Intracellular localization and binding of technetium-95m in the seastar Marthasterias glacialis

Abstract

The subcellular distribution of technetium was studied using the seastar Marthasterias glacialis which had previously ingested prey labelled with 95mTc either as pertechnetate (VII) or in the reduced state (IV). The majority of the Tc [98% (IV) and 96% (VII)] was taken up and retained in the pyloric caeca, the gland responsible for digestive and food storage processes. Differential centrifugation and separation techniques have demonstrated that, at the subcellular level, technetium in the pyloric caeca was largely associated with the lysosomes. 95mTc (IV) was distributed between the lysosomes and the soluble fraction to roughly the same degree, whereas pertechnetate was more strongly associated with the lysosomal fraction. Chromatography of the cytosol by gel filtration indicated the presence of two distinct protein compounds which were responsible for binding virtually all of the technetium in the soluble fraction. Technetium had a greater relative affinity for the low molecular weight compound, more so for Tc (VII) than for Tc (IV). This anionic protein had an apparent molecular weight of approximately 10 000, and thus may play a role in metal detoxification mechanisms at the cellular level.