Biomaterial Database

Ultracytochemistry of glycoconjugates in rat Brunner's gland with labeled lectins. 1990

S Yotsumoto, and S Tsuyama, and M Tashiro, and F Murata

Department of Dermatology, Faculty of Medicine, Kagoshima University, Japan.

Mucous glycoproteins of rat Brunner's gland were examined ultracytochemically to elucidate the intracellular localization and sites of glycosylation in relation to the functional polarity of the cell organellae using a combination of hydrophilic resin embedment and postembedding staining with labeled lectins. A few cis cisternae were stained with HPA (Helix pomatia agglutinin, specific for terminal alpha-N-acetylgalactosamine) and DBA (Dolichos biflorus aggulutinin, specific for terminal alpha-N-acetylgalactosamine). Trans cisternae as well as cisternae following secretory granules were stained with HPA and RCA-I (Recinus communis agglutinin I, specific for terminal beta-galactose). UEA-I (Ulex europaeus agglutinin I, specific for terminal alpha-L-fucose) seemed to bind to transmost cisternae rather than trans cisternae. HPA bound to the whole cisternae, but to the cis or trans cisternae depending on a cell type. Apical mucous granules were stained with UEA-I, RCA-I, and HPA, but not with DBA. DGA seemed to be a good marker of the cis side of the Golgi apparatus and cell membrane. The glycosylation of mucous glycoprotein in rat Brunner's gland was partly clarified electron microscopically.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D008854	Microscopy, Electron	Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.	Electron Microscopy
D002011	Brunner Glands	The abundant submucosal mucous glands in the DUODENUM. These glands secrete BICARBONATE IONS; GLYCOPROTEINS; and PEPSINOGEN II.	Brunner's Gland,Brunner Gland,Brunner's Glands,Brunners Gland,Brunners Glands,Gland, Brunner,Gland, Brunner's,Glands, Brunner,Glands, Brunner's
D004386	Duodenum	The shortest and widest portion of the SMALL INTESTINE adjacent to the PYLORUS of the STOMACH. It is named for having the length equal to about the width of 12 fingers.	Duodenums
D005260	Female		Females
D006001	Glycoconjugates	Carbohydrates covalently linked to a nonsugar moiety (lipids or proteins). The major glycoconjugates are glycoproteins, glycopeptides, peptidoglycans, glycolipids, and lipopolysaccharides. (From Biochemical Nomenclature and Related Documents, 2d ed; From Principles of Biochemistry, 2d ed)	Glycoconjugate
D006651	Histocytochemistry	Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods.	Cytochemistry
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D051381	Rats	The common name for the genus Rattus.	Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus
D037102	Lectins	Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.	Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal