High impact information on ferritin

• When rat liver nuclei that had been incubated with ferritin-labeled WGA were examined by electron microscopy, multiple molecules of WGA were found bound to the cytoplasmic face of each nuclear pore [1].
• In contrast, estrogen has no effect on actin, ferritin, or poly(A)-binding protein mRNA, all of which encode intracellular proteins [2].
• This report describes an estrogen-inducible ribonuclease activity found in liver polysomes that degrades albumin mRNA 4 times faster in vitro than it degrades ferritin mRNA [3].
• The CE bound greater amounts of ferritin in comparison to the VE and FE, indicating the presence of a basic domain, presumably in the 43-kDa glycoprotein, which is lost upon proteolysis to 41 kDa during the CE----VE conversion [4].
• This approach for enhancing ferritin contrast was demonstrated by NMR microscopy of ferritin-injected Xenopus oocytes, thus showing the feasibility of ferritin detection in a high magnetic field, even in systems with short transverse relaxation [5].

Biological context of ferritin

• Accumulation of ferritin, the iron storage protein, has been linked recently to aging and a number of pathologies [5].
• Single injections of either horseradish peroxidase (HRP), ferritin or fluorescein-conjugated human IgG were injected around the right optic nerve and tadpoles were then sacrificed between 15 min and 48 h [6].

Anatomical context of ferritin

• The distribution of surface immunoglobulin (Ig) determinants on Xenopus laevis splenic lymphocytes after combination with divalent rabbit anti-Ig coupled to ferritin was studied [7].

Associations of ferritin with chemical compounds

• The level of ferritin mRNA in XL2 cells rises 10- to 15-fold following exposure of cells to cadmium or copper [8].
• The tracers used were horseradish peroxidase, iron dextran, ferritin, and thorotrast [9].
• This report now reveals a distant evolutionary relationship between bacterioferritins and ferritins derived by 'Profile Analysis'. Optimum alignment of bacterioferritin and ferritin sequences suggests that key residues of the ferroxidase centres of ferritins are conserved in bacterioferritins [10].
• By means of electron microscopy, sodium dodecyl sulfate-electrophoresis and other methods it has been identified as ferritin [11].
• The main adenosine triphosphate-binding component of amphibian oocytes is ferritin [11].

Other interactions of ferritin

• One of them is the ferritin light chain homologous (LCH), which is reported for the first time in Xenopus and the other is the ferritin heavy chain homologous (HCH) that is first reported in Xenopus GV oocyte [12].

Analytical, diagnostic and therapeutic context of ferritin

• Molecular cloning and expression of ferritin mRNA in heavy metal-poisoned Xenopus laevis cells [8].

References