Calcineurin (CN) exhibits a bimodal regulation by different concentrations of vanadyl ions (VO[2+]) in the presence of Mn[2+]. Low concentrations of VO[2+] inhibit the enzyme, with 50[] VO[2+] completely inhibiting CN activity, while high concentrations, up to 500[] VO[2+], stimulate the CN activity. A similar bimodal regulation of CN was not observed with either calcium or vanadate under the same conditions. Xband electron spin resonance spectroscopy, used to study the binding of VO[2+] to the catalytic subunit A of calcineurin, show that there are two kinds of binding sites in the A subunit.
Print ISSN: 1431-6730
Volume: 381, 04/2000
Pages: 309 - 312