Influence of imprinting with A and B chains of insulin on binding and functional changes in tetrahymena.
Insulin and its A and B chain increased the quantity of intracellular PAS-positive material (glycogen) in tetrahymena, whereas the combined A + B chains decreased it. Imprinting--previous interaction--with insulin, its A and B chains in themselves and with the A + B chain increased the hormone binding capacity of tetrahymena, but the functional effect of imprinting (storage or breakdown of glycogen) showed a different tendency with insulin and A + B chain on the one hand, and A chain and B chain on the other. Since the imprinting potential of a molecule promotes the induction of receptor formation, the fact remains that both component chains of insulin were able to act as potential imprinters, although the A chain was superior to the B chain in this respect throughout, and combined treatment with the A + B chain ultimately induced the formation of a similar binding site as insulin itself.
Csaba
G
G
Department of Biology, Semmelweis University of Medicine, Hungary.
Kovács
P
P
D000818:Animals; D016650:Fluorescein-5-isothiocyanate / Q000031:analogs & derivatives*; D005786:Gene Expression Regulation / Q000187:drug effects*; D006003:Glycogen / Q000096:biosynthesis; D007328:Insulin / Q000031:analogs & derivatives; D049528:Insulin, Long-Acting / Q000494:pharmacology*; D010503:Periodic Acid-Schiff Reaction; D011972:Receptor, Insulin / Q000096:biosynthesis*; D013769:Tetrahymena pyriformis / Q000187:drug effects* / Q000502:physiology
D007328:Insulin; D049528:Insulin, Long-Acting; C031573:insulin, fluorescein-isothiocyanated-; D006003:Glycogen; D011972:Receptor, Insulin; D016650:Fluorescein-5-isothiocyanate