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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two major species of ferritin are found in heart and other muscles of the rat, which may be separated in polyacrylamide gel electrophoresis after preliminary purification. We have examined the time-course of incorporation of [3H]leucine and 59Fe into these slow- and fast-migrating ferritins in heart and diaphragm, in vivo, following intraperitoneal or intravenous injection. The results show: 1. Both species of ferritin are synthesized from amino acids in parallel with total tissue protein and receive iron in concert; consequently, there is no structural precursor/product or iron-donor/receiver relationship between them. 2. Under iron stimulation, both ferritins are synthesized at different rates within the same tissue and between tissues, and there is a correlation between tissue concentration and its rate of synthesis. In the diaphragm, the concentration and rate of synthesis of the slow-migrating species predominate, and in the heart the opposite pertains. 3. In both tissues iron is preferentially absorbed by the first species upon entry into the tissue, and this is independent of the relative concentration of the two ferritins or their iron saturation. 4. From the data on 59Fe uptake it appears that myoglobin synthesis and metabolism are considerably more active in the heart than in the diaphragm. However, neither ferritin species is a direct iron donor for myoglobin synthesis. Instead, the ferritins and myoglobin all draw their iron from a common pool, which may be of the small molecular weight type reported for intestinal epithelium and some other cells.
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PMID:Synthesis of rat muscle ferritins and function in iron metabolism of heart and diaphragm. 744 5

Numerous mechanisms have been invoked to explain the cardiotoxicity of Adriamycin, most of which share a requirement for iron. Adriamycin is chemically reactive with iron loosely associated with subcellular membranes as well as with ferritin and the heme iron of hemoglobin. The present investigation examined whether Adriamycin also reacts with myoglobin, an abundant source of iron in cardiac muscle. Adriamycin caused a 4-fold stimulation of the autoxidation of oxymyoglobin to metmyoglobin. Hydrogen peroxide is an obligatory intermediate as catalase completely inhibited the reaction. Superoxide dismutase, however, was without effect. This interaction of Adriamycin with myoglobin may impose significant restrictions on oxygen storage and delivery in vivo. In light of the abundance of myoglobin and the deficiency of catalase in the heart, this interaction with myoglobin may be an important determinant of the cardioselective toxicity of Adriamycin.
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PMID:Adriamycin-induced oxidation of myoglobin. 794 75

Iron deficiency is common in adolescents. This age-group needs more iron owing to the spurt of growth in puberty, and, in girls, because of menstrual losses, and in the event of pregnancy. In boys there is a normal rise in haemoglobin level from about 13 to about 15 g/100 ml, and in myoglobin (muscular mass). Physical training increases the need of iron (21). In addition, poor eating habits are quite common in adolescents. There are few data in the literature on the iron status of Norwegian adolescents, but large studies from USA, Canada and Sweden have disclosed iron depletion (s-ferritin below 16 micrograms/l) with or without anaemia in 40% of adolescent girls and 15% of adolescent boys. Screening, including haemoglobin and s-ferritin determinations, is advocated.
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PMID:[Teenage iron deficiency]. 823 3

It is established that a high-frequency chromosomal deletion of ca. 100 kb accounts for the loss of properties making up the pigmented phenotype (Pgm+) of wild-type Yersinia pestis. These determinants are known to include virulence by peripheral routes of injection, sensitivity to the bacteriocin pesticin, adsorption of exogenous hemin or Congo red at 26 degrees C, and growth in iron-sequestered medium at 37 degrees C. We have now identified the outer membrane as the primary site of exogenous hemin storage in Pgm+ cells grown at 26 degrees C. Significant outer membrane storage of hemin did not occur in Pgm- mutants or in Pgm+ cells cultivated at 37 degrees C. However, both Pgm+ and Pgm- organisms grown at 37 degrees C contained a periplasmic reservoir of hemin, which may be associated with a temperature-dependent ca. 70-kDa peptide recently equated with antigen 5. At 37 degrees C, Pgm+ and Pgm- yersiniae also utilized a cytoplasmic ca. 19-kDa bacterioferritin-like peptide for deposition of inorganic iron. Incorporation of [55Fe]hemin into pools at 37 degrees C was not significantly inhibited by competition with excess unlabeled Fe3+. However, excess unlabeled hemin modestly competed with incorporation of label from 55FeCl3. This relative independence of storage pools observed at 37 degrees C is consistent with physiological linkage to in vivo acquisition and transport of Fe3+ from ferritin and of hemin from hemoglobin, myoglobin, or hemopexin.
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PMID:Storage reservoirs of hemin and inorganic iron in Yersinia pestis. 841 54

High prevalence of anemia and iron deficiency state are found among athletes. To determine the influence of sports activities on the hematological state, we have performed hematological tests and examined the iron metabolism, in addition to some serum enzyme activities and some characters of red blood cells before and after exercise in high school boy athletes. The red blood cell count, hemoglobin level, and hematocrit value were significantly lower than those in the non-athletes boy students. The serum ferritin level in the athletes was significantly lower than that in the control group and healthy adults. Iron deficiency anemia was found in 12% of the athletes. The serum haptoglobin level in the athletes was significantly lower than that in the control group and the level before exercise, suggesting intravascular hemolysis, but the serum hemopexin level showed no difference before and after exercise, suggesting that the hemolysis was not so severe. The serum CPK and myoglobin levels showed a significant increase after exercise, but those levels were quite lower than that of muscle diseases. These findings suggest that daily exercise is closely associated with the increased risk of iron deficiency state, particularly in the high school boy athletes. The mechanism of hemolysis in athletes may partly depend on the increased fragility of iron deficiency red blood cells on mechanical strength.
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PMID:[Sport-anemia: studies on hematological status in high school boy athletes]. 874 90

A density gradient electrophoresis apparatus made of Perspex (7 cm, O 2.2 cm) with a circular platinum anode and a palladium cathode was used for the separation of proteins in free liquid. Following a concept developed by M. Bier et al. (Electrophoresis 1993, 14, 1011-1018), mixtures of two suitable amphoteric buffers I and II provide for media with a fixed and electrophoretically stable pH or were used for the generation of preformed (electrophoretically stable) pH gradients covering about 1 pH unit. Amphoters I and II are considered suitable if there is overlap between (pK(1,1)-1-2) and the pK(2,II)+1+2) region. 3-(N-Morpholino)propanesulfonic acid (MOPS) and gamma-amino-n-butyric acid (GABA) were used as an example. Two approaches were followed: (i) rate-zonal separation of test proteins in a pH window, formed by a fixed ratio of MOPS/GABA. (ii) Isoelectric focusing in a shallow preformed pH gradient, made up of inverse reciprocal linear gradients of MOPS and GABA. At isopH, test proteins (bovine serum albumin, cytochrome c, ferritin, hemoglobin, lactoglobulin, myoglobin, and transferrin) were rate-zonally separated within a short time. Even the separation of the A and B forms of lactoglobulin was feasible at isopH. The glycoforms of transferrin were separated and enriched on a pH 5.2-6.1 pH gradient, indicating that pH differences of about 0.01 still permit resolution. Contrary to the ill-defined Ampholines, the cost of these well-defined amphoters is low.
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PMID:Density gradient isoelectric focusing of proteins in artificial pH gradients made up of binary mixtures of amphoteric buffers. 919 4

Heme oxygenase (HO) proteins are members of the HSP30 family and consist of 2 isozymes identified to date, termed HO-1 and HO-2. Separate genes encode the isozymes and protein products which are immunochemically distinct, share less than 50% similarity at the amino acid sequence level. Each form, however, shows greater than 90% similarity among species, including human and the rat (reviewed in ref.). Furthermore, these isozymes function in a well-defined role to carry out oxidation of the heme molecule (Fe-protoporphyrin IX) in concert with NADPH-cytochrome P450 reductase. The oxidation of heme is isomer specific and results in the formation of bile pigments, carbon monoxide, and iron. The heme molecule constitutes the prosthetic moiety of hemoproteins, such as hemoglobin, myoglobin, catalase, soluble guanylate cyclase, cytochrome b5, cytochromes P450 and NO synthase. HO-1 also known as heat shock protein (HSP) 32 is encoded by a gene which is exquisitely stress-responsive and a host of stimuli that mediate oxidative stress cause induction of the protein both in vivo and in vitro. The HO-2 form shows a unique pattern of regulation from that of HO-1. HO-2 is a constitutive protein and its expression is not affected by the inducers of HO-1 tested to date; rather, the only known regulator of HO-2 yet identified is adrenal glucocorticoids. The two isozymes display vast differences in tissue distribution and under normal conditions HO-1 is present in the whole brain at the limit of immunodetection and is discreetly localized in select neuronal populations. HO-1 protein (approximately 32 kDa) and its approximately 1.8 kb transcript are increased, however, in response to stressful stimuli primarily in non-neuronal cell populations. The heme oxygenase system serves in both a catabolic and anabolic capacity in the cell. In the former capacity, it down-regulates cellular heme and hemoprotein levels. And, as such it inactivates the most effective catalyst for formation of free radicals, the heme molecule. In its anabolic role, as noted above, heme oxygenase produces bile pigments, carbon monoxide, and iron, all of which are biologically active: bile pigments function as antioxidants; the carbon monoxide generated by HO activity has been correlated with the generation of cGMP; and iron regulates expression of various genes, including that of HO-1 itself, as well as transferrin receptors, ferritin, and NO synthase. We used rabbit anti-rat HO-2 polyclonal antibody and HO-2 cDNA to localize HO-2 immunoreactive protein and the 1.3- and 1.9 kb homologous transcripts, respectively, in rodent brain as visualized by histochemical staining procedures. These protocols provide the first detailed description of methodologies successfully used to define the pattern of HO-2 expression at the transcriptional and translational levels in the adult rat brain and glucocorticoid-treated newborn rats. The procedures described herein have the virtue of being non-radioactive, as well as applicability to the systemic organs, such as the cardiovascular system and the male reproductive organs. Visualization of cellular HO-2 expression aids in assessment of potential sites of carbon monoxide, iron, and bilirubin production within the nervous system.
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PMID:Histochemical localization of heme oxygenase-2 protein and mRNA expression in rat brain. 938 81

Under iron-restricted conditions staphylococcal strains could utilize in vitro several animals body iron sources in form of bovine haemoglobin, hemin, lactoferrin and transferrin, ovotransferrin, horse myoglobin ferritin and cytochrome C. Spectrum of utilized iron sources was not dependent on species affiliation and kind of siderophores system. Strains isolated from clinical materials utilized largest spectrum of animal iron body sources.
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PMID:[Animal systemic iron sources utilized in vitro by staphylococci]. 941 Oct 71

Free radical species have been implicated as important agents involved in myocardial ischemic and reperfusion injuries. Superoxide is capable of mobilizing iron from ferritin and the released iron can cause hydroxyl formation from H2O2. The aim of this study was to evaluate the time-dependent increase in lipid peroxidation assessed by plasma thiobarbituric acid reactive substances (TBARS) and the relationship between lipid-peroxidation and the iron status. Peripheral venous blood samples were obtained from 17 men with acute myocardial infarction (AMI) before thrombolytic treatment (T0) and 1, 2, 3, 4, 8, 12, 16, 20, 24 and 48 hours after commencing fibrinolytic treatment. The concentration of TBARS, the parameters of iron metabolism, serum myoglobin, creatine kinase, and creatine kinase-MB were measured. Early reperfusion was judged by regression of sinus tachycardia (ST) elevation and reduction of chest pain. Recanalization of coronary artery was evaluated by a late coronary angiography 24-96 hours after thrombolysis. After thrombolytic therapy, the TBARS level was raised from 2.98 +/- 0.80 (T0) to 4.57 +/- 1.24 (peak), and decreased to 2.96 +/- 0.40 nmol/mL plasma at T48 (T0 vs peak: P < 0.001, peak vs T48: P < 0.001, T0 vs T48: NS). The mean time of the peak was observed at 9.7 +/- 7.5 hours. The iron increased significantly from 0.67 +/- 0.34 (T0) to 1.15 +/- 0.52 mg/L (peak), and returned to the pre-reperfusion to levels: 0.53 +/- 0.28 UI/L at T48 (TO vs peak: P < 0.001, peak vs T48: P < 0.001, T0 vs T48: NS). The mean time of the peak was observed at 9.4 +/- 7.3 hours. In return, no correlation was found between the increase of plasma creatine-kinase activity, myoglobin and iron or between the biochemical markers and time of fibrinolytic therapy. The results confirmed the importance of the temporal relationship between lipid peroxidation and iron status after thrombolytic therapy. Our results are in agreement with the concept that antioxidant agents used in association with thrombolytic therapy might be useful.
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PMID:Plasma iron status and lipid peroxidation following thrombolytic therapy for acute myocardial infarction. 956 80

Using the manipulation force microscope, a novel atomic force microscope, the adhesion forces of bovine serum albumin, myoglobin, ferritin, and lysozyme proteins to glass and polystyrene substrates were characterized by following the force necessary to displace an adsorbed protein-covered microsphere over several orders of magnitude in time. This force was consistent with a power law with exponent a = 0.37 +/- 0.03 on polystyrene, indicating that there is no typical time scale for adhesion on this substrate. On glass, the rate of adhesion depended strongly on protein charge. Forces corresponding to single protein adhesion events were identified. The typical rupture force of a single lysozyme, ferritin, bovine serum albumin, and myoglobin protein adhering to glass was estimated to be 90 +/- 10 pN, 115 +/- 13 pN, 277 +/- 44 pN, and 277 +/- 44 pN, respectively, using a model of the experimental system. These forces, as well as the force amplitudes on hydrophobic polystyrene, correlate with protein stiffness.
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PMID:Protein adhesion force dynamics and single adhesion events. 1038 77


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