Disease relevance of Ftl1

• In rats with chronic dietary iron overload, a higher amount of liver ferritin L-subunit mRNA was found mainly engaged on polysomes, whereas in control rats ferritin L-subunit mRNA molecules were largely stored in ribonucleoprotein particles [1].

High impact information on Ftl1

• To elucidate the structural features of these mRNAs involved in the translational response to iron, a chimera was constructed from the 5' and 3' untranslated regions (UTRs) of ferritin L subunit mRNA fused to the reading frame of the mRNA of bacterial chloramphenicol acetyltransferase (CAT) [2].
• The rat genome contains approximately 20 copies of the ferritin L-subunit gene, of which we have sequenced seven [3].
• The proteins up-regulated were mostly HSPs (heat-shock proteins) and antioxidative stress proteins, including HSP70, aldose reductase, haem oxygenase-1, HSP27, ferritin light chain and alphaB-crystallin [4].

Anatomical context of Ftl1

• In agreement with previous reports, in rats acutely treated with parenteral iron, only the ferritin L-subunit mRNA increased in amount, whereas both ferritin subunit mRNAs shifted to polysomes [1].

Analytical, diagnostic and therapeutic context of Ftl1

• Sequence analysis of a tryptic peptide from the 24.5-kDa protein revealed its identity with rat ferritin light chain [5].

References