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)

Isolated rat liver lysosomes were incubated with [14C]methemoglobin under various conditions. Optimal pH for the in vitro proteolysis was found to be 4-5. To evaluate whether or not degradation of added proteins could be due to enzyme leakage the integrity of the lysosomes was measured. Isolated lysosomes were found to be stable for up to 10 min of incubation at pH 5.5 and for 30 min at pH 7. The degradation of three different proteins (methemoglobin, ovalbumin, and lysozyme) was analyzed. No correlation was detected between rate of breakdown and physical properties of the proteins. Leupeptin, chloroquine, and propylamine inhibited proteolysis of added proteins by 45-65% in both neutral and acid milieu. Possible energy requirement was tested by the addition of Mg2+ and ATP to the incubation medium. A dose-dependent increase in proteolytic rate was found when ATP was added to the lysosomal suspension, a finding most likely due to acidification of the lysosomes and ensuing increased degradation. GTP and ITP were somewhat less effective. The noncleavable ATP analogue 5'-adenylylimidodiphosphate gave no stimulation. The ATP-driven proteolysis was inhibited by ethylmaleimide. Isolated lysosomes were also incubated with ferritin in order to visualize a possible uptake process of a protein in the electron microscope. Following incubation, ferritin particles were seen inside intralysosomal vesicles which appeared to be formed by invagination of the lysosomal membrane, a process designated microautophagy. The results thus support the notion that isolated lysosomes may micropinocytose and degrade exogenously added proteins and that this process is ATP dependent.
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PMID:Uptake--microautophagy--and degradation of exogenous proteins by isolated rat liver lysosomes. Effects of pH, ATP, and inhibitors of proteolysis. 396 51

ATP depletion crenates human red blood cells. With ferritin-avidin (FA) and cationized ferritin (CF) cell surface labeling, it is demonstrated that the discocyte----crenated shape transformation alters the two-dimensional topography of negative charge sites. With restoration of ATP levels, cell shape and charge topography return to normal. Concurrent changes in red cell shape and surface charge topography can be explained by associations between membrane integral proteins and the red cell cytoskeleton.
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PMID:Changes of cell shape and surface charge topography in ATP-depleted human red blood cells. 399 Mar 85

1. The microsome fraction of rat liver has been fractionated and the ability of the fractions to incorporate ribonucleotides into polyribonucleotides has been studied. Activity was found in the rough-surfaced vesicle (light) fraction and in the free-ribosome fraction and this latter activity has been examined. 2. The free-ribosome fraction contains ribosome monomers, dimers and trimers together with some higher oligomers and ferritin. In addition to catalysing the incorporation of ribonucleotides into acid-insoluble material it contains diesterase activity. It catalyses the incorporation of UMP from UTP, but not UDP, AMP from ATP and CMP from CTP into polyribonucleotide material, and for UTP the product appears to be a homopolymer not more than eight units long attached to the ends of primer polyribonucleotide strands. 3. The activity could not be removed from the free-ribosome fraction by washing or by isolation in the presence of ethylenediaminetetra-acetic acid. 4. Partially hydrolysed polyuridylic acid but not polyadenylic acid could serve as a primer for the incorporation of UMP, but some activity was always associated with an endogenous primer. 5. Analysis of RNA extracted from the free-ribosome fraction after incubation with [(3)H]UTP showed the presence of 28s, 18s, 5s and transfer RNA types, but no radioactivity was associated with any of these RNA fractions.
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PMID:Polyribonucleotide synthesis by subfractions of microsomes from rat liver. 497 Dec 86

A newborn female, the second child of consanguineous parents, exhibited general muscle hypotonia, apathy, hepatomegaly and failure to thrive from birth and signs of craniofacial dysmorphia were present. Pipecolic and trihydroxicoprostanoic acid were excreted in the urine and serum transferrin, ferritin and iron were markedly elevated. At the age of 7 weeks the baby died of respiratory insufficiency. Besides malformations of the brain, renal cysts, liver damage with hypoplastic intrahepatic bile ducts and cholestasis, increased storage of iron and cytochemically proven deficiency of peroxisomes in liver and kidney, morphological studied provided evidence of a mitochondrial myopathy in striated muscle with the accumulation of enlarged bizarre mitochondria, showing only minor structural abnormalities. No defects of NADH-reductase, succinate-dehydrogenase or cytochrome-c-oxidase were demonstrated histochemically. Cytochemical-ultrastructural investigation of mitochondrial ATPase revealed activation of the ATP-synthesising enzyme even before the addition of an uncoupler, this indicating loosely coupled oxidative phosphorylation. In addition a high rate of subcellular autophagy with segregation of mitochondria and focal loss of fibrils was present. Muscle damage in Zellweger syndrome appears to be the consequence of complex, interacting metabolic processes. The mitochondrial myopathy thereby induced allows a better understanding of general muscle hypotonia, one of the leading symptoms of this disorder.
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PMID:Mitochondrial myopathy with loosely coupled oxidative phosphorylation in a case of Zellweger syndrome. A cytochemical-ultrastructural study. 614 41

Two different procedures were employed for the isolation of sarcolemma from the rat heart and the membranes were studied with respect to the presence of cell surface material as well as their functional characteristics. Both hypotonic shock-LiBr treatment method (fraction HL) and sucrose density gradient method (fraction S) yielded membranes enriched 8 to 13 fold with respect to Na+-K+ ATPase and adenylate cyclase activities in comparison to heart homogenate. Cell surface material was demonstrated on the outer surface of the vesicles only in fraction HL with cationic dyes, lanthanum and ferritin, applied either to the isolated fractions or perfused in the heart through coronaries. Fraction HL also had high sialic acid content. ATP independent Ca2+ binding in fraction HL was about 6 times more than that in fraction S which had little sialic acid and showed no cell surface staining with cationic dyes. On the other hand, ATP-dependent Ca2+ binding and Ca2+-stimulated Mg2+ dependent ATPase activities in fraction S were 4 to 6 times higher than those in fraction HL. Epinephrine stimulated adenylate cyclase in fractions HL and S by 24 and 3% whereas ouabain was found to inhibit Na+-K+ ATPase in these fractions by 80 and 10% respectively. A mild treatment of the membranes with deoxycholate to eliminate the semipermeable characteristics or effects of sidedness of the vesicles resulted in an almost complete ouabain inhibition of Na+-K+ ATPase in both fractions. These data suggest that presence of cell surface material as well as membrane sidedness has an important role in in vitro expression of functional characteristics of sarcolemma. It is emphasized that sarcolemmal preparations containing cell surface material will provide information more realistic to the native conditions in situ.
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PMID:Differences in sarcolemmal preparations: cell surface material and membrane sidedness. 619 85

We have studied iron transfer from transferrin to ferritin in the presence of ATP, GTP, ADP, AMP and 2,3-diphosphoglycerate. These compounds, with the exception of AMP, can release iron from transferrin at pH 7.4 and form a stable Fe(III)-phosphate complex. From these complexes, only a limited number of Fe(III) atoms can be incorporated into ferritin. Ascorbate enhances iron transfer from transferrin to ferritin at the beginning of the process but subsequently inhibits further iron deposition in ferritin.
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PMID:Iron transfer form transferrin to ferritin mediated by polyphosphate compounds. 627 Dec 55

Cell-specific differences occur in the primary structure of ferritin. For example, red cell and liver ferritin from bullfrog tadpoles differ by 1.5 times in serine content. To determine if cell-specific differences in ferritin primary structure are expressed in the tetraeicosomer, which thus might distinguish the proteins in a functional state, phosphorylation in vitro was employed as a probe using [gamma-32P]ATP and the catalytic subunit from the cAMP-dependent protein kinase of bovine skeletal muscle. Subunits of both proteins in the tetraeicosomers were phosphorylated. Based on tryptic peptide maps, five regions common to both red cell and liver apoferritin were phosphorylated, as confirmed for two peptides by amino acid analyses. [32P]Apoferritin from red cells yielded an additional four 32P-fragments by mapping, at least three of which were unique by amino acid analysis and, in one case, might represent a 32P-Fe complex bound by a fragment of the iron-binding site. One peptide appeared to be unique to liver apoferritin. High concentrations of ATP yielded one additional peptide common to liver and red cell and one red cell-specific peptide in the tryptic peptide maps. The maximum moles of 32P/molecule were 13 +/- 4 and 6 +/- 2, respectively, for red cell and liver apoferritin, which corresponded within experimental error to the number of 32P-tryptic peptides. The level of phosphorylation was, on the average, not more than one site/subunit. Furthermore, above certain levels of phosphorylation, some subunits in the assemblage of 24 appeared to be unavailable as substrates, possibly because of charge repulsion or conformational changes. The possibility that post-translational modifications of ferritin which amplify cell-specific structural features occur in vivo with cytoplasmic components, e.g. protein kinases, is considered in terms of the physiological availability of iron from different iron storage cells and developmental changes in iron storage.
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PMID:Cell-specific properties of red cell and liver ferritin from bullfrog tadpoles probed by phosphorylation in vitro. 660 21

The binding of gallium 67 or iron 59 to ferritin in vitro was investigated using equilibrium dialysis. Gallium 67 did not bind to apo-ferritin until the protein was transformed into ferritin in the presence of iron citrate. Apotransferrin inhibited the binding of 67Ga to ferritin, especially in the presence of sodium bicarbonate and citrate, thus indicating that 67Ga has not gained access to ferritin from its complex with transferrin. Similar inhibition was observed for ferritin-59Fe. The release of 59Fe from its transferrin complex was enhanced by ATP, citrate, or ascorbic acid, while these reagents did not stimulate the dissociation of 67Ga from its transferrin complex. On the other hand, 67Ga injected intravenously in vivo was not found in the ferritin fractions of rat liver, kidney, and tumor. The difference between experimental results in vivo and in vitro supports the hypothesis that 67Ga in the cytoplasm is not labile enough to be bound to ferritin. We have indicated a significant role of ferritin in distinguishing between 67Ga and 59Fe in the cell, and provided some clues to interpret the chemical forms of 67Ga in the cytoplasm.
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PMID:The role of ferritin in the intracellular distribution of gallium 67. 673 67

Terminal webs prepared from mouse intestinal epithelial cells were examined by the quick-freeze, deep-etch, and rotary-replication method. The microvilli of these cells contain actin filaments that extend into the terminal web in compact bundles. Within the terminal web these bundles remain compact; few filaments are separated from the bundles and fewer still bend towards the lateral margins of the cell. Decoration with subfragment 1 (S1) of myosin confirmed that relatively few actin filaments travel horizontally in the web. Instead, between actin bundles there are complicated networks of the fibrils. Here we present two lines of evidence which suggest that myosin is one of the major cross-linkers in the terminal web. First, when brush borders are exposed to 1 mM ATP in 0.3 M KCl, they lose their normal ability to bind antimyosin antibodies as judged by immunofluorescence, and they lose the thin fibrils normally found in deep-etch replicas. Correspondingly, myosin is released into the supernatant as judged by SDS gel electrophoresis. Second, electron microscope immunocytochemistry with antimyosin antibodies followed by ferritin-conjugated second antibodies leads to ferritin deposition mainly on the fibrils at the basal part of rootlets. Deep-etching also reveals that the actin filament bundles are connected to intermediate filaments by another population of cross-linkers that are not extracted by ATP in 0.3 M KCl. From these results we conclude that myosin in the intestinal cell may not only be involved in a short range sliding-filament type of motility, but may also play a purely structural role as a long range cross-linker between microvillar rootlets.
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PMID:Organization of actin, myosin, and intermediate filaments in the brush border of intestinal epithelial cells. 720 10

There are several inherited and acquired disorders that can result in chronic iron overload in humans, and the major clinical consequences are hepatic fibrosis, cirrhosis, hepatocellular cancer, cardiac disease, and diabetes. It is clear that lipid peroxidation occurs in experimental iron overload if sufficiently high levels of iron within hepatocytes are achieved. Lipid peroxidation is associated with hepatic mitochondrial and microsomal dysfunction in experimental iron overload, and lipid peroxidation may underlie the increased lysosomal fragility that has been detected in liver samples from both iron-loaded human subjects and experimental animals. Reduced cellular ATP levels, impaired cellular calcium homeostasis, and damage to DNA may all contribute to hepatocellular injury in iron overload. Long-term dietary iron overload in rats can lead to increased collagen gene expression and hepatic fibrosis, perhaps due to activation of hepatic lipocytes. The mechanisms whereby lipocytes are activated in iron overload remain to be elucidated; possible mediators include aldehydic products of iron-induced lipid peroxidation produced in hepatocytes, tissue ferritin, and/or cytokines released by activated Kupffer cells.
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PMID:Pathophysiology of iron toxicity. 788 29


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