Biomaterial Database

Development of Dolichos biflorus agglutinin (DBA) binding sites in the bile duct of the embryonic mouse liver. 1988

N Shiojiri, and H Katayama

Biological Institute, Faculty of Science, Shizuoka University, Japan.

The distribution of binding sites for Dolichos biflorus agglutinin (DBA) was studied by histochemical staining in the embryonic mouse liver. The liver primordium consists of cranial and caudal diverticula. DBA bound to the pseudostratified endodermal cells of the caudal hepatic diverticulum, and also to some endodermal cells of the cranial one. Most extrahepatic bile duct cells and all epithelial cells of the gall bladder were consistently DBA-positive. In intrahepatic bile ducts and their precursors, the DBA binding sites showed a patchy distribution. Most hepatocytes were DBA-negative, though some young hepatocytes were DBA-positive. The results suggest that DBA binding sites are useful markers of epithelial cells of the gall bladder and the bile ducts, especially the extrahepatic bile duct. Differentiation of bile duct cells was also discussed with special reference to the developmental change of the distribution of the DBA binding sites.

UI	MeSH Term	Description	Entries
D008099	Liver	A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.	Livers
D008809	Mice, Inbred C3H	An inbred strain of mouse that is used as a general purpose strain in a wide variety of RESEARCH areas including CANCER; INFECTIOUS DISEASES; sensorineural, and cardiovascular biology research.	Mice, C3H,Mouse, C3H,Mouse, Inbred C3H,C3H Mice,C3H Mice, Inbred,C3H Mouse,C3H Mouse, Inbred,Inbred C3H Mice,Inbred C3H Mouse
D011975	Receptors, Mitogen	Glycoprotein molecules on the surface of B- and T-lymphocytes, that react with molecules of antilymphocyte sera, lectins, and other agents which induce blast transformation of lymphocytes.	Lectin Receptors,Mitogen Receptors,Receptors, Lectin,Mitogen Receptor,Receptor, Mitogen
D004707	Endoderm	The inner of the three germ layers of an embryo.	Definitive Endoderm,Definitive Endoderms,Endoderm, Definitive,Endoderms
D005704	Gallbladder	A storage reservoir for BILE secretion. Gallbladder allows the delivery of bile acids at a high concentration and in a controlled manner, via the CYSTIC DUCT to the DUODENUM, for degradation of dietary lipid.	Gallbladders
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
D001652	Bile Ducts	The channels that collect and transport the bile secretion from the BILE CANALICULI, the smallest branch of the BILIARY TRACT in the LIVER, through the bile ductules, the bile ducts out the liver, and to the GALLBLADDER for storage.	Bile Duct,Duct, Bile,Ducts, Bile
D051379	Mice	The common name for the genus Mus.	Mice, House,Mus,Mus musculus,Mice, Laboratory,Mouse,Mouse, House,Mouse, Laboratory,Mouse, Swiss,Mus domesticus,Mus musculus domesticus,Swiss Mice,House Mice,House Mouse,Laboratory Mice,Laboratory Mouse,Mice, Swiss,Swiss Mouse,domesticus, Mus musculus
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
D037121	Plant Lectins	Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.	Lectins, Plant,Phytagglutinin,Plant Agglutinin,Plant Lectin,Agglutinins, Plant,Phytagglutinins,Plant Agglutinins,Agglutinin, Plant,Lectin, Plant