Effect of modification of membrane saccharides on hormonal imprinting in Tetrahymena. 1987

P Kovács, and G Csaba, and Z Darvas, and G Liszkay

Concanavalin-A (Con-A) competes with insulin for the insulin binding sites of the receptor, an event resulting in overlapping bonds. If the saccharide components of the receptor are subjected to periodate treatment the binding of insulin decreases and so does the imprinting evoked by it. Simultaneously, the binding of Con-A increase immediately after the treatment and 24 hours following the insulin imprinting. This phenomenon indicates that though the two ligands (i.e. insulin and Con-A) overlap on the intact receptor, alterations in the saccharide component influence their binding though not in the same manner and not in the same direction. Periodate treatment, similarly as observed in mammalian lymphocyte cultures, enhanced the division of Tetrahymenas and the peak of Con-A binding occurred parallel to the peak of division after periodate treatment of equal duration. Periodate treatment disturbed not only the binding of Con-A but that of other lectins as well. It has been concluded that hormonal imprinting requires a physiological condition of the membrane and any disturbance of the membrane will lead to a decrease in the efficacy of imprinting.

UI MeSH Term Description Entries
D010504 Periodic Acid A strong oxidizing agent. Paraperiodic Acid,Periodic Acid (HIO4),Periodic Acids,Acid, Paraperiodic,Acid, Periodic,Acids, Periodic
D011972 Receptor, Insulin A cell surface receptor for INSULIN. It comprises a tetramer of two alpha and two beta subunits which are derived from cleavage of a single precursor protein. The receptor contains an intrinsic TYROSINE KINASE domain that is located within the beta subunit. Activation of the receptor by INSULIN results in numerous metabolic changes including increased uptake of GLUCOSE into the liver, muscle, and ADIPOSE TISSUE. Insulin Receptor,Insulin Receptor Protein-Tyrosine Kinase,Insulin Receptor alpha Subunit,Insulin Receptor beta Subunit,Insulin Receptor alpha Chain,Insulin Receptor beta Chain,Insulin-Dependent Tyrosine Protein Kinase,Receptors, Insulin,Insulin Receptor Protein Tyrosine Kinase,Insulin Receptors
D002241 Carbohydrates A class of organic compounds composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n. The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrate
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D013769 Tetrahymena pyriformis A species of ciliate protozoa used extensively in genetic research. Tetrahymena pyriformi,pyriformi, Tetrahymena
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

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