Ferritin mRNAs in <i>Schistosoma Mansoni</i> do not have Iron‐Responsive Elements for Post‐Transcriptional Regulation

Schüssler, P; Pötters, Elke; Winnen, Ralf; Michel, Anja; Bottke, Werner; Kunz, Werner

doi:10.1111/j.1432-1033.1996.0064t.x

Cited by 20 publications

(14 citation statements)

References 36 publications

(38 reference statements)

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“…The only metazoan species where we failed to identify an IRE were Caenorhabditis elegans and Schistosoma mansoni, consistent with previous observations (Schussler et al 1996;Gourley et al 2003). We were not able to find IREs in organisms outside the metazoan group.…”

Section: Ferritinsupporting

confidence: 80%

Evolution of the iron-responsive element

Piccinelli¹,

Samuelsson²

2007

RNA

150

153

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An RNA hairpin structure referred to as the iron-responsive element (IRE) and iron regulatory proteins (IRPs) are key players in the control of iron metabolism in animal cells. They regulate translation initiation or mRNA stability, and the IRE is found in a variety of mRNAs, such as those encoding ferritin, transferrin receptor (Tfr), erythroid aminolevulinic acid synthase (eALAS), mitochondrial aconitase (mACO), ferroportin, and divalent metal transporter 1 (DMT1). We have studied the evolution of the IRE by considering all mRNAs previously known to be associated with this structure and by computationally examining its occurrence in a large variety of eukaryotic organisms. More than 100 novel sequences together with ;50 IREs that were previously reported resulted in a comprehensive view of the phylogenetic distribution of this element. A comparison of the different mRNAs shows that the IREs of eALAS and mACO are found in chordates, those of ferroportin and Tfr1 are found in vertebrates, and the IRE of DMT1 is confined to mammals. In contrast, the IRE of ferritin occurs in a majority of metazoa including lower metazoa such as sponges and Nematostella (sea anemone). These findings suggest that the ferritin IRE represents the ancestral version of this type of translational control and that during the evolution of higher animals the IRE structure was adopted by other genes. On the basis of primary sequence comparison between different organisms, we suggest that some of these IREs developed by ''convergent evolution'' through stepwise changes in sequence, rather than by recombination events.

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Section: Ferritinsupporting

confidence: 80%

Evolution of the iron-responsive element

Piccinelli¹,

Samuelsson²

2007

RNA

150

153

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“…Sequence analysis showed that Hlfer2 mRNA lacks an IRE, similar to the secretory ferritin of I. ricinus (Hajdusek et al, 2009), the yolk ferritin of L. stagnalis (von Darl et al, 1994), S. mansoni ferritins (Schüssler et al, 1996) and Haliotis discus discus Abf1 (De Zoysa and Lee, 2007). In contrast to HlFER1, HlFER2 contains a signal peptide and was detected in the hemolymph using a specific antiserum.…”

Section: Discussionmentioning

confidence: 99%

Multiple ferritins are vital to successful blood feeding and reproduction of the hard tick Haemaphysalis longicornis

Galay

Aung

Umemiya‐Shirafuji

et al. 2013

Journal of Experimental Biology

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SUMMARYTicks are obligate hematophagous parasites and important vectors of diseases. The large amount of blood they consume contains great quantities of iron, an essential but also toxic element. The function of ferritin, an iron storage protein, and iron metabolism in ticks need to be further elucidated. Here, we investigated the function a newly identified secreted ferritin from the hard tick Haemaphysalis longicornis (HlFER2), together with the previously identified intracellular ferritin (HlFER1). Recombinant ferritins, expressed in Escherichia coli, were used for anti-serum preparation and were also assayed for iron-binding activity. RT-PCR and western blot analyses of different organs and developmental stages of the tick during blood feeding were performed. The localization of ferritins in different organs was demonstrated through an indirect immunofluorescent antibody test. RNA interference (RNAi) was performed to evaluate the importance of ferritin in blood feeding and reproduction of ticks. The midgut was also examined after RNAi using light and transmission electron microscopy. RT-PCR showed differences in gene expression in some organs and developmental stages. Interestingly, only HlFER2 was detected in the ovary during oviposition and in the egg despite the low mRNA transcript. RNAi induced a reduction in post-blood meal body weight, high mortality and decreased fecundity. The expression of vitellogenin genes was affected by silencing of ferritin. Abnormalities in digestive cells, including disrupted microvilli, and alteration of digestive activity were also observed. Taken altogether, our results show that the iron storage and protective functions of ferritin are crucial to successful blood feeding and reproduction of H. longicornis. Supplementary material available online at

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“…Instead, transcriptional regulation of ferritin is most frequently (although not universally) identified as a primary mode of response to exogenous iron as well as stress-related signals. [65][66][67][68][69][70][71][72] …”

Section: Ferritin Genes and Mutationsmentioning

confidence: 99%