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Gene Review

ftn-2  -  Protein FTN-2

Caenorhabditis elegans

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Disease relevance of ferritin

  • Those WFSs in HIV-1 mRNA, various ferritin mRNAs and genomic sequences containing let-7 RNA gene were searched by a novel method, ed_scan [1].

High impact information on ferritin

  • This is consistent with the lack of iron-responsive elements in the C. elegans ferritin genes, ftn-1 and ftn-2 [2].
  • Cytosolic aconitase (aco-1), iron regulatory protein, is known to regulate cellular iron concentration by modulating translation of the ferritin mRNA in addition to its enzymatic activity that converts citrate into iso-citrate [3].
  • Our results indicate that the detected WFSs are coincident with known Rev response element in HIV-1 mRNA, iron-responsive elements in ferritin mRNAs and small let-7 RNAs in Caenorhabditis elegans, Caenorhabditis briggsae and Drosophila melanogaster genomic sequences [1].
  • Cationised ferritin was then used to assess whether stress-induction was truly a surface reactive event; binding of cationised ferritin to the nematode surface also resulted in two-fold induction of beta-galactosidase activity [4].
  • A strong electronegative charge was demonstrated on the microvillar surface and basal membrane with ruthenium red and cationic ferritin staining [5].

Biological context of ferritin

  • Since the stronger acidic groups of sulfates or phosphates would not be protonated under the conditions employed in this study, and therefore susceptible to methylation, staining by ferritin is thought to be due to its interaction with carboxyl groups [5].

Anatomical context of ferritin

  • 4. Pretreatment to block sulfate groups followed by ferritin labeling at pH 7.2-7.4 gave a 35% reduction of binding on the cuticle and an 80% reduction in binding on the microvilli [6].

Associations of ferritin with chemical compounds

  • The ionic nature of ferritin binding was demonstrated with poly-L-lysine, a polycation that interacts with anionic groups on the membrane and thus blocks the subsequent binding of ferritin [5].
  • Surface anionic sites of C. elegans were visualized by using cationized ferritin particles, at pH 7.2, and by using colloidal iron hydroxide particles at pH 1 [7].

Other interactions of ferritin


Analytical, diagnostic and therapeutic context of ferritin


  1. Discovering well-ordered folding patterns in nucleotide sequences. Le, S.Y., Chen, J.H., Konings, D., Maizel, J.V. Bioinformatics (2003) [Pubmed]
  2. Cytosolic aconitase and ferritin are regulated by iron in Caenorhabditis elegans. Gourley, B.L., Parker, S.B., Jones, B.J., Zumbrennen, K.B., Leibold, E.A. J. Biol. Chem. (2003) [Pubmed]
  3. Transcriptional regulation and life-span modulation of cytosolic aconitase and ferritin genes in C.elegans. Kim, Y.I., Cho, J.H., Yoo, O.J., Ahnn, J. J. Mol. Biol. (2004) [Pubmed]
  4. Caenorhabditis elegans as a biomonitor for immunological stress in nematodes. Nowell, M.A., De Pomerai, D.I., Pritchard, D.I. Parasite Immunol. (1999) [Pubmed]
  5. Ultrastructural observations on the cell surface of the intestinal epithelium of the nematode, Ascaris suum. Nature of the electronegative charge. Trimble, J.J., Thompson, S.A. Cell Tissue Res. (1980) [Pubmed]
  6. Caenorhabditis elegans: characters of negatively charged groups on the cuticle and intestine. Himmelhoch, S., Zuckerman, B.M. Exp. Parasitol. (1983) [Pubmed]
  7. Cytochemical characterization of the cuticle of Caenorhabditis elegans (Nematoda: Rhabditoidea). Peixoto, C.A., De Souza, W. J. Submicrosc. Cytol. Pathol. (1992) [Pubmed]
  8. O-Crystallin, arginine kinase and ferritin from the octopus lens. Zinovieva, R.D., Piatigorsky, J., Tomarev, S.I. Biochim. Biophys. Acta (1999) [Pubmed]
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