Biomaterial Database

Effect on inhibitors of glycoprotein synthesis (swainsonine, 1-deoxynojirimycin) on hormonal imprinting and lectin binding in Tetrahymena pyriformis. 1993

P Kovács, and G Csaba

Department of Biology, Semmelweis University Medical School, Budapest, Hungary.

Glycoprotein synthesis inhibitors (swainsonine = SW and 1-deoxynojirimycin = DNJ) influenced the insulin binding, insulin provoked hormonal imprinting and lectin binding of Tetrahymena. Insulin binding was increased and lectin binding decreased by both of them immediately after treatment, however, SW decreased insulin binding and both of them increased lectin binding after 24 h. SW inhibited, DNJ allowed the development of insulin imprinting. This means that the disturbance of glycosylation in general does not influence, but the blocking of mannosidase II disturbs the process of imprinting.

UI	MeSH Term	Description	Entries
D007328	Insulin	A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).	Iletin,Insulin A Chain,Insulin B Chain,Insulin, Regular,Novolin,Sodium Insulin,Soluble Insulin,Chain, Insulin B,Insulin, Sodium,Insulin, Soluble,Regular Insulin
D006023	Glycoproteins	Conjugated protein-carbohydrate compounds including MUCINS; mucoid, and AMYLOID glycoproteins.	C-Glycosylated Proteins,Glycosylated Protein,Glycosylated Proteins,N-Glycosylated Proteins,O-Glycosylated Proteins,Glycoprotein,Neoglycoproteins,Protein, Glycosylated,Proteins, C-Glycosylated,Proteins, Glycosylated,Proteins, N-Glycosylated,Proteins, O-Glycosylated
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
D013769	Tetrahymena pyriformis	A species of ciliate protozoa used extensively in genetic research.	Tetrahymena pyriformi,pyriformi, Tetrahymena
D017026	Swainsonine	An indolizidine alkaloid from the plant Swainsona canescens that is a potent alpha-mannosidase inhibitor. Swainsonine also exhibits antimetastatic, antiproliferative, and immunomodulatory activity.	Swainsonine, (1R-(2 beta,8a alpha))-Isomer,Swainsonine, (2 beta,8a alpha)-Isomer,Swainsonine, (8 alpha)-Isomer,Swainsonine, (8 alpha,8a alpha)-Isomer,Swainsonine, (8a alpha)-Isomer
D017485	1-Deoxynojirimycin	An alpha-glucosidase inhibitor with antiviral action. Derivatives of deoxynojirimycin may have anti-HIV activity.	1,5-Deoxy-1,5-imino-D-mannitol,1-Deoxymannojirimycin,1,5-Dideoxy-1,5-imino-D-mannitol,1-Deoxynojirimycin Hydrochloride,Bay n 5595,Moranoline,1 Deoxymannojirimycin,1 Deoxynojirimycin,1 Deoxynojirimycin Hydrochloride
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