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PubMed1992

The effect of different iron compounds on transferrin receptor expression in term human cytotrophoblast cells.

During pregnancy, the mother is faced with an increased food demand. A good example of this increased demand is iron (Fe). Fe is needed in all growing cells. During pregnancy, the Fe transport to the fetus increases enormously. This amount can easily induce an Fe deficiency in the mother. Fe supplementation is very important for her, but not for the Fe status of the fetus, which is protected against Fe toxicity as well as deficiency. The placenta seems to be autonomous in Fe uptake. Likely there is a regulation mechanism. The human placenta is hemomonochorial. The cell layer of the fetus in contact with the maternal blood is formed by syncytiotrophoblasts. Fe is transported to the placenta by transferrin. Transferrin binds to a transferrin receptor on the trophoblast membrane and is internalized via an endocytic pathway. During this cycle, Fe is released from transferrin and the transferrin-transferrin receptor complex is recycled to the membrane. Isolated trophoblast cells from term placentas form a syncytium in vitro, and transferrin receptors are expressed. Expression depends on the number of cells in culture, culture time, the amount of Fe available, and the Fe compound. By regulation of the number of transferrin receptors, trophoblasts are able to control their Fe uptake.

Binding Sites↗
PubMed1992

Structural studies of oxygen-bridged iron compounds.

Compound (I): cis-dichloro[mu-[bis[mu-[[2,6-diacetylpyridine dioximato](2-)-O:O']]dihydroxodiphenyl-diborato](3-)]- mu- mithoxydiiron, [Fe2(C30H29B2N6-O6)Cl2(CH3O)], M(r) = 804.9, monoclinic, Cc, a = 21.228 (6), b = 8.020 (2), c = 20.865 (5) A, beta = 105.2 (1) degrees, V = 3428 (2) A3, Z = 4, Dx = 1.56 g cm-3, lambda(Mo K alpha) = 0.7107 A, mu = 10.6 cm-1, F(000) = 1648, T = 275 K, R = 0.055 for 3018 unique reflections. Compound (I) contains a pseudo-twofold axis relating the two pyridine dioxime groups bound to the Fe atoms. In addition, two O atoms from the phenylborate moieties bridge the iron atoms, as does a methoxide. The two Cl atoms are bound to the seven coordinate metals axial to the methoxide. Compound (II): cis-dichloro[mu-[bis[mu-[[2,6-diacetylpyridine dioximato](2-)-O:O']]dihydroxodiphenyldiborato](3-)]-mu- hydroxodiiron, [Fe2(C30H29B2N6-O6)Cl2(OH)].H2O.2C2H3N, M(r) = 891.0, monoclinic, P2(1)/n, a = 11.860 (2), b = 20.911 (5), c = 16.175 (3) A, beta = 92.88 (1) degrees, V = 4006 (3) A3, Z = 4, Dx = 1.48 g cm-3, lambda(Mo K alpha) = 0.7107 A, mu = 9.1 cm-1, F(000) = 1832, T = 275 K, R = 0.051 for 7034 unique reflections. Compound (II) contains a hydroxide group replacing the methoxide in compound (I). The crystals also contain two acetonitriles of solvation. The bond lengths in the complex and the hydrogen-bonding pattern in the crystals are consistent with one of the bridging borate O atoms being protonated.(ABSTRACT TRUNCATED AT 250 WORDS)

Bridged-Ring Compounds↗
PubMed1990

Induction of ferritin synthesis in vitro: problems of specificity inherent in the use of iron compounds.

The potential importance of heme as a translational regulator has been recognized for nearly 30 years. However, the ability to distinguish the specific regulatory effects of heme from the nonspecific effects has been hampered by its high reactivity and its tendency to generate reactive by-products in most systems. In this article we discuss some of the technical difficulties in studying the effects of iron salts and compounds, notably heme, in biochemical systems in vitro. Data are presented which show that the nonspecific inhibitory effects of heme on two restriction endonucleases can be eliminated by (a) including a redox buffer in the reaction mixture, and (b) maintaining a sufficiently high total protein concentration. Under these conditions, the specific effects of hemin on the ferritin repressor protein are still observed. A possible relationship between these observations and the status of 'free' heme in vivo is considered.

Deoxyribonuclease BamHI↗
PubMed1975

The influence of oral administered iron compounds on the intestinal absorption of immunoglobulin-G in newborn piglets.

The intestinal absorption of IgG from colostrum in newborn piglets was not disturbed by oral administration of iron preparations used for prophylactic treatment of anaemia in piglets. Iron dextran, ferrous fumarate or a combination of these compounds were administered simultaneously with the colostrum supply, soon after birth and the concentrations of IgG in serum were determined.

Administration, Oral↗
PubMed2002

Towards evidence based emergency medicine: best BETs from the Manchester Royal Infirmary. Activated charcoal and gastric absorption of iron compounds.

A short cut review was carried out to establish whether activated charcoal is effective in iron overdose. Altogether 17 papers were found using the reported search, of which only one was relevant. The author, date and country of publication, patient group studied, study type, relevant outcomes, results and study weaknesses of this paper are shown in table 4. A clinical bottom line is stated.

Adult↗
PubMed2000

Injection of iron compounds followed by induction of the stress response causes tissue injury and apoptosis.

To determine whether iron-laden tissue subsequently stimulated to produce the stress ("heat shock") response-sustained injury, hindlimbs of male ND4 mice were injected with iron salts, hemin, or hemoglobin. The stress response was induced with sodium arsenite or with heat. Ulcers appeared at the injection site. Tissues were analyzed by three distinct techniques-electron microscopy, TUNEL stain, and agarose gel electrophoresis of low molecular weight DNA-which collectively suggest that the tissue injury is, at least in part, the consequence of accelerated apoptosis. The data suggest that the toxicity of free iron is amplified by induction of the stress (heat shock) response to signal a programmed response. This model and mechanism may have implications in pathological processes ranging from the cutaneous wounds of venous stasis disease to the tissue failure of multiple organ dysfunction.

Animals↗
PubMed1984

[Characteristics of the chemiluminescence of the system containing H202 in the presence of iron compounds].

The relative effectiveness of radical formation by different concentrations of hemoglobin, hemin and Fe2+ in the reaction with H2O2 evaluated by the intensity of chemiluminescence was studied. Hemoglobin was shown to be remarkably effective at the concentrations close to those in blood plasma. It is suggested that exoerythrocyte hemoglobin and the products of its destruction up to hemin are the most effective prooxidants and potential centers of radical formation in the blood.

Ferrous Compounds↗
PubMed1995

Effect of concentration of compounds containing iron on the growth of Porphyromonas gingivalis.

We examined the effect of the concentration of various types of iron molecules on the regulation of growth of Porphyromonas gingivalis. Bacterial growth was monitored spectrophotometrically. The hemin-depleted cells of P. gingivalis 381 were incubated in the basal medium plus test substrates such as hemoglobin, hemin, transferrin and various inorganic iron compounds. The relationship between the specific growth rate of organisms and the concentration of iron-containing compounds was determined. The value of Ks, a parameter analogous to the Michaelis-Menten constant, was estimated. P. gingivalis 381 showed a Ks value of 3.85, 4.91 and 0.0017 microM for hemin, transferrin and hemoglobin, respectively. However, the inorganic iron compounds tested did not support growth of P. gingivalis. These findings suggest that P. gingivalis utilizes hemoglobin as an iron source much more effectively than other iron-containing compounds under an iron-limited environment.

Culture Media↗