Biomaterial Database

Multi-antennary Gal beta1-->4GlcNAc and Gal beta1-->3GalNAc clusters as important ligands for a lectin isolated from the sponge Geodia cydonium. 1998

J H Wu, and S C Song, and Y Y Chen, and M C Tsai, and E A Kabat, and A M Wu

Glyco-Immunochemistry Research Laboratory, Institute of Molecular and Cellular Biology, Chang-Gung Medical College, Tao-yuan, Taiwan.

The affinity of a lectin from the sponge Geodia cydonium (GCL-I) for multi-antennary Gal beta1-->4GlcNAc and Gal beta1-->3GalNAc ligands was studied by both the biotin/avidin-based microtiter plate lectin binding assay and the inhibition of lectin-glycoform interaction. Among the glycoforms tested for binding, GCL-I reacted strongly with three multi-antennary Gal beta1-->4GlcNAc clusters containing glycoproteins (asialo human and bovine alpha1-acid gps and asialo fetuin), T (Gal beta1-->3GalNAc) rich glycoprotein from porcine salivary gland, asialo bird nest gp, and human blood group A active cyst gp, while human and bovine alpha1-acid gps, fetuin, and Tn containing gps were inactive. Among the haptens tested for inhibition, tri-antennary Gal beta1-->4GlcNAc (Tri-II) was about 1500, 72, and 72 times more active than GalNAc, Gal beta1-->4GlcNAc (II), and Gal beta1-->3GalNAc (T), respectively. Based on the present and previous results, it is proposed that tri-antennary Gal beta1-->4GlcNAc and Gal beta1-->3GalNAc clusters, in addition to GalNAc alpha1-->3GalNAc and GalNAc alpha1-->3Gal, are also important ligands for binding; and sialic acid of glycoprotein does interfere with binding.

UI	MeSH Term	Description	Entries
D008024	Ligands	A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)	Ligand
D011161	Porifera	The phylum of sponges which are sessile, suspension-feeding, multicellular animals that utilize flagellated cells called choanocytes to circulate water. Most are hermaphroditic. They are probably an early evolutionary side branch that gave rise to no other group of animals. Except for about 150 freshwater species, sponges are marine animals. They are a source of ALKALOIDS; STEROLS; and other complex molecules useful in medicine and biological research.	Demospongiae,Sponges (Zoology),Sponge (Zoology),Sponges,Poriferas,Sponge
D002417	Cattle	Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.	Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D004187	Disaccharides	Oligosaccharides containing two monosaccharide units linked by a glycosidic bond.	Disaccharide
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
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
D014312	Trisaccharides	Oligosaccharides containing three monosaccharide units linked by glycosidic bonds.	Trisaccharide
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