Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:Q86TM3 (cage)
 29,987 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The development of new and effective marker substances has optimized tumor-marker-guided follow-up programs to monitor generalization of disease and to assess the therapeutic outcome. Isoferritins of placental origin were first determined in the serum of patients with lymphoproliferative disease by way of the recently developed monoclonal antibody CMH-9. We have set up an Austro-Israeli working group and analysed 64 patients in terms of the sensitivity of placental ferritin (PLF) compared with the standard markers carcinoembryonic antigen (CEA) and mucinous-like cancer-associated antigen (MCA) in patients with metastatic breast cancer. We have additionally evaluated the importance of combined marker determination. Analysis of the data in view of site of metastatic spread yielded satisfying results both for PLF (sensitivity 70.4%) as well as MCA (sensitivity 76.9%) for visceral metastases; a combination of these two markers revealed a striking sensitivity of 88.4%, which, however, could not be improved by adding the third marker (CEA). With regard to non-visceral metastases, CEA and MCA were clearly superior.
 ...
PMID:Placental isoferritin (PLF) in comparison with MCA and CEA in advanced breast cancer--first data from a pilot study. 177 47

Using tissue cages implanted in rabbits the growth of some strains of group B streptococci and the development of cell surface antigens were analyzed and compared to those under in vitro conditions. Two encapsulated strains grew well in the tissue cage fluid. Their capsules could be heavily labelled by ferritin-conjugated antibody against the type-specific polysaccharide. However, the thickness of the capsule was different to that following cultivation in vitro. In both strains the labelling of the group polysaccharide in the cell wall was sterically hindered by the large capsule. Two strains lacking a capsule did not grow in the tissue cage fluid but were mostly phagocytized. This again demonstrates the importance of the type-specific polysaccharides as significant virulence factors of group B streptococci.
 ...
PMID:Growth of group B streptococci and development of surface antigens in tissue cages implanted in rabbits. 675 17

Chronic anemia associated with cancer often causes poor quality of life and is often exacerbated by intensive treatment. In recent controlled trials, recombinant human erythropoietin (rhEpo) proved to be well tolerated and effective in amelioration and reduction of transfusion requirements of cancer-associated anemia. Double-blind placebo-controlled trials of rhEpo in patients undergoing allogenic, but not autologous, bone marrow transplantation showed significant acceleration of the reconstitution of erythropoiesis. Multivariate analysis revealed that serum erythropoietin levels of 100 mU/mL or greater and an increase in hemoglobin by at least 0.5 g/dL was a probable response; conversely, a serum ferritin level of 400 ng/mL or greater after 2 weeks indicated a poor response to rhEpo therapy. Further studies are needed to define patient populations in whom cost-effective rhEpo therapy is justified.
 ...
PMID:Management of chemotherapy-induced anemia. 757 78

A protein-encaged superparamagnetic iron oxide has been developed and characterized by using horse spleen apoferritin as a novel bioreactive environment. The roughly spherical magnetoferritin molecules, 120 A in diameter, are composed of a monocrystalline maghemite or magnetite core 73 A +/- 14 in diameter. Except for the additional presence of iron-rich molecules of higher molecular weight, the appearance and molecular weight (450 kd) of magnetoferritin are identical to that of natural ferritin; the molecules are externally indistinguishable from their precursor, with a pI (isoelectric point) in the range 4.3-4.6. The measured magnetic moment of the superparamagnetic cores is 13,200 Bohr magnetons per molecule, with T1 and T2 relaxivities (r1 and r2) of 8 and 175 L.mmol-1 (Fe).sec-1, respectively, at body temperature and clinical field strengths. The unusually high r2/r1 ratio of 22 is thought to arise from ideal core composition, with no evidence of crystalline paramagnetic inclusions. T2 relaxation enhancement can be well correlated to the field-dependent molecular magnetization, as given by the Langevin magnetization function, raised to a power in the range 1.4-1.6. With its nanodimensional biomimetic protein cage as a rigid, convenient matrix for complexing a plethora of bioactive substances, magnetoferritin may provide a novel template for specific targeting of selected cellular sites.
 ...
PMID:Magnetoferritin: characterization of a novel superparamagnetic MR contrast agent. 780 66

A multimeric protein that behaves functionally as an authentic ferritin has been isolated from the Gram-positive bacterium Listeria innocua. The purified protein has a molecular mass of about 240,000 Da and is composed of a single type of subunit (18,000 Da). L. innocua ferritin is able to oxidize and sequester about 500 iron atoms inside the protein cage. The primary structure reveals a high similarity to the DNA-binding proteins designated Dps. Among the proven ferritins, the most similar sequences are those of mammalian L chains that appear to share with L. innocua ferritin the negatively charged amino acids corresponding to the iron nucleation site. In L. innocua ferritin, an additional aspartyl residue may provide a strong complexing capacity that renders the iron oxidation and incorporation processes extremely efficient. This study provides the first experimental evidence for the existence of a non-heme bacterial ferritin that is related to Dps proteins, a finding that lends support to the recent suggestion of a common evolutionary origin of these two protein families.
 ...
PMID:A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua. 901 63

Ferritin is a protein of 24 subunits which assemble into a shell with 432 point symmetry. It can be denatured reversibly in acidic guanidine hydrochloride, with the formation of poorly populated renaturation intermediates. In order to increase the accumulation of intermediates and to study the mechanism of ferritin renaturation, we analysed variants of the human ferritin H-chain altered at the N-terminus (delta(1-13)), near the 4-fold axis (Leu-169 --> Arg), the 3-fold axis (Asp-131 --> Ile + Glu-134 --> Phe) or the 2-fold axis (Ile-85 --> Cys). We also carried out specific chemical modifications of Cys-130 (near the 3-fold axis) and Cys-85 (near the 2-fold axis). Renaturation of the modified ferritins yielded assembly intermediates that differed in size and physical properties. Alterations of residues around the 2-, 4- and 3-fold axes produced subunit monomers, dimers and higher oligomers respectively. All these intermediates could be induced to assemble into ferritin 24-mers by concentrating them or by co-renaturing them with wild-type H-ferritin. The results support the hypothesis that the symmetric subunit dimers are the building blocks of ferritin assembly, and are consistent with a reassembly pathway involving the coalescence of dimers, probably around the 4-fold axis, followed by stepwise addition of dimers until the 24-mer cage is completed. In addition they show that assembly interactions are responsible for the large hysteresis of folding and unfolding plots. The implications of the studies for in vivo heteropolymer formation in vertebrates, which have two types of ferritin chain (H and L), are discussed.
 ...
PMID:Effects of modifications near the 2-, 3- and 4-fold symmetry axes on human ferritin renaturation. 906 64

Ferritin is characterized by a highly conserved architecture that comprises 24 subunits assembled into a spherical cage with 432 symmetry. The only known exception is the dodecameric ferritin from Listeria innocua. The structure of Listeria ferritin has been determined to a resolution of 2.35 A by molecular replacement, using as a search model the structure of Dps from Escherichia coli. The Listeria 12-mer is endowed with 23 symmetry and displays the functionally relevant structural features of the ferritin 24-mer, namely the negatively charged channels along the three-fold symmetry axes that serve for iron entry into the cavity and a negatively charged internal cavity for iron deposition. The electron density map shows 12 iron ions on the inner surface of the hollow core, at the interface between monomers related by two-fold axes. Analysis of the nature and stereochemistry of the iron-binding ligands reveals strong similarities with known ferroxidase sites. The L. innocua ferritin site, however, is the first described so far that has ligands belonging to two different subunits and is not contained within a four-helix bundle.
 ...
PMID:The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site. 1062 25

We performed a comparative study of iliac bone graft (the iliac bone group) and carbon cage with local bone graft (the cage group) in PLIF to evaluate the clinical results of both methods. We examined both groups about the operating time, the estimated blood loss, the operative results using the score rating system of Japanese Orthopaedic Association (JOA score), and the presence of bone union on radiography. The operating time and the estimated blood loss of the cage group were statistically less than those of the iliac bone group. There were no significant differences between both groups about the operative results. The radiographic evaluation on bone union showed that half of the iliac bone group had collapsed union, but all cases of the cage group revealed union without collapse.
 ...
PMID:Comparative study of iliac bone graft and carbon cage with local bone graft in posterior lumbar interbody fusion. 1240 14

The iron-storage protein ferritin encapsulates a nanoparticle of iron oxide. The size and properties of these nanoparticles can be adjusted by controlled oxidative hydrolysis reactions of Fe(II). This mineralized ferritin protein cage has previously been shown to act as an effective photocatalyst for reduction of Cr(VI). In the present work, we demonstrate that Fe(O)OH-mineralized ferritin catalyzes the photoreduction of Cu(II) to form a stable, air-sensitive, colloidal dispersion of Cu(0). In addition, the particle sizes of the Cu colloids can be controlled by varying the ratio of Cu(II) to ferritin. This illustrates an important principle, namely that the properties of one preformed material can be utilized for the specific synthesis of a second material, thus tailoring the desired physical properties of the final products. This procedure represents a multistep materials synthesis: the formation of a new nanomaterial from a catalytic precursor.
 ...
PMID:Photocatalytic synthesis of copper colloids from CuII by the ferrihydrite core of ferritin. 1515 6

Ferritin, a major form of endogenous iron in food legumes such as soybeans, is a novel and natural alternative for iron supplementation strategies where effectiveness is limited by acceptability, cost, or undesirable side effects. A member of the nonheme iron group of dietary iron sources, ferritin is a complex with Fe3+ iron in a mineral (thousands of iron atoms inside a protein cage) protected from complexation. Ferritin illustrates the wide range of chemical and biological properties among nonheme iron sources. The wide range of nonheme iron receptors matched to the structure of the iron complexes that occurs in microorganisms may, by analogy, exist in humans. An understanding of the chemistry and biology of each type of dietary iron source (ferritin, heme, Fe2+ ion, etc.), and of the interactions dependent on food sources, genes, and gender, is required to design diets that will eradicate global iron deficiency in the twenty-first century.
 ...
PMID:Iron, ferritin, and nutrition. 1518 24


1 2 3 4 5 6 7 8 9 10 Next >>