Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ferritin, the iron-storage protein, binds porphyrins, metalloporphyrins and the fluorescent dyes ANS (8-anilino-1-naphthalenesulfonic acid) and TNS (2-p-toluidinyl-6-naphthalenesulfonic acid), similarly to apo-myoglobin. Octahedral crystals of horse-spleen apo-ferritin (HSF; 174 amino acids) complexes prepared by the addition of haem, hematoporphyrin or Sn-protoporphyrin IX to a solution of apo-ferritin crystallize in space group F432 with cell parameter a = 184.0 A. X-ray crystallographic analysis of single crystals prepared from a mixture containing haem or Sn-protoporphyrin IX shows that the haem-binding sites in these crystals are occupied by protoporphyrin IX, which is free of metal, rather than by the original metalloporphyrin. The present paper describes the structure of horse-spleen apo-ferritin cocrystallized with Sn-protoporphyrin IX. The 6797 reflections up to 2.6 A resolution used in the refinement were obtained from a data set recorded on a Nicolet/Xentronics area detector with Cu Kalpha radiation from a Rigaku RU 200 rotating anode. The final structure comprises 1613 non-H atoms, two Cd atoms and 170 solvent molecules. Four residues are described as disordered. The root-mean-square deviations from ideal bond lengths and angles are 0.013 A and 2.88 degrees, respectively. Protoporphyrins are observed in special positions on the twofold axes of the ferritin molecule with a stoichiometry of 0.4 per subunit.
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PMID:A crystallographic study of haem binding to ferritin. 1529 70

The effects of ascorbic acid (AA), phytate and tannic acid (TA) on Fe bioavailability from Fe supplied as reconstituted ferritin were compared with FeSO4 using an in vitro digestion-Caco-2 cell model. Horse spleen apoferritin was chemically reconstituted into an animal-type ferritin (HSF) and a plant-type ferritin (P-HSF) according to the typical ratios of Fe:P found in these molecules. In the presence of AA (Fe:AA molar ratio of 1:20), significantly more Fe was absorbed from FeSO4 (about 303 %), HSF (about 454 %) and P-HSF (about 371 %) when compared with ferrous sulfate or ferritin without AA. Phytic acid (PA; Fe:PA molar ratio of 1:20) significantly reduced Fe bioavailability from FeSO4 (about 86 %), HSF (about 82 %) and P-HSF (about 93 %) relative to FeSO4 and the ferritin controls. Treatment with TA (Fe:TA molar ratio of 1:1) significantly decreased Fe bioavailability (about 97 %) from both FeSO4 and the ferritin samples. AA was able to partially reverse the negative effect of PA (Fe:PA:AA molar ratio of 1:20:20) on Fe bioavailability but did not reverse the inhibiting effect of TA (Fe:TA:AA molar ratio of 1:1:20) on Fe bioavailability from ferritin and FeSO4. Overall, there were no significant differences in bioavailable Fe between P-HSF, HSF or FeSO4. Furthermore, the addition of AA (a known promoter) or the inhibitors, PA and TA, or both, did not result in significant differences in bioavailable Fe from ferritin relative to FeSO4. The results suggest that Fe in the reconstituted ferritin molecule is easily released during in vitro digestion and interacts with known promoters and inhibitors.
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PMID:Effects of ascorbic acid, phytic acid and tannic acid on iron bioavailability from reconstituted ferritin measured by an in vitro digestion-Caco-2 cell model. 1875 51

Proanthocyanidins (PAs) possess superior antioxidant properties and nutritious value, however, low bioavailability and stability limit their applications. Here, we developed a novel method to encapsulate PA dimers successfully into horse spleen apoferritin (apoHSF) using a disassembly/reassembly method based on pH change. The PA-HSF nanoparticles were characterized using fluorescence spectroscopy, transmission electron microscopy, circular dichroism, and high-performance liquid chromatography. One apoferritin cage could approximately encapsulate 25.6 molecules of the PA dimer. The results showed that the encapsulation of the PA dimers protected it from the damage of oxidants and temperature below room temperature would be an appropriate condition for HSF-578 solution storage. Moreover, HepG2 cell monolayer absorption and adhesion analyses indicated that the PA dimers encapsulated within apoHSF cages were more efficient in transport. In addition, it was indicated that the PA-HSF nanoparticles had higher cellular antioxidant activity. The novel strategy provided in this study indicates that the protein cage structures like ferritin have potential to be applied in the field of food nutrition.
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PMID:Proanthocyanidin Encapsulated in Ferritin Enhances Its Cellular Absorption and Antioxidant Activity. 3154 55