Some properties of thyroidal membrane adenosinetriphosphatase and iodide uptake: effects of basic polyamino acids.
Poly L-lysine, poly L-ornithine, and histone significantly inhibited the iodide uptake by the thyroid slices, as previously reported. These basic polymers diminshed Na, K-ATPase and concomitantly markedly elevated Mg-ATPase activity in the NaI-treated microsomal preparation and the plasma membrane fraction obtained from thyroid. Poly L-glutamic acid, which was noneffetive to the iodide uptake in vitro, did not show such phenomenon. K-dependent p-nitrophenylphosphatase activity which is considered to reflect the terminal step of the reaction sequence of Na, K-ATPase was also inhibited by poly L-lysine. The effects mentioned above of poly L-lysine and other basic polyamino acids on membrane ATPase system were only found in the preparations from thyroid. The inhibitory effect of these reagents on thyroidal iodide uptake was discussed in terms of the change in membrane ATPase activities.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D001693:Biological Transport, Active; D001921:Brain / Q000378:metabolism; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism*; D004789:Enzyme Activation; D006657:Histones / Q000494:pharmacology*; D007454:Iodides / Q000378:metabolism*; D007668:Kidney / Q000378:metabolism; D008274:Magnesium / Q000494:pharmacology; D051379:Mice; D009928:Organ Specificity; D010455:Peptides / Q000494:pharmacology*; D011107:Polylysine / Q000494:pharmacology; D011188:Potassium / Q000494:pharmacology; D051381:Rats; D012964:Sodium / Q000494:pharmacology; D013045:Species Specificity; D013552:Swine; D013961:Thyroid Gland / Q000378:metabolism*
D006657:Histones; D007454:Iodides; D010455:Peptides; D011107:Polylysine; D012964:Sodium; D000251:Adenosine Triphosphatases; D008274:Magnesium; D011188:Potassium