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

The presence of two electrophoretically and structurally distinguishable forms of ferritin ("fast" and "slow") in cardiac and skeletal muscle (diaphragm) of the rat was confirmed. Although the total amount of cardiac ferritin showed no difference in concentration in male and female rats, the distribution between the fast and slow species was markedly different in the two sexes, the fast form predominating in the cardiac muscle and diaphragm of the female. In agreement with this, the rates of synthesis and of degradation of the fast species were greater in the female, while the opposite obtained for the male. Iron administration stimulated synthesis of each ferritin species in the cardiac muscle and diaphragm of both sexes. Induction of cardiac connective tissue hypertrophy with isoproterenol inverted the ratio of slow to fast ferritin in female rats, while iron administration along with isoproterenol restored this to normal. It is concluded that the metabolism of ferritin in cardiac and skeletal muscle is sensitive both to sexual status and to iron administration.
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PMID:Sex difference in distribution and iron responsiveness of the two ferritins of rat cardiac and skeletal muscle. 84 83

Studies with extracellular fine structural diffusion protein tracers, horseradish peroxidase and ferritin, were carried out on catecholamine-induced cardiac muscle cell injury. Epinephrine, norepinephrine, and isoproterenol were administered in a dose of 4- 6 mug/100g body weight by continuous intravenous infusion. For follow-up studies, isoproterenol was also given subcutaneously in a dose of 8.5 mg/100 g body weight as a single injection. In contrast to saline-infused controls and following epinephrine infusion, where these tracers always remained extracellular, norepinephrine- and isoproterenol-infused animals exhibited alteration of sarcoplasmic membrane permeability to macromolecules in the early stage of evolution preceding fine structural changes of cardiac muscle cells. This was reflected by the intrasarcoplasmic presence of peroxidase in some cardiac muscle cells which otherwise showed no ultrastructural alteration. Deposition upon and selective binding of the extracellular protein tracer, peroxidase, to intact myofilament was also a characteristic early change that may affect the contraction-relaxation mechanism of the myofilaments and may contribute to the evolution of necrobiotic alteration. In structurally altered cells, peroxidase showed similar affinity to contraction bands and fragmented myofilaments. Furthermore, these studies disclosed different sensitivities of various membrane components of the cardiac muscle cell. While in the early pahse of cell damage no peroxidase could be detected in various intrasarcoplasmic compartments, with increasing severity of the lesion the external and internal mitochondrial membranes as well as the sarcoplasmic reticulum were also affected. When the large molecular tracer, ferritin, was used, the sequence of events in altered cardiac muscle cells followed that outlined for peroxidase. However, free ferritin molecules could not be demonstrated in the sarcoplasm of cardiac muscle cells which exhibited normal ultrastructure.
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PMID:Membrane permeability alterations as manifestation of early cardiac muscle cell injury. 119 96

The exchange area of the submandibular salivary gland microvasculature has been measured to allow the value of microvascular permeability (P) to hydrophilic solutes to be calculated from previous measurements of permeability-surface area (PS) products. Glands whose ducts had been ligated for 2 weeks and the contralateral control glands were perfusion-fixed with a modified Karnovsky's fixative after perfusion with a solution containing cationized ferritin, and examined with transmission electron microscopy. Stereological techniques were used to estimate the surface area of the exchange vessels on random thin sections from four control and four duct-ligated glands. The mean exchange surface area in control glands was 512 cm2 g-1 and 336 cm2 g-1 in duct-ligated glands. The fenestral density was calculated to be 0.57% of the exchange surface in control glands and 0.30% in duct-ligated tissue. Molecules of cationized ferritin appeared bound to the luminal surface of the microvascular endothelium, including the surface of the fenestrae to a depth of about 25 nm in both control and ligated glands. These experiments have shown that the exchange surface area of the fenestrated endothelium of the submandibular salivary gland is comparable to that in cardiac muscle but the permeability (P) to small solutes is about 10 times greater. Following ligation of the salivary gland duct, solute permeability falls and an explanation of this, based on the reduced surface area and the nature of the permeability-flow relationship for small solutes is offered.
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PMID:Exchange area and surface properties of the microvasculature of the rabbit submandibular gland following duct ligation. 648 42

Compartmentalization of cellular amino acid pools occurs in cultures of cardiac and skeletal muscle cells, but the factors involved in this are not clear. We have further defined this problem by analyzing the intracellular free leucine and the transfer-RNA-(tRNA)-bound leucine pool in cultures of skeletal and cardiac muscle incubated with 3H-leucine in the presence and absence of serum and amino acids. Withdrawal of nitrogen substrates caused substantial changes in leucine pool relationships--in particular, a change in the degree to which intracellular free leucine and tRNA-leucine were derived from the culture medium. In separate experiments, the validity of our tRNA measurements was confirmed by measurements of the specific activity of newly synthesized ferritin after iron induction. We discuss the implications of these findings with regard to factors involved in the control of amino acid flux through the cell, as well as with regard to design of experiments using isotopic amino acids to measure rates of amino acid utilization.
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PMID:Amino acid pools in cultured muscle cells. 656 76

The ultrastructural localization of alpha-actinin and vinculin in chicken cardiac muscle was studied by double indirect immunoelectron microscopy, using ferritin and iron-dextran (Imposil) as the electron-dense markers conjugated to the secondary antibodies, on ultrathin frozen sections of fixed tissue. Fixation and immunolabeling procedures were developed that permitted maximal retention of the two proteins at their natural sites as well as their adequate labeling. alpha-Actinin was found both on the Z-bands, as expected, and near the fascia adherens of the intercalated discs, whereas vinculin was confined to the latter sites. At the fascia adherens, the double labeling results clearly showed that vinculin was situated closer to the membrane than was alpha-actinin. These results, coupled with earlier observations, suggest that vinculin may participate in the linkage of actin-containing microfilament bundles to membranes in a variety of cell types.
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PMID:Ultrastructure of chicken cardiac muscle as studied by double immunolabeling in electron microscopy. 680 54

Autopsy studies of two infants, one a newborn, the other 4 months old, revealed massive amounts of iron in lysosomes of hepatocytes and pancreatic acinar cells. Iron, which had been transported across the placenta, accumulated in the same cell types as in adults with primary and secondary hemochromatosis. Hemosiderin was found in cardiac muscle cells, gastric and intestinal glands, and endocrine and exocrine organs including pituitary, thyroid, adrenals, islets of Langerhans, and sublingual and sweat glands. The liver was the most affected organ and the normal hepatic architecture was replaced by hepatocytes which were arranged in cluster, pseudoacinar structures, and multinucleated giant cells embedded in a collagen matrix. The islets of Langerhans were hyperplastic and hypertrophic. Ten similar cases, in five families, have been described; no patients liver longer than 4 months. Neonatal iron storage disease is clinically and pathologically distinct from Zellweger's cerebrohepatorenal syndrome and hypermethioninemia (tyrosinemia) neonatal diseases in which large stores of iron are present in hepatocytes. No abnormalities in serum iron, ferritin, or transferrin concentrations were detected in five parents of the affected children.
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PMID:Idiopathic neonatal iron storage involving the liver, pancreas, heart, and endocrine and exocrine glands. 728 89

Hemoglobin concentration, iron parameters and cardiac status of 25 patients with beta thalassemia/hemoglobin E disease were measured. Two-dimensional echocardiography was employed to evaluate chamber size, ejection fraction and muscle fiber shortening. The seventeen patients who had a mean hemoglobin concentration of less than 7.7 g/dl were found to have significantly larger cardiac chambers and higher cardiac output than the patients with higher hemoglobin concentrations. A statistically significant difference in ejection fraction and per cent of fractional shortening of cardiac muscle fibers was not found. A comparison of subjects with ferritin concentrations above and below 1,500 micrograms/L showed no significant difference in chamber sizes, ejection fraction and in per cent fractional shortening. However, a comparison of 14 patients with transferrin saturation > or = 80 per cent with those less than 80 per cent showed a significant decrease in both ejection fraction and fiber fractional shortening in the more highly saturated subjects. By using stepwise multiple regression analysis, the hemoglobin level was shown to significantly determine cardiac enlargement, while ejection fraction and percentage fractional shortening were significantly associated with transferrin-iron saturation. Thus, anemia leads to chamber enlargement, while high transferrin iron saturation is associated with cardiac muscle dysfunction. The findings in the individual patient reflect the integration of these two effects.
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PMID:Echocardiographic features in patients with beta thalassemia/hemoglobin E: a combining effect of anemia and iron load. 779 36

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

This review accounts for the current development in microfluidic immunosensing chips. The basic knowledge of immunoassay in relation to its microfluidic material substrate, fluid handling and detection mode are briefly discussed. Here, we mainly focused on the surface modification, antibody immobilization, detection, signal enhancement and multiple analyte sensing. Some of the clinically important currently implemented on the microfluidic immunoassay chips are C-reactive protein (CRP), prostate specific antigen (PSA), ferritin, vascular endothelial growth factor (VEGF), myoglobin (Myo), cardiac troponin T (cTnT), cardiac troponin I (cTnI), and creatine kinase-cardiac muscle isoform (CK-MB). The emerging microfludic immunosensor technology may be a promising prospect that can propel the improvement of clinical and medical diagnosis.
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PMID:Current development in microfluidic immunosensing chip. 1829 63

Progressive oxidation of cellular components constitutes a major mechanism of the aging process. An emerging paradigm of redox signaling suggests that low level oxidants activate protective pathways resulting in prolonged cell survival. This report centers on the study of cardiac muscle in young and old rats, including (i) the expression of ferritin (Ft) the major iron storage protein, and (ii) the expression of the major proteins of the methionine-centered redox cycle (MCRC), which controls the cellular methionine redox status. Total amounts of Ft (protein) and its mRNA encoding for Ft L-subunit (Ft-L) were higher in the aged hearts, indicating that the iron-binding capacity of myocardial Ft increased with age. Among the proteins of the MCRC, methionine sulfoxide reductases A and B (MsrA, MsrB) and MsrA mRNA were significantly higher in hearts of old rats with a significant decrease in MsrA activity. The observed up-regulation of the expression of Msr and Ft-L could represent a protective response to the increased oxidative stress in the aging myocardium.
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PMID:Iron, ferritin and proteins of the methionine-centered redox cycle in young and old rat hearts. 1899 41


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