02b265905f9e7e781c67
schema:url	https://doi.org/10.1038/s41598-018-38079-0
resource representing a document's title	Characterisation of N-glycans in the epithelial-like tissue of the rat cochlea
has PubMed Central identifier	PMC6367448
has PubMed identifier	30733536
schema:publication	Sci Rep
resource representing a document's body	covid:575ce9765e914a2bdb2a02b265905f9e7e781c67#body_text
is http://vocab.deri.ie/void#inDataset of	https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/575ce9765e914a2bdb2a02b265905f9e7e781c67
is schema:about of	named entity 'LIKE' named entity 'TISSUE' named entity 'ION CHANNELS' named entity 'FOCUSED' named entity 'TO BE EXAMINED' named entity 'ESSENTIAL' named entity 'TISSUE' named entity 'BALANCE' named entity 'INVOLVED' named entity 'COMPREHENSIVE' named entity 'DERIVATISATION' named entity 'MONOSACCHARIDE' named entity 'ORGAN' named entity 'MEMBRANE PROTEINS' named entity 'HEARING' named entity 'STRUCTURES' named entity 'HERE' named entity 'TRANSPORTERS' named entity 'COCHLEA' named entity 'N-GLYCANS' named entity 'MAINTAIN' named entity 'SPECIES' named entity 'ACTIVITY' named entity 'DETERMINED' named entity 'PATTERNS' named entity 'GLYCANS' named entity 'LIQUID CHROMATOGRAPHY ' named entity 'FUNCTION' named entity '2C6' named entity 'MAMMALIAN' named entity 'PARTIAL' named entity 'RECEPTORS' named entity 'EPITHELIAL' named entity 'LIKE' named entity 'MASS SPECTROMETRY' named entity 'TO CONTROL' named entity 'INNER EAR' named entity 'DETERMINED BY' named entity 'CELLULAR' named entity 'THESE' named entity 'REACTIONS' named entity 'RAT' named entity 'ORGANS' named entity 'N-GLYCANS' named entity 'PROCESS' named entity 'ACTIVITIES' named entity 'DIFFERENT' named entity 'N-LINKED GLYCOSYLATION' named entity 'DATA' named entity 'STRIA VASCULARIS' named entity 'COMPOSITION' named entity 'ARCHITECTURE' named entity 'COMPLETE' named entity 'SEVENTY-NINE' named entity 'SECRETED' named entity 'PROTEINS' named entity 'IDENTIFIED' named entity 'RAT' named entity 'EPITHELIAL' named entity 'MEDIATING' named entity 'STABILITY' named entity 'B12' named entity 'ION' named entity 'LINKAGE' named entity 'ACCELERATE'

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