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)

Stimulation of the immune system results in a series of metabolic changes that are antagonistic toward growth. Monokines, including interleukin-1, tumor necrosis factor, and interleukin-6, are released from cells of the monocyte-macrophage lineage after recognition of immunogens. They appear to mediate homeorhetic response, which alters the partitioning of dietary nutrients away from growth and skeletal muscle accretion in favor of metabolic processes which support the immune response and disease resistance. These alterations include 1) decreased skeletal muscle accretion due to increased rates of protein degradation and decreased protein synthesis; 2) increased basal metabolic rate resulting in increased energy utilization; 3) use of dietary amino acids for gluconeogenesis and as an energy source instead of for muscle protein accretion; 4) synthesis by the liver of acute phase proteins; 5) redistribution of iron, zinc, and copper within the body due to the hepatic synthesis of metallothionein, ferritin, and ceruloplasmin; (6) impaired accretion of cartilage and bone; and 7) release of hormones such as insulin, glucagon, and corticosterone. These monokines also influence the differentiation of cells. Tumor necrosis factor suppresses the differentiation of myoblasts and adipocytes whereas the chicken monokine myelomonocytic growth factor induces the differentiation of granulocytes.
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PMID:Monokines in growth and development. 171 68

Plasma zinc, iron, copper, and selenium and selected blood proteins were measured in 66 men before (BHW) and after (AHW) a 5-d period of sustained physical and psychological stress called Hell Week. Recovery blood samples were obtained from 26 men 7 d after Hell Week. Dietary intakes were determined BHW and during Hell Week; zinc, iron, copper, and selenium intakes during Hell Week averaged 23.6 +/- 3.4 mg/d, 35.4 +/- 3.9 mg/d, 3.0 +/- 0.5 mg/d, and 92.5 +/- 26.7 micrograms/d, respectively. C-reactive protein was detected in only five subjects BHW and in all subjects AHW. Zinc, iron, selenium, and albumin decreased by 33%, 44%, 12%, and 9%, respectively, whereas ferritin, ceruloplasmin, and creatine kinase concentrations increased AHW by 59%, 8%, and 266%, respectively. Haptoglobin concentrations increased 57% in 30 subjects but decreased 32% in 23 subjects AHW. The biochemical changes were transitory because protein (except ferritin) and mineral concentrations were similar to BHW values 7 d after Hell Week. Hell Week induced changes characteristic of an acute-phase response in physically active men.
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PMID:Biochemical indices of selected trace minerals in men: effect of stress. 198 37

Using stored serum samples collected during from 1970 to 1972 and/or 1977 to 1979 from a fixed population in Hiroshima and Nagasaki, Japan, serum ferritin, transferrin, and ceruloplasmin levels were determined immunologically for persons in whom stomach (233 cases) or lung cancer (84 cases) subsequently developed as well as for their controls. An elevated stomach cancer risk was associated with low antecedent serum ferritin levels, with more than a threefold excess among those in the lowest compared with the highest ferritin quintile. The risk did not vary with the time between blood collection and stomach cancer onset, remaining high among those with low ferritin levels 5 or more years before cancer diagnosis. Achlorhydria, diagnosed in a sample of the population about 10 years before the 1970-to-1972 blood collection and up to 25 years before cancer, was an independent marker of stomach cancer risk. In combination, low serum ferritin and achlorhydria were associated with a tenfold increase in the subsequent risk. No effect of transferrin or ceruloplasmin, independent of ferritin, was observed in the gastric cancer risk, and the risk of lung cancer was not related to these three serum proteins. These prospective findings indicate that biologic markers of an increased risk of stomach cancer can be detected long before cancer onset.
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PMID:Serum ferritin and stomach cancer risk among a Japanese population. 200 62

The copper binding tripeptide, glycyl-L-histidyl-L-lysine [GHK:Cu(II)] has a plethora of biological effects related to the wound healing process. The presence of iron complexes in damaged tissues is detrimental to wound healing, due to local inflammation, as well as microbial infection mediated by iron. To test if the wound healing properties of GHK:Cu(II) are due to an affect on iron metabolism, we examined the effects of GHK:Cu(II) on iron catalyzed lipid peroxidation. GHK:Cu(II) inhibited lipid peroxidation only if the iron source was ferritin. Whereas GHK:Cu(II) inhibited ferritin iron release it did not exhibit significant superoxide dismutase-like or ceruloplasmin-like activity. We propose that GHK:Cu(II) binds to the channels of ferritin involved in iron release and physically prevents the release of Fe(II). Thus, a biological effect of GHK:Cu(II), possibly related to wound healing, may be the inhibition of ferritin iron release in damaged tissues, preventing inflammation and microbial infections.
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PMID:Effects of glycyl-histidyl-lysyl chelated Cu(II) on ferritin dependent lipid peroxidation. 224 43

In unseparated human blood the reactivity of yeast copper (I)-thionein on TPA-activated polymorphonuclear leukocytes was evaluated and compared with low Mr copper chelates exerting Cu2Zn2 superoxide dismutase mimetic activity. Cu, 18 microM, in the form of Cu-thionein was sufficient to inhibit the superoxide production of activated human blood phagocytes by 50%. Furthermore, the scavenging of hydroxyl radicals and singlet oxygen by Cu(I)-thionein was determined, using the 2-deoxyribose fragmentation assay induced by decaying K3CrO8 and the NADPH oxidation caused by UVA illuminated psoralen, respectively. The inhibitory reactivity of Cu-thionein in both assays was compared with that of serum proteins including albumin, ceruloplasmin, transferrin, and ferritin. The galactosamine/endotoxin-induced hepatitis in male NMRI mice was used to evaluate the antiinflammatory reactivity of Cu-thionein in vivo. The serum copper, superoxide dismutase, and sorbitol dehydrogenase concentrations, as well as the activity of polymorphonuclear leukocytes in unseparated blood seemed most appropriate to quantify the protective capacity of Cu-thionein in the course of an oxidative stress-dependent liver injury. The intraperitoneal application of 32.5 mumols/kg thionein-Cu limited this damage to 45%.
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PMID:Antiinflammatory reactivity of copper(I)-thionein. 224 84

Eleven potential biochemical markers were measured in serum from 33 patients with malignant and 13 with benign colorectal disease: four isoenzymes (creatine kinase-BB, homoarginine-sensitive alkaline phosphatase, salivary-type amylase, and macro-creatine kinase type 2), five specific proteins (ferritin, alpha 1-acid glycoprotein, C-reactive protein, alpha 1-antitrypsin, and ceruloplasmin), one oncofetal antigen (carcinoembryonic antigen, CEA), and one hormone (beta human choriogonadotropin). The sensitivity of individual markers for the detection of early-stage malignancy (n = 11) ranged from 0% to 64% (CEA 18%); for late-stage colon malignancy (n = 12) from 8% to 83% (CEA 83%). Specificity in patients (n = 10) with benign intestinal disease ranged from 80% to 100% (CEA 100%). The five most-sensitive markers--C-reactive protein, alpha 1-glycoprotein, CEA, macrocreatine kinase type 2, and homoarginine-sensitive alkaline phosphatase--were selected for use as a "colon panel." In retrospective comparison, use of the colon panel instead of CEA alone increased sensitivity by 17% and 64% for late-and early-stage cancer, respectively; specificity, however, decreased by 30%, but should improve with serial testing.
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PMID:Multiple markers of malignancy in sera of patients with colorectal carcinoma: preliminary clinical studies. 241 37

Two-wk-old broiler chicks were inoculated via crop intubation with Eimeria acervulina at two doses: 10(5) or 10(6) sporulated oocysts/bird or with Eimeria tenella at a dose of 10(5) sporulated oocysts/bird. Serum and liver samples were collected on days 3 and 6 post-inoculation (PI). There were no significant changes in serum or liver zinc, copper, and iron concentrations in any of the infected groups by 3 d PI. However, on d 6, PI serum protein was significantly reduced in all of the infected groups compared to their pair-fed controls. The chicks infected with E. tenella had significantly reduced serum zinc (1.20 vs 1.77 micrograms/mL) and iron (0.44 vs 1.28 micrograms/mL) concentrations and significantly elevated serum copper (0.28 vs 0.17 micrograms/mL) and ceruloplasmin levels (20.33 vs 11.11 micrograms/mL) compared to their pair-fed counterparts. Those chicks infected with E. acervulina (10(6) oocysts/bird) exhibited significantly reduced serum iron concentration by 6 days PI (0.90 vs 1.14 micrograms/mL). Liver zinc was significantly increased in the chicks infected with E. tenella (349 vs 113 micrograms/g dry liver wt), as was copper (24 vs 19 micrograms/g), whereas liver iron concentration was significantly reduced (172 vs 243 micrograms/g) compared to pair-fed controls. At both dose levels, the chicks infected with E. acervulina exhibited a significant reduction in liver iron by 6 d PI. Hepatic cytosol metals generally reflected whole tissue levels. Metallothionein (MT)-bound zinc was significantly elevated in the chicks infected with E. tenella. Iron bound to a high molecular weight, heat-stable protein fraction (presumably cytoplasmic ferritin) was significantly reduced in chicks infected with E. acervulina, as well as those infected with E. tenella. Collectively, the changes in serum zinc, copper, and iron concentrations, as well as the changes in hepatic zinc and MT-zinc concentrations in the chicks infected with E. tenella were similar to changes evoked during an acute phase response to infection. It is possible that a secondary bacterial infection or inflammation stemming from erosion of the lining of the cecum may play a role in the response of trace element metabolism to the E. tenella infection.
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PMID:Serum and liver zinc, copper, and iron in chicks infected with Eimeria acervulina or Eimeria tenella. 248 59

5-Hydroperoxymethyl-2'-deoxyuridine (HPMdU) is formed in DNA by ionizing radiation. Although relatively stable, HPMdU eventually decomposes to two products 5-hydroxymethyl-2'-deoxyuridine (HMdU) and 5-formyl-2'-deoxyuridine (FdU). We show that a number of transition metal ions and metalloproteins accelerate this process. Of the metal ions tested, Sn(II) and Fe(II) were the most active, with the former producing exclusively HMdU, and the latter, a mixture of both. Cu(I), Cu(II), Co(II), and Ni(II) induced a predominant generation of FdU, with copper ions being more effective than Co and Ni. FdU was also preferentially formed in the presence of the iron-containing proteins transferrin and ferritin, whereas HMdU was the major product in the presence of apotransferrin as well as in the presence of ceruloplasmin, a copper-containing protein.
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PMID:Decomposition of nucleoside hydroperoxide by metals and metalloproteins. 248 13

The diabetogenic action of alloxan is believed to involve oxygen free radicals and iron. Incubation of glutathione (GSH) and alloxan with rat liver ferritin resulted in release of ferrous iron as assayed by spectrophotometric detection of ferrous-bathophenanthroline complex formation. Neither GSH nor alloxan alone mediated iron release from ferritin. Superoxide dismutase (SOD) and catalase did not affect initial rates of iron release whereas ceruloplasmin was an effective inhibitor of iron release. The reaction of GSH with alloxan resulted in the formation of the alloxan radical which was detected by ESR spectroscopy and by following the increase in absorbance at 310nm. In both instances, the addition of ferritin resulted in diminished alloxan radical detection. Incubation of GSH, alloxan, and ferritin with phospholipid liposomes also resulted in lipid peroxidation. Lipid peroxidation did not occur in the absence of ferritin. The rates of lipid peroxidation were not affected by the addition of SOD or catalase, but were inhibited by ceruloplasmin. These results suggest that the alloxan radical releases iron from ferritin and indicates that ferritin iron may be involved in alloxan-promoted lipid peroxidation.
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PMID:Alloxan- and glutathione-dependent ferritin iron release and lipid peroxidation. 253 98

Total plasma iron turnover in man is about 36 mg/day. Transferrin is the iron transport protein of plasma, which can bind 2 atoms of iron per protein molecule, and which interacts with various cell types to provide them with the iron required for their metabolic and proliferative processes. All tissues contain transferrin receptors on their plasma membrane surfaces, which interact preferentially with diferric transferrin. In erythroid cells as well as certain laboratory cell lines, the removal of iron from transferrin apparently proceeds via the receptor-mediated endocytosis process. Transferrin and its receptor are recycled to the cell surface, whereas the iron remains in the cell. The mode of iron uptake in the hepatocyte, the main iron storage tissue, is less certain. The release of iron by hepatocytes, as well as by the reticuloendothelial cells, apparently proceeds nonspecifically. All tissues contain the iron storage protein ferritin, which stores iron in the ferric state, though iron must be in the ferrous state to enter and exit the ferritin molecule. Cellular cytosol also contains a small-molecular-weight ferrous iron pool, which may interact with protoporphyrin to form heme, and which apparently is the form of iron exported by hepatocytes and macrophages. In plasma, the ferrous iron is converted into the ferric form via the action of ceruloplasmin.
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PMID:Biochemistry of nonheme iron in man. I. Iron proteins and cellular iron metabolism. 266 99


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