Schistosoma mansoni possesses two isoforms of the iron storage protein ferritin, Fer1 and Fer2. At the mRNA level as well as at the protein level, Fer1 is much more abundant than Fer2; females contain an about 15-fold excess of Fer1 compared with males. In contrast, nearly equal amounts of Fer2 occur in both sexes. By electron microscopy we identified ferritin as a component of electron dense membrane-bound bodies in cells of the vitellarium. The mode of formation of these inclusions (as inferred from electron microscopy) and the abundance of phospholipid multilayered membranes suggest that these bodies are of a lysosomal nature. Here we interpret these ferritin-containing inclusions as protein yolk platelets. To date, most of the literature does not contain any hints of the existence of protein yolk in trematodes. The possible function of ferritin in embryonic development is discussed.

Schistosomu mansoni possesses two isoforms of ferritin, soma and yolk ferritin. The soma ferritin occurs at a low level in most cells of both genders, whereas the yolk ferritin is a female-specific gene product that is expressed at high level in the vitellarium. In higher animals, ferritin mRNA is regulated by iron via the interaction of cytoplasmic binding proteins (IRPs) with a specific sequence element in the 5' untranslated region (UTR) referred to as the iron-responsive element (IRE). Sequence studies of the 5' UTRs, gel retardation assays, and hybridization experiments show that neither ferritin mRNAs of S. rnansoni is regulated by an IRE/IRP mechanism. It is suggested that ferritins in schistosomes are controlled only at the transcriptional level.